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1

Brechtel, Elke, and Hubert Bahl. "In Thermoanaerobacterium thermosulfurigenes EM1 S-Layer Homology Domains Do Not Attach to Peptidoglycan." Journal of Bacteriology 181, no. 16 (August 15, 1999): 5017–23. http://dx.doi.org/10.1128/jb.181.16.5017-5023.1999.

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ABSTRACT Three exocellular enzymes of Thermoanaerobacterium thermosulfurigenes EM1 possess a C-terminal triplicated sequence related to a domain of bacterial cell surface proteins (S-layer proteins). At least one copy of this sequence, named the SLH (for S-layer homology) domain, is also present at the N terminus of the S-layer protein of this bacterium. The hypothesis that SLH domains serve to anchor proteins to the cell surface was investigated by using the SLH domain-containing xylanase. This enzyme was isolated fromT. thermosulfurigenes EM1, and different forms with and without SLH domains were synthesized in Escherichia coli. The interaction of these proteins with isolated components of the cell envelope was determined to identify the attachment site in the cell wall. In addition, a polypeptide consisting of three SLH domains and the N terminus of the S-layer protein of T. thermosulfurigenes EM1 were included in these studies. The results indicate that SLH domains are necessary for the attachment of these proteins to peptidoglycan-containing sacculi. Extraction of the native sacculi with hydrofluoric acid led to the conclusion that not peptidoglycan but accessory cell wall polymers function as the adhesion component in the cell wall. Our results provide further evidence that attachment of proteins via their SLH domains represents an additional mode to display polypeptides on the cell surfaces of bacteria.
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2

Ozdemir, Inci, Sara E. Blumer-Schuette, and Robert M. Kelly. "S-Layer Homology Domain Proteins Csac_0678 and Csac_2722 Are Implicated in Plant Polysaccharide Deconstruction by the Extremely Thermophilic Bacterium Caldicellulosiruptor saccharolyticus." Applied and Environmental Microbiology 78, no. 3 (December 2, 2011): 768–77. http://dx.doi.org/10.1128/aem.07031-11.

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ABSTRACTThe genusCaldicellulosiruptorcontains extremely thermophilic bacteria that grow on plant polysaccharides. The genomes ofCaldicellulosiruptorspecies reveal certain surface layer homology (SLH) domain proteins that have distinguishing features, pointing to a role in lignocellulose deconstruction. Two of these proteins inCaldicellulosiruptor saccharolyticus(Csac_0678 and Csac_2722) were examined from this perspective. In addition to three contiguous SLH domains, the Csac_0678 gene encodes a glycoside hydrolase family 5 (GH5) catalytic domain and a family 28 carbohydrate-binding module (CBM); orthologs to Csac_0678 could be identified in all genome-sequencedCaldicellulosiruptorspecies. Recombinant Csac_0678 was optimally active at 75°C and pH 5.0, exhibiting both endoglucanase and xylanase activities. SLH domain removal did not impact Csac_0678 GH activity, but deletion of the CBM28 domain eliminated binding to crystalline cellulose and rendered the enzyme inactive on this substrate. Csac_2722 is the largest open reading frame (ORF) in theC. saccharolyticusgenome (predicted molecular mass of 286,516 kDa) and contains two putative sugar-binding domains, two Big4 domains (bacterial domains with an immunoglobulin [Ig]-like fold), and a cadherin-like (Cd) domain. Recombinant Csac_2722, lacking the SLH and Cd domains, bound to cellulose and had detectable carboxymethylcellulose (CMC) hydrolytic activity. Antibodies directed against Csac_0678 and Csac_2722 confirmed that these proteins bound to theC. saccharolyticusS-layer. Their cellular localization and functional biochemical properties indicate roles for Csac_0678 and Csac_2722 in recruitment and hydrolysis of complex polysaccharides and the deconstruction of lignocellulosic biomass. Furthermore, these results suggest that related SLH domain proteins in otherCaldicellulosiruptorgenomes may also be important contributors to plant biomass utilization.
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3

Chauvaux, Sylvie, Markus Matuschek, and Pierre Beguin. "Distinct Affinity of Binding Sites for S-Layer Homologous Domains in Clostridium thermocellum and Bacillus anthracis Cell Envelopes." Journal of Bacteriology 181, no. 8 (April 15, 1999): 2455–58. http://dx.doi.org/10.1128/jb.181.8.2455-2458.1999.

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ABSTRACT Binding parameters were determined for the SLH (S-layer homologous) domains from the Clostridium thermocellum outer layer protein OlpB, from the C. thermocellum S-layer protein SlpA, and from the Bacillus anthracis S-layer proteins EA1 and Sap, using cell walls from C. thermocellum and B. anthracis. Each SLH domain bound to C. thermocellumand B. anthracis cell walls with a differentKD , ranging between 7.1 × 10−7 and 1.8 × 10−8 M. Cell wall binding sites for SLH domains displayed different binding specificities in C. thermocellum and B. anthracis. SLH-binding sites were not detected in cell walls of Bacillus subtilis. Cell walls of C. thermocellum lost their affinity for SLH domains after treatment with 48% hydrofluoric acid but not after treatment with formamide or dilute acid. A soluble component, extracted from C. thermocellum cells by sodium dodecyl sulfate treatment, bound the SLH domains from C. thermocellum but not those from B. anthracisproteins. A corresponding component was not found in B. anthracis.
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4

Kosugi, Akihiko, Koichiro Murashima, Yutaka Tamaru, and Roy H. Doi. "Cell-Surface-Anchoring Role of N-Terminal Surface Layer Homology Domains of Clostridium cellulovorans EngE." Journal of Bacteriology 184, no. 4 (February 15, 2002): 884–88. http://dx.doi.org/10.1128/jb.184.4.884-888.2002.

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ABSTRACT engE, coding for endoglucanase E, one of the three major subunits of the Clostridium cellulovorans cellulosome, has been cloned and sequenced (Y. Tamaru and R. H. Doi, J. Bacteriol. 181:3270-3276, 1999). The N-terminal-half region of EngE possesses three repeated surface layer homology (SLH) domains, which are homologous to those of some bacterial S-layer proteins. Also, the C-terminal-half region consists of a catalytic domain of glycosyl hydrolase family 5 and a duplicated sequence (dockerin) for binding EngE to scaffolding protein CbpA. Our hypothesis is that the SLH domains serve in the role of anchoring to the cell surface. This model was investigated by using recombinant EngEs (rEngE) with and without SLH domains that were synthesized in Escherichia coli and cell wall preparations from C. cellulovorans. When rEngE and SLH polypeptides of EngE were incubated with cell wall fragments prepared by sodium dodecyl sulfate treatment, these proteins bound strongly to the cell wall. However, rEngEs without SLH domains lost their ability to bind to cell walls. When rEngE was incubated with mini-CbpA, consisting of two cohesin domains, and cell wall fragments, the mini-CbpA was able to bind to the cell wall with rEngE. However, the binding of mini-CbpA was dramatically inhibited by addition of a chelating reagent, such as EDTA, which prevents cohesin-dockerin interactions. These results suggest not only that the SLH domains of EngE can bind to the cell surface but also that EngE plays an anchoring role for cellulosomes through the interaction of its dockerin domain with a CbpA cohesin.
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5

Cann, Isaac K. O., Svetlana Kocherginskaya, Michael R. King, Bryan A. White, and Roderick I. Mackie. "Molecular Cloning, Sequencing, and Expression of a Novel Multidomain Mannanase Gene from Thermoanaerobacterium polysaccharolyticum." Journal of Bacteriology 181, no. 5 (March 1, 1999): 1643–51. http://dx.doi.org/10.1128/jb.181.5.1643-1651.1999.

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ABSTRACT The manA gene of Thermoanaerobacterium polysaccharolyticum was cloned in Escherichia coli. The open reading frame of manA is composed of 3,291 bases and codes for a preprotein of 1,097 amino acids with an estimated molecular mass of 119,627 Da. The start codon is preceded by a strong putative ribosome binding site (TAAGGCGGTG) and a putative −35 (TTCGC) and −10 (TAAAAT) promoter sequence. The ManA of T. polysaccharolyticum is a modular protein. Sequence comparison and biochemical analyses demonstrate the presence of an N-terminal leader peptide, and three other domains in the following order: a putative mannanase-cellulase catalytic domain, cellulose binding domains 1 (CBD1) and CBD2, and a surface-layer-like protein region (SLH-1, SLH-2, and SLH-3). The CBD domains show no sequence homology to any cellulose binding domain yet reported, hence suggesting a novel CBD. The duplicated CBDs, which lack a disulfide bridge, exhibit 69% identity, and their deletion resulted in both failure to bind to cellulose and an apparent loss of carboxymethyl cellulase and mannanase activities. At the C-terminal region of the gene are three repeats of 59, 67, and 56 amino acids which are homologous to conserved sequences found in the S-layer-associated regions within the xylanases and cellulases of thermophilic members of theBacillus-Clostridium cluster. The ManA of T. polysaccharolyticum, besides being an extremely active enzyme, is the only mannanase gene cloned which shows this domain structure.
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6

Li, Jia, Xiaomin Hu, Jianpin Yan, and Zhiming Yuan. "Species-Specific Cell Wall Binding Affinity of the S-Layer Proteins of Mosquitocidal Bacterium Bacillus sphaericus C3-41." Applied and Environmental Microbiology 75, no. 12 (April 24, 2009): 3891–95. http://dx.doi.org/10.1128/aem.00356-09.

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ABSTRACT The binding affinities and specificities of six truncated S-layer homology domain (SLH) polypeptides of mosquitocidal Bacillus sphaericus strain C3-41 with the purified cell wall sacculi have been assayed. The results indicated that the SLH polypeptide comprised of amino acids 31 to 210 was responsible for anchoring the S-layer subunits to the rigid cell wall layer via a distinct type of secondary cell wall polymer and that a motif of the recombinant SLH polypeptide comprising amino acids 152 to 210 (rSLH152-210) was essential for the stable binding of the S-layer with the bacterial cell walls. The quantitative assays revealed that the KD (equilibrium dissociation constant) values of rSLH152-210 and rSLH31-210 with purified cell wall sacculi were 1.11 × 10−6 M and 1.40 × 10−6 M, respectively. The qualitative assays demonstrated that the SLH domain of strain C3-41 could bind only to the cell walls or the cells treated with 5 M guanidinium hydrochloride of both toxic and nontoxic B. sphaericus strains but not to those from other bacteria, indicating the species-specific binding of the SLH polypeptide of B. sphaericus with bacterial cell walls.
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7

Kojima, Seiji, Kyong-Cheol Ko, Yumiko Takatsuka, Naoki Abe, Jun Kaneko, Yoshifumi Itoh, and Yoshiyuki Kamio. "Cadaverine Covalently Linked to Peptidoglycan Is Required for Interaction between the Peptidoglycan and the Periplasm-Exposed S-Layer-Homologous Domain of Major Outer Membrane Protein Mep45 in Selenomonas ruminantium." Journal of Bacteriology 192, no. 22 (September 17, 2010): 5953–61. http://dx.doi.org/10.1128/jb.00417-10.

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ABSTRACT The peptidoglycan of Selenomonas ruminantium is covalently bound to cadaverine (PG-cadaverine), which likely plays a significant role in maintaining the integrity of the cell surface structure. The outer membrane of this bacterium contains a 45-kDa major protein (Mep45) that is a putative peptidoglycan-associated protein. In this report, we determined the nucleotide sequence of the mep45 gene and investigated the relationship between PG-cadaverine, Mep45, and the cell surface structure. Amino acid sequence analysis showed that Mep45 is comprised of an N-terminal S-layer-homologous (SLH) domain followed by α-helical coiled-coil region and a C-terminal β-strand-rich region. The N-terminal SLH domain was found to be protruding into the periplasmic space and was responsible for binding to peptidoglycan. It was determined that Mep45 binds to the peptidoglycan in a manner dependent on the presence of PG-cadaverine. Electron microscopy revealed that defective PG-cadaverine decreased the structural interactions between peptidoglycan and the outer membrane, consistent with the proposed role for PG-cadaverine. The C-terminal β-strand-rich region of Mep45 was predicted to be a membrane-bound unit of the 14-stranded β-barrel structure. Here we propose that PG-cadaverine possesses functional importance to facilitate the structural linkage between peptidoglycan and the outer membrane via specific interaction with the SLH domain of Mep45.
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8

Tamaru, Yutaka, and Roy H. Doi. "Three Surface Layer Homology Domains at the N Terminus of the Clostridium cellulovorans Major Cellulosomal Subunit EngE." Journal of Bacteriology 181, no. 10 (May 15, 1999): 3270–76. http://dx.doi.org/10.1128/jb.181.10.3270-3276.1999.

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ABSTRACT The gene engE, coding for endoglucanase E, one of the three major subunits of the Clostridium cellulovoranscellulosome, has been isolated and sequenced. engE is comprised of an open reading frame (ORF) of 3,090 bp and encodes a protein of 1,030 amino acids with a molecular weight of 111,796. The amino acid sequence derived from engE revealed a structure consisting of catalytic and noncatalytic domains. The N-terminal-half region of EngE consisted of a signal peptide of 31 amino acid residues and three repeated surface layer homology (SLH) domains, which were highly conserved and homologous to an S-layer protein from the gram-negative bacterium Caulobacter crescentus. The C-terminal-half region, which is necessary for the enzymatic function of EngE and for binding of EngE to the scaffolding protein CbpA, consisted of a catalytic domain homologous to that of family 5 of the glycosyl hydrolases, a domain of unknown function, and a duplicated sequence (DS or dockerin) at its C terminus. engE is located downstream of an ORF, ORF1, that is homologous to theBacillus subtilis phosphomethylpyrimidine kinase (pmk) gene. The unique presence of three SLH domains and a DS suggests that EngE is capable of binding both to CbpA to form a CbpA-EngE cellulosome complex and to the surface layer of C. cellulovorans.
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9

Lupas, Andrei. "A circular permutation event in the evolution of the SLH domain?" Molecular Microbiology 20, no. 4 (May 1996): 897–98. http://dx.doi.org/10.1111/j.1365-2958.1996.tb02528.x.

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10

Fukuda, Mutsumi, Seiji Watanabe, Shigeki Yoshida, Hiroya Itoh, Yoshifumi Itoh, Yoshiyuki Kamio, and Jun Kaneko. "Cell Surface Xylanases of the Glycoside Hydrolase Family 10 Are Essential for Xylan Utilization by Paenibacillus sp. W-61 as Generators of Xylo-Oligosaccharide Inducers for the Xylanase Genes." Journal of Bacteriology 192, no. 8 (February 12, 2010): 2210–19. http://dx.doi.org/10.1128/jb.01406-09.

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ABSTRACT Paenibacillus sp. W-61 is capable of utilizing water-insoluble xylan for carbon and energy sources and has three xylanase genes, xyn1, xyn3, and xyn5. Xyn1, Xyn3, and Xyn5 are extracellular enzymes of the glycoside hydrolase (GH) families 11, 30, and 10, respectively. Xyn5 contains several domains including those of carbohydrate-binding modules (CBMs) similar to a surface-layer homologous (SLH) protein. This study focused on the role of Xyn5, localized on the cell surface, in water-insoluble xylan utilization. Electron microscopy using immunogold staining revealed Xyn5 clusters over the entire cell surface. Xyn5 was bound to cell wall fractions through its SLH domain. A Δxyn5 mutant grew poorly and produced minimal amounts of Xyn1 and Xyn3 on water-insoluble xylan. A Xyn5 mutant lacking the SLH domain (Xyn5ΔSLH) grew poorly, secreting Xyn5ΔSLH into the medium and producing minimal Xyn1 and Xyn3 on water-insoluble xylan. A mutant with an intact xyn5 produced Xyn5 on the cell surface, grew normally, and actively synthesized Xyn1 and Xyn3 on water-insoluble xylan. Quantitative reverse transcription-PCR showed that xylobiose, generated from water-insoluble xylan decomposition by Xyn5, is the most active inducer for xyn1 and xyn3. Luciferase assays using a Xyn5-luciferase fusion protein suggested that xylotriose is the best inducer for xyn5. The cell surface Xyn5 appears to play two essential roles in water-insoluble xylan utilization: (i) generation of the xylo-oligosaccharide inducers of all the xyn genes from water-insoluble xylan and (ii) attachment of the cells to the substrate so that the generated inducers can be immediately taken up by cells to activate expression of the xyn system.
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11

Karjalainen, Tuomo, Anne-Judith Waligora-Dupriet, Marina Cerquetti, Patrizia Spigaglia, Andrea Maggioni, Pierluigi Mauri, and Paola Mastrantonio. "Molecular and Genomic Analysis of Genes Encoding Surface-Anchored Proteins from Clostridium difficile." Infection and Immunity 69, no. 5 (May 1, 2001): 3442–46. http://dx.doi.org/10.1128/iai.69.5.3442-3446.2001.

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ABSTRACT The gene slpA, encoding the S-layer precursor protein in the virulent Clostridium difficile strains C253 and 79–685, was identified. The precursor protein carries a C-terminal highly conserved anchoring domain, similar to the one found in the Cwp66 adhesin (previously characterized in strain 79–685), an SLH domain, and a variable N-terminal domain mediating cell adherence. The genes encoding the S-layer precursor proteins and the Cwp66 adhesin are present in a genetic locus carrying 17 open reading frames, 11 of which encode a similar two-domain architecture, likely to include surface-anchored proteins.
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12

Anderson, Valerie J., Justin W. Kern, Justin W. McCool, Olaf Schneewind, and Dominique Missiakas. "The SLH‐domain protein BslO is a determinant of Bacillus anthracis chain length." Molecular Microbiology 81, no. 1 (May 17, 2011): 192–205. http://dx.doi.org/10.1111/j.1365-2958.2011.07688.x.

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13

Ito, Yasuko, Toshio Tomita, Narayan Roy, Akito Nakano, Noriko Sugawara-Tomita, Seiji Watanabe, Naoko Okai, Naoki Abe, and Yoshiyuki Kamio. "Cloning, Expression, and Cell Surface Localization of Paenibacillus sp. Strain W-61 Xylanase 5, a Multidomain Xylanase." Applied and Environmental Microbiology 69, no. 12 (December 2003): 6969–78. http://dx.doi.org/10.1128/aem.69.12.6969-6978.2003.

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ABSTRACT We have shown that a xylan-degrading bacterium, W-61, excretes multiple xylanases, including xylanase 5 with a molecular mass of 140 kDa. Here, we emend the previously used classification of the bacterium (i.e., Aeromonas caviae W-61) to Paenibacillus sp. strain W-61 on the basis of the nucleotide sequence of the 16S rRNA gene, and we clone and express the xyn5 gene encoding xylanase 5 (Xyn5) in Escherichia coli and study the subcellular localization of Xyn5. xyn5 encodes 1,326 amino acid residues, including a 27-amino-acid signal sequence. Sequence analysis indicated that Xyn5 comprises two family 22 carbohydrate-binding modules (CBM), a family 10 catalytic domain of glycosyl hydrolases, a family 9 CBM, a domain similar to the lysine-rich region of Clostridium thermocellum SdbA, and three S-layer-homologous (SLH) domains. Recombinant Xyn5 bound to a crystalline cellulose, Avicel PH-101, while an N-terminal 90-kDa fragment of Xyn5, which lacks the C-terminal half of the family 9 CBM, did not bind to Avicel PH-101. Xyn5 was cell bound, and the cell-bound protein was digested by exogenous trypsin to produce immunoreactive and xylanolytic fragments with molecular masses of 80 and 60 kDa. Xyn5 was exclusively distributed in the cell envelope fraction consisting of a peptidoglycan-containing layer and an associated S layer. Thus, Paenibacillus sp. strain W-61 Xyn5 is a cell surface-anchored modular xylanase possessing a functional cellulose-binding module and SLH domains. Possible cooperative action of multiple xylanases produced by strain W-61 is discussed on the basis of the modular structure of Xyn5.
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14

Kwiatkowski, Grzegorz. "Wiersze." Studia Litteraria et Historica, no. 3–4 (January 31, 2016): 67–78. http://dx.doi.org/10.11649/slh.2015.006.

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PoemsKwiatkowski’s poems resemble the spirit of The Spoon River Anthology by Edgar Lee Masters, The Chronicles of the Town of Pornic by Czesław Miłosz, and uprising poems by Anna Świrszczyńska. The author is interested in the mask lyric and attempts to lead his poetry in to the domain of fact, while neither leaving the sphere of poetry nor entering the sphere of journalism. WierszePoezja utrzymana w duchu Umarłych ze Spoon River Edgara Lee Mastersa, Kronik miasta Pornic Czesława Miłosza i wierszy powstańczych Anny Świrszczyńskiej. Autora interesuje liryka maski i próba wy­prowadzenia poezji na teren faktu przy jednoczesnym niewychodzeniu poza sferę poezji i niewchodzeniu w sferę publicystyki.
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15

StJohn, Franz J., John D. Rice, and James F. Preston. "Paenibacillus sp. Strain JDR-2 and XynA1: a Novel System for Methylglucuronoxylan Utilization." Applied and Environmental Microbiology 72, no. 2 (February 2006): 1496–506. http://dx.doi.org/10.1128/aem.72.2.1496-1506.2006.

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ABSTRACT Environmental and economic factors predicate the need for efficient processing of renewable sources of fuels and chemicals. To fulfill this need, microbial biocatalysts must be developed to efficiently process the hemicellulose fraction of lignocellulosic biomass for fermentation of pentoses. The predominance of methylglucuronoxylan (MeGAXn), a β-1,4 xylan in which 10% to 20% of the xylose residues are substituted with α-1,2-4-O-methylglucuronate residues, in hemicellulose fractions of hardwood and crop residues has made this a target for processing and fermentation. A Paenibacillus sp. (strain JDR-2) has been isolated and characterized for its ability to efficiently utilize MeGAXn. A modular xylanase (XynA1) of glycosyl hydrolase family 10 (GH 10) was identified through DNA sequence analysis that consists of a triplicate family 22 carbohydrate binding module followed by a GH 10 catalytic domain followed by a single family 9 carbohydrate binding module and concluding with C-terminal triplicate surface layer homology (SLH) domains. Immunodetection of the catalytic domain of XynA1 (XynA1 CD) indicates that the enzyme is associated with the cell wall fraction, supporting an anchoring role for the SLH modules. With MeGAXn as substrate, XynA1 CD generated xylobiose and aldotetrauronate (MeGAX3) as predominant products. The inability to detect depolymerization products in medium during exponential growth of Paenibacillus sp. strain JDR-2 on MeGAXn, as well as decreased growth rate and yield with XynA1 CD-generated xylooligosaccharides and aldouronates as substrates, indicates that XynA1 catalyzes a depolymerization process coupled to product assimilation. This depolymerization/assimilation system may be utilized for development of biocatalysts to efficiently convert MeGAXn to alternative fuels and biobased products.
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16

Han, Yejun, Dylan Dodd, Charles W. Hespen, Samuel Ohene-Adjei, Charles M. Schroeder, Roderick I. Mackie, and Isaac K. O. Cann. "Comparative Analyses of Two Thermophilic Enzymes Exhibiting both β-1,4 Mannosidic and β-1,4 Glucosidic Cleavage Activities from Caldanaerobius polysaccharolyticus." Journal of Bacteriology 192, no. 16 (June 18, 2010): 4111–21. http://dx.doi.org/10.1128/jb.00257-10.

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ABSTRACT The hydrolysis of polysaccharides containing mannan requires endo-1,4-β-mannanase and 1,4-β-mannosidase activities. In the current report, the biochemical properties of two endo-β-1,4-mannanases (Man5A and Man5B) from Caldanaerobius polysaccharolyticus were studied. Man5A is composed of an N-terminal signal peptide (SP), a catalytic domain, two carbohydrate-binding modules (CBMs), and three surface layer homology (SLH) repeats, whereas Man5B lacks the SP, CBMs, and SLH repeats. To gain insights into how the two glycoside hydrolase family 5 (GH5) enzymes may aid the bacterium in energy acquisition and also the potential application of the two enzymes in the biofuel industry, two derivatives of Man5A (Man5A-TM1 [TM1 stands for truncational mutant 1], which lacks the SP and SLH repeats, and Man5A-TM2, which lacks the SP, CBMs, and SLH repeats) and the wild-type Man5B were biochemically analyzed. The Man5A derivatives displayed endo-1,4-β-mannanase and endo-1,4-β-glucanase activities and hydrolyzed oligosaccharides with a degree of polymerization (DP) of 4 or higher. Man5B exhibited endo-1,4-β-mannanase activity and little endo-1,4-β-glucanase activity; however, this enzyme also exhibited 1,4-β-mannosidase and cellodextrinase activities. Man5A-TM1, compared to either Man5A-TM2 or Man5B, had higher catalytic activity with soluble and insoluble polysaccharides, indicating that the CBMs enhance catalysis of Man5A. Furthermore, Man5A-TM1 acted synergistically with Man5B in the hydrolysis of β-mannan and carboxymethyl cellulose. The versatility of the two enzymes, therefore, makes them a resource for depolymerization of mannan-containing polysaccharides in the biofuel industry. Furthermore, on the basis of the biochemical and genomic data, a molecular mechanism for utilization of mannan-containing nutrients by C. polysaccharolyticus is proposed.
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17

Kalmokoff, M. L., J. W. Austin, M. F. Whitford, and R. M. Teather. "Characterization of a major envelope protein from the rumen anaerobeSelenomonas ruminantiumOB268." Canadian Journal of Microbiology 46, no. 4 (April 1, 2000): 295–303. http://dx.doi.org/10.1139/w99-149.

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Cell envelopes from the Gram-negative staining but phylogenetically Gram-positive rumen anaerobe Selenomonas ruminantium OB268 contained a major 42 kDa heat modifiable protein. A similarly sized protein was present in the envelopes of Selenomonas ruminantium D1 and Selenomonas infelix. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of Triton X-100 extracted cell envelopes from S. ruminantium OB268 showed that they consisted primarily of the 42 kDa protein. Polyclonal antisera produced against these envelopes cross-reacted only with the 42 kDa major envelope proteins in both S. ruminantium D1 and S. infelix, indicating a conservation of antigenic structure among each of the major envelope proteins. The N-terminus of the 42 kDa S. ruminantium OB268 envelope protein shared significant homology with the S-layer (surface) protein from Thermus thermophilus, as well as additional envelope proteins containing the cell surface binding region known as a surface layer-like homologous (SLH) domain. Thin section analysis of Triton X-100 extracted envelopes demonstrated the presence of an outer bilayer overlaying the cell wall, and a regularly ordered array was visible following freeze-fracture etching through this bilayer. These findings suggest that the regularly ordered array may be composed of the 42 kDa major envelope protein. The 42 kDa protein has similarities with regularly ordered outer membrane proteins (rOMP) reported in certain Gram-negative and ancient eubacteria.Key words: Selenomonas envelope surface SLH domain.
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18

Xu, Qi, Edward A. Bayer, Milana Goldman, Rina Kenig, Yuval Shoham, and Raphael Lamed. "Architecture of the Bacteroides cellulosolvens Cellulosome: Description of a Cell Surface-Anchoring Scaffoldin and a Family 48 Cellulase." Journal of Bacteriology 186, no. 4 (February 15, 2004): 968–77. http://dx.doi.org/10.1128/jb.186.4.968-977.2004.

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ABSTRACT A large gene downstream of the primary Bacteroides cellulosolvens cellulosomal scaffoldin (cipBc, now renamed scaA) was sequenced. The gene, termed scaB, contained an N-terminal leader peptide followed by 10 type I cohesins, an “X” domain of unknown structure and function, and a C-terminal S-layer homology (SLH) surface-anchoring module. In addition, a previously identified gene in a different part of the genome, encoding for a dockerin-borne family 48 cellulosomal glycoside hydrolase (Cel48), was sequenced completely, and a putative cellulosome-related family 9 glycosyl hydrolase was detected. Recombinant fusion proteins, comprising dockerins derived from either the ScaA scaffoldin or Cel48, were overexpressed. Their interaction with ScaA and ScaB cohesins was examined by immunoassay. The results indicated that the ScaB type I cohesin of the new anchoring protein binds selectively to the ScaA dockerin, whereas the Cel48 dockerin binds specifically to the type II ScaA cohesin 5. Thus, by virtue of the 11 type II ScaA cohesins and the 10 type I ScaB cohesins, the relatively simple two-component cellulosome-integrating complex would potentially incorporate 110 enzyme molecules onto the cell surface via the ScaB SLH module. Compared to previously described cellulosome systems, the apparent roles of the B. cellulosolvens cohesins are reversed, in that the type II cohesins are located on the enzyme-binding primary scaffoldin, whereas the type I cohesins are located on the anchoring scaffoldin. The results underscore the extensive diversity in the supramolecular architecture of cellulosome systems in nature.
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Mader, Christoph, Carina Huber, Dieter Moll, Uwe B. Sleytr, and Margit Sára. "Interaction of the Crystalline Bacterial Cell Surface Layer Protein SbsB and the Secondary Cell Wall Polymer of Geobacillus stearothermophilus PV72 Assessed by Real-Time Surface Plasmon Resonance Biosensor Technology." Journal of Bacteriology 186, no. 6 (March 15, 2004): 1758–68. http://dx.doi.org/10.1128/jb.186.6.1758-1768.2004.

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ABSTRACT The interaction between S-layer protein SbsB and the secondary cell wall polymer (SCWP) of Geobacillus stearothermophilus PV72/p2 was investigated by real-time surface plasmon resonance biosensor technology. The SCWP is an acidic polysaccharide that contains N-acetylglucosamine, N-acetylmannosamine, and pyruvic acid. For interaction studies, recombinant SbsB (rSbsB) and two truncated forms consisting of either the S-layer-like homology (SLH) domain (3SLH) or the residual part of SbsB were used. Independent of the setup, the data showed that the SLH domain was exclusively responsible for SCWP binding. The interaction was found to be highly specific, since neither the peptidoglycan nor SCWPs from other organisms nor other polysaccharides were recognized. Data analysis from that setup in which 3SLH was immobilized on a sensor chip and SCWP represented the soluble analyte was done in accordance with a model that describes binding of a bivalent analyte to a fixed ligand in terms of an overall affinity for all binding sites. The measured data revealed the presence of at least two binding sites on a single SCWP molecule with a distance of about 14 nm and an overall K d of 7.7 × 10−7 M. Analysis of data from the inverted setup in which the SCWP was immobilized on a sensor chip was done in accordance with an extension of the heterogeneous-ligand model, which indicated the existence of three binding sites with low (K d = 2.6 × 10−5 M), medium (K d = 6.1 × 10−8 M), and high (K d = 6.7 × 10−11 M) affinities. Since in this setup 3SLH was the soluble analyte and the presence of small amounts of oligomers in even monomeric protein solutions cannot be excluded, the high-affinity binding site may result from avidity effects caused by binding of at least dimeric 3SLH. Solution competition assays performed with both setups confirmed the specificity of the protein-carbohydrate interaction investigated.
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Mesnage, S. "Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation." EMBO Journal 19, no. 17 (September 1, 2000): 4473–84. http://dx.doi.org/10.1093/emboj/19.17.4473.

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Candela, Thomas, Tâm Mignot, Xavier Hagnerelle, Michel Haustant, and Agnès Fouet. "Genetic analysis of Bacillus anthracis Sap S-layer protein crystallization domain." Microbiology 151, no. 5 (May 1, 2005): 1485–90. http://dx.doi.org/10.1099/mic.0.27832-0.

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Bacillus anthracis, the aetiological agent of anthrax, synthesizes two surface-layer (S-layer) proteins. S-layers are two-dimensional crystalline arrays that completely cover bacteria. In rich medium, the B. anthracis S-layer consists of Sap during the exponential growth phase. Sap is a modular protein composed of an SLH (S-layer homology)-anchoring domain followed by a putative crystallization domain (Sapc). A projection map of the two-dimensional Sap array has been established on deflated bacteria. In this work, the authors used two approaches to investigate whether Sapc is the crystallization domain. The purified Sapc polypeptide (604 aa) was sufficient to form a crystalline structure, as illustrated by electron microscopy. Consistent with this result, the entire Sapc domain promoted auto-interaction in a bacterial two-hybrid screen developed for the present study. The screen was derived from a system that takes advantage of the Bordetella pertussis cyclase subdomain structure to enable one to identify peptides that interact. A screening strategy was then employed to study Sapc subdomains that mediate interaction. A random library, derived from the Sapc domain, was constructed and screened. The selected polypeptides interacting with the complete Sapc were all larger (155 aa and above) than the mean size of the randomly cloned peptides (approx. 60 residues). This result suggests that, in contrast with observations for other interactions studied with this two-hybrid system, large fragments were required to ensure efficient interaction. It was noteworthy that only one polypeptide, which spanned aa 148–358, was able to interact with less than the complete Sapc, in fact, with itself.
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Xu, Qi, Wenchen Gao, Shi-You Ding, Rina Kenig, Yuval Shoham, Edward A. Bayer, and Raphael Lamed. "The Cellulosome System of Acetivibrio cellulolyticus Includes a Novel Type of Adaptor Protein and a Cell Surface Anchoring Protein." Journal of Bacteriology 185, no. 15 (August 1, 2003): 4548–57. http://dx.doi.org/10.1128/jb.185.15.4548-4557.2003.

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ABSTRACT A scaffoldin gene cluster was identified in the mesophilic cellulolytic anaerobe Acetivibrio cellulolyticus. The previously described scaffoldin gene, cipV, encodes an N-terminal family 9 glycoside hydrolase, a family 3b cellulose-binding domain, seven cohesin domains, and a C-terminal dockerin. The gene immediately downstream of cipV was sequenced and designated scaB. The protein encoded by this gene has 942 amino acid residues and a calculated molecular weight of 100,358 and includes an N-terminal signal peptide, four type II cohesions, and a C-terminal dockerin. ScaB cohesins 1 and 2 are very closely linked. Similar, but not identical, 39-residue Thr-rich linker segments separate cohesin 2 from cohesin 3 and cohesin 3 from cohesin 4, and an 84-residue Thr-rich linker connects the fourth cohesin to a C-terminal dockerin. The scaC gene downstream of scaB codes for a 1,237-residue polypeptide that includes a signal peptide, three cohesins, and a C-terminal S-layer homology (SLH) module. A long, ca. 550-residue linker separates the third cohesin and the SLH module of ScaC and is characterized by an 18-residue Pro-Thr-Ala-Ser-rich segment that is repeated 27 times. The calculated molecular weight of the mature ScaC polypeptide (excluding the signal peptide) is 124,162. The presence of the cohesins and the conserved SLH module implies that ScaC acts as an anchoring protein. The ScaC cohesins are on a separate branch of the phylogenetic tree that is close to, but distinct from, the type I cohesins. Affinity blotting with representative recombinant probes revealed the following specific intermodular interactions: (i) an expressed CipV cohesin binds selectively to an enzyme-borne dockerin, (ii) a representative ScaB cohesin binds to the CipV band of the cell-free supernatant fraction, and (iii) a ScaC cohesin binds to the ScaB dockerin. The experimental evidence thus indicates that CipV acts as a primary (enzyme-recognizing) scaffoldin, and the protein was also designated ScaA. In addition, ScaB is thought to assume the role of an adaptor protein, which connects the primary scaffoldin (ScaA) to the cohesin-containing anchoring scaffoldin (ScaC). The cellulosome system of A. cellulolyticus thus appears to exhibit a special type of organization that reflects the function of the ScaB adaptor protein. The intercalation of three multiple cohesin-containing scaffoldins results in marked amplification of the number of enzyme subunits per cellulosome unit. At least 96 enzymes can apparently be incorporated into an individual A. cellulolyticus cellulosome. The role of such amplified enzyme incorporation and the resultant proximity of the enzymes within the cellulosome complex presumably contribute to the enhanced synergistic action and overall efficient digestion of recalcitrant forms of cellulose. Comparison of the emerging organization of the A. cellulolyticus cellulosome with the organizations in other cellulolytic bacteria revealed the diversity of the supramolecular architecture.
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Tarlovsky, Yael, Marian Fabian, Elena Solomaha, Erin Honsa, John S. Olson, and Anthony W. Maresso. "A Bacillus anthracis S-Layer Homology Protein That Binds Heme and Mediates Heme Delivery to IsdC." Journal of Bacteriology 192, no. 13 (April 30, 2010): 3503–11. http://dx.doi.org/10.1128/jb.00054-10.

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ABSTRACT The sequestration of iron by mammalian hosts represents a significant obstacle to the establishment of a bacterial infection. In response, pathogenic bacteria have evolved mechanisms to acquire iron from host heme. Bacillus anthracis, the causative agent of anthrax, utilizes secreted hemophores to scavenge heme from host hemoglobin, thereby facilitating iron acquisition from extracellular heme pools and delivery to iron-regulated surface determinant (Isd) proteins covalently attached to the cell wall. However, several Gram-positive pathogens, including B. anthracis, contain genes that encode near iron transporter (NEAT) proteins that are genomically distant from the genetically linked Isd locus. NEAT domains are protein modules that partake in several functions related to heme transport, including binding heme and hemoglobin. This finding raises interesting questions concerning the relative role of these NEAT proteins, relative to hemophores and the Isd system, in iron uptake. Here, we present evidence that a B. anthracis S-layer homology (SLH) protein harboring a NEAT domain binds and directionally transfers heme to the Isd system via the cell wall protein IsdC. This finding suggests that the Isd system can receive heme from multiple inputs and may reflect an adaptation of B. anthracis to changing iron reservoirs during an infection. Understanding the mechanism of heme uptake in pathogenic bacteria is important for the development of novel therapeutics to prevent and treat bacterial infections.
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Chow, Virginia, Young Sik Kim, Mun Su Rhee, Neha Sawhney, Franz J. St. John, Guang Nong, John D. Rice, and James F. Preston. "A 1,3-1,4-β-Glucan Utilization Regulon in Paenibacillus sp. Strain JDR-2." Applied and Environmental Microbiology 82, no. 6 (January 8, 2016): 1789–98. http://dx.doi.org/10.1128/aem.03526-15.

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ABSTRACTPaenibacillussp. strain JDR-2 (PaenibacillusJDR-2) secretes a multimodular cell-associated glycoside hydrolase family 10 (GH10) endoxylanase (XynA10A1) that catalyzes the depolymerization of methylglucuronoxylan (MeGXn) and rapidly assimilates the products of depolymerization. Efficient utilization of MeGXnhas been postulated to result from the coupling of the processes of exocellular depolymerization and assimilation of oligosaccharide products, followed by intracellular metabolism. Growth and substrate utilization patterns with barley glucan and laminarin similar to those observed with MeGXnas a substrate suggest similar processes for 1,3-1,4-β-glucan and 1,3-β-glucan depolymerization and product assimilation. ThePaenibacillusJDR-2 genome includes a cluster of genes encoding a secreted multimodular GH16 β-glucanase (Bgl16A1) containing surface layer homology (SLH) domains, a secreted GH16 β-glucanase with only a catalytic domain (Bgl16A2), transporter proteins, and transcriptional regulators. Recombinant Bgl16A1and Bgl16A2catalyze the formation of trisaccharides, tetrasaccharides, and larger oligosaccharides from barley glucan and of mono-, di-, tri-, and tetrasaccharides and larger oligosaccharides from laminarin. The lack of accumulation of depolymerization products during growth and a marked preference for polymeric glucan over depolymerization products support a process coupling extracellular depolymerization, assimilation, and intracellular metabolism for β-glucans similar to that ascribed to the GH10/GH67 xylan utilization system inPaenibacillusJDR-2. Coordinate expression of genes encoding GH16 β-glucanases, transporters, and transcriptional regulators supports their role as a regulon for the utilization of soluble β-glucans. As in the case of the xylan utilization regulons, this soluble β-glucan regulon provides advantages in the growth rate and yields on polymeric substrates and may be exploited for the efficient conversion of plant-derived polysaccharides to targeted products.
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Ariel, N., A. Zvi, K. S. Makarova, T. Chitlaru, E. Elhanany, B. Velan, S. Cohen, A. M. Friedlander, and A. Shafferman. "Genome-Based Bioinformatic Selection of Chromosomal Bacillus anthracis Putative Vaccine Candidates Coupled with Proteomic Identification of Surface-Associated Antigens." Infection and Immunity 71, no. 8 (August 2003): 4563–79. http://dx.doi.org/10.1128/iai.71.8.4563-4579.2003.

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ABSTRACT Bacillus anthracis (Ames strain) chromosome-derived open reading frames (ORFs), predicted to code for surface exposed or virulence related proteins, were selected as B. anthracis-specific vaccine candidates by a multistep computational screen of the entire draft chromosome sequence (February 2001 version, 460 contigs, The Institute for Genomic Research, Rockville, Md.). The selection procedure combined preliminary annotation (sequence similarity searches and domain assignments), prediction of cellular localization, taxonomical and functional screen and additional filtering criteria (size, number of paralogs). The reductive strategy, combined with manual curation, resulted in selection of 240 candidate ORFs encoding proteins with putative known function, as well as 280 proteins of unknown function. Proteomic analysis of two-dimensional gels of a B. anthracis membrane fraction, verified the expression of some gene products. Matrix-assisted laser desorption ionization-time-of-flight mass spectrometry analyses allowed identification of 38 spots cross-reacting with sera from B. anthracis immunized animals. These spots were found to represent eight in vivo immunogens, comprising of EA1, Sap, and 6 proteins whose expression and immunogenicity was not reported before. Five of these 8 immunogens were preselected by the bioinformatic analysis (EA1, Sap, 2 novel SLH proteins and peroxiredoxin/AhpC), as vaccine candidates. This study demonstrates that a combination of the bioinformatic and proteomic strategies may be useful in promoting the development of next generation anthrax vaccine.
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Schaller, Franziska, Brittany Lee, Zed Sevcikova Sehyr, Lucinda O’Grady Farnady, and Karen Emmorey. "Cross-linguistic metaphor priming in ASL-English bilinguals." Special Issue in Memory of Irit Meir 23, no. 1-2 (October 30, 2020): 96–111. http://dx.doi.org/10.1075/sll.00045.sch.

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Abstract Meir’s (2010) Double Mapping Constraint (DMC) states the use of iconic signs in metaphors is restricted to signs that preserve the structural correspondence between the articulators and the concrete source domain and between the concrete and metaphorical domains. We investigated ASL signers’ comprehension of English metaphors whose translations complied with the DMC (Communication collapsed during the meeting) or violated the DMC (The acid ate the metal). Metaphors were preceded by the ASL translation of the English verb, an unrelated sign, or a still video. Participants made sensibility judgments. Response times (RTs) were faster for DMC-Compliant sentences with verb primes compared to unrelated primes or the still baseline. RTs for DMC-Violation sentences were longer when preceded by verb primes. We propose the structured iconicity of the ASL verbs primed the semantic features involved in the iconic mapping and these primed semantic features facilitated comprehension of DMC-Compliant metaphors and slowed comprehension of DMC-Violation metaphors.
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27

Klingler, Franca-Maria, Markus Wolf, Sandra Wittmann, Philip Gribbon, and Ewgenij Proschak. "Bacterial Expression and HTS Assessment of Soluble Epoxide Hydrolase Phosphatase." Journal of Biomolecular Screening 21, no. 7 (July 10, 2016): 689–94. http://dx.doi.org/10.1177/1087057116637609.

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Soluble epoxide hydrolase (sEH) is a bifunctional enzyme that possesses an epoxide hydrolase and lipid phosphatase activity (sEH-P) at two distinct catalytic domains. While the physiological role of the epoxide hydrolase domain is well understood, the consequences of the phosphatase activity remain unclear. Herein we describe the bacterial expression of the recombinant N-terminal domain of sEH-P and the development of a high-throughput screening protocol using a sensitive and commercially available substrate fluorescein diphosphate. The usability of the assay system was demonstrated and novel inhibitors of sEH-P were identified.
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28

Mason, A. W. "Free quotients of infinite rank of GL2 over Dedekind domains." Proceedings of the Royal Society of Edinburgh: Section A Mathematics 129, no. 1 (1999): 77–84. http://dx.doi.org/10.1017/s0308210500027475.

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This paper is concerned with integral domains R, for which the factor group SL2(R)/U2(R) has a non-trivial, free quotient, where U2(R) is the subgroup of GL2(R) generated by the unipotent matrices. Recently, Krstić and McCool have proved that SL2(P[x])/U2(P[x]) has a free quotient of infinite rank, where P is a domain which is not a field. This extends earlier results of Grunewald, Mennicke and Vaserstein.Any ring of the type P[x] has Krull dimension at least 2. The purpose of this paper is to show that result of Krstić and McCool extends to some domains of Krull dimension 1, in particular to certain Dedekind domains. This result, which represents a two-dimensional anomaly is the best possible in the following sense. It is well known that SL2(R) = U2(R), when R is a domain of Krull dimension zero, i.e. when R is a field. It is already known that for some arithmetic Dedekind domains A, the factor group SL2(A)/U2(A) has a free quotient of finite (and not infinite) rank.
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29

Manzi, Susan, Jorge Sánchez-Guerrero, Joan T. Merrill, Richard Furie, Dafna Gladman, Sandra V. Navarra, Ellen M. Ginzler, et al. "Effects of belimumab, a B lymphocyte stimulator-specific inhibitor, on disease activity across multiple organ domains in patients with systemic lupus erythematosus: combined results from two phase III trials." Annals of the Rheumatic Diseases 71, no. 11 (May 1, 2012): 1833–38. http://dx.doi.org/10.1136/annrheumdis-2011-200831.

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ObjectiveTo evaluate the effects of belimumab versus placebo, plus standard systemic lupus erythematosus (SLE) therapy, on organ domain-specific SLE disease activity.MethodsData obtained after 52 weeks of treatment from two phase III trials (BLISS-52 and BLISS-76) comparing belimumab 1 and 10 mg/kg versus placebo, plus standard therapy, in 1684 autoantibody-positive patients were analysed post hoc for changes in British Isles Lupus Assessment Group (BILAG) and Safety of Estrogens in Lupus National Assessment–Systemic Lupus Erythematosus Disease Activity Index (SELENA–SLEDAI) organ domain scores.ResultsAt baseline, the domains involved in the majority of patients were musculoskeletal and mucocutaneous by both BILAG and SELENA–SLEDAI, and immunological by SELENA–SLEDAI. At 52 weeks, significantly more patients treated with belimumab versus placebo had improvement in BILAG musculoskeletal and mucocutaneous domains (1 and 10 mg/kg), and in SELENA–SLEDAI mucocutaneous (10 mg/kg), musculoskeletal (1 mg/kg) and immunological (1 and 10 mg/kg) domains. Improvement was also observed in other organ systems with a low prevalence (≤16%) at baseline, including the SELENA–SLEDAI vasculitis and central nervous system domains. Significantly fewer patients treated with belimumab versus placebo had worsening in the BILAG haematological domain (1 mg/kg) and in the SELENA–SLEDAI immunological (10 mg/kg), haematological (10 mg/kg) and renal (1 mg/kg) domains.ConclusionsBelimumab treatment improved overall SLE disease activity in the most common musculoskeletal and mucocutaneous organ domains. Less worsening occurred in the haematological, immunological and renal domains.
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Fry, Christopher J., Anne Norris, Michael Cosgrove, Jef D. Boeke, and Craig L. Peterson. "The LRS and SIN Domains: Two Structurally Equivalent but Functionally Distinct Nucleosomal Surfaces Required for Transcriptional Silencing." Molecular and Cellular Biology 26, no. 23 (October 2, 2006): 9045–59. http://dx.doi.org/10.1128/mcb.00248-06.

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ABSTRACT Genetic experiments have identified two structurally similar nucleosomal domains, SIN and LRS, required for transcriptional repression at genes regulated by the SWI/SNF chromatin remodeling complex or for heterochromatic gene silencing, respectively. Each of these domains consists of histone H3 and H4 L1 and L2 loops that form a DNA-binding surface at either superhelical location (SHL) ±2.5 (LRS) or SHL ±0.5 (SIN). Here we show that alterations in the LRS domain do not result in Sin− phenotypes, nor does disruption of the SIN domain lead to loss of ribosomal DNA heterochromatic gene silencing (Lrs− phenotype). Furthermore, whereas disruption of the SIN domain eliminates intramolecular folding of nucleosomal arrays in vitro, alterations in the LRS domain have no effect on chromatin folding in vitro. In contrast to these dissimilarities, we find that the SIN and LRS domains are both required for recruitment of Sir2p and Sir4p to telomeric and silent mating type loci, suggesting that both surfaces can contribute to heterochromatin formation. Our study shows that structurally similar nucleosomal surfaces provide distinct functionalities in vivo and in vitro.
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Teo, Rachel, Preeti Dhanasekaran, Sen Hee Tay, and Anselm Mak. "Mathematical processing is affected by daily but not cumulative glucocorticoid dose in patients with systemic lupus erythematosus." Rheumatology 59, no. 9 (January 28, 2020): 2534–43. http://dx.doi.org/10.1093/rheumatology/keaa002.

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Abstract Objectives The impact of glucocorticoids on neurocognitive performance in patients with SLE is not fully addressed. We aimed to study the effect of daily and cumulative glucocorticoid dose on neurocognitive performance in SLE patients. Methods Consecutive SLE patients and gender- and age-matched healthy controls (HCs) underwent the computer-based Automated Neuropsychological Assessment Matric (ANAM), which evaluates eight neurocognitive domains including learning, recall, visual perception, mental rotation, short-term memory, attention, sustained attention and working memory. The total and individual-domain throughput scores (TPSs) and the presence of cognitive dysfunction (total TPS <1.5 s.d. below the mean TPS of HCs) were compared between SLE patients and HCs. Within the SLE group, univariate and independent associations between prednisolone dose (daily and cumulative) and individual-domain TPS were studied by univariate and multivariable linear regression, respectively. Results A total of 96 SLE patients and 96 HCs were studied. SLE patients scored significantly worse across all the neurocognitive domains and had a significantly lower mean total TPS (P < 0.001) and a higher prevalence of cognitive dysfunction compared with HCs (25.0 vs 7.3%, P = 0.001). In SLE patients, daily prednisolone dose was significantly and negatively correlated with mathematical-processing TPS, which probes working memory (P = 0.018). No significant correlation between cumulative prednisolone dose and any of the individual-domain TPSs was found. In multivariable regression, higher daily prednisolone dose and doses >9 mg daily remained independently associated with lower mathematical-processing TPSs (P = 0.031). Conclusion Daily prednisolone dose ≥9 mg, but not cumulative glucocorticoid dose, had an independent negative impact on mathematical processing in SLE patients.
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Zhu, Yu-Xiu, Chunxia Ge, Shijun Ma, Xiao-Ying Liu, Mengjie Liu, Yang Sun, and Guan-Feng Wang. "Maize ZmFNSI Homologs Interact with an NLR Protein to Modulate Hypersensitive Response." International Journal of Molecular Sciences 21, no. 7 (April 5, 2020): 2529. http://dx.doi.org/10.3390/ijms21072529.

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Nucleotide binding, leucine-rich-repeat (NLR) proteins are the major class of resistance (R) proteins used by plants to defend against pathogen infection. The recognition between NLRs and their cognate pathogen effectors usually triggers a rapid localized cell death, termed the hypersensitive response (HR). Flavone synthase I (FNSI) is one of the key enzymes in the flavone biosynthesis pathway. It also displays salicylic acid (SA) 5-hydroxylase (S5H) activity. A close homolog of FNSI/S5H displays SA 3-hydroxylase (S3H) activity. Both FNSI/S5H and S3H play important roles in plant innate immunity. However, the underlying molecular mechanisms and the relationship between S5H and S3H with the NLR-mediated HR are not known in any plant species. In this study, we identified three genes encoding ZmFNSI-1, ZmFNSI-2 and ZmS3H that are significantly upregulated in a maize line carrying an autoactive NLR Rp1-D21 mutant. Functional analysis showed that ZmFNSI-1 and ZmFNSI-2, but not ZmS3H, suppressed HR conferred by Rp1-D21 and its signaling domain CCD21 when transiently expressed in N. benthamiana. ZmFNSI-1 and ZmFNSI-2 physically interacted with CCD21. Furthermore, ZmFNSI-1 and ZmFNSI-2 interacted with HCT, a key enzyme in lignin biosynthesis pathway, which can also suppress Rp1-D21-mediated HR. These results lay the foundation for the further functional analysis of the roles of FNSI in plant innate immunity.
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Peckham, Michelle. "Coiled coils and SAH domains in cytoskeletal molecular motors." Biochemical Society Transactions 39, no. 5 (September 21, 2011): 1142–48. http://dx.doi.org/10.1042/bst0391142.

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Cytoskeletal motors include myosins, kinesins and dyneins. Myosins move along tracks of actin filaments, whereas kinesins and dyneins move along microtubules. Many of these motors are involved in trafficking cargo in cells. However, myosins are mostly monomeric, whereas kinesins are mostly dimeric, owing to the presence of a coiled coil. Some myosins (myosins 6, 7 and 10) contain an SAH (single α-helical) domain, which was originally thought to be a coiled coil. These myosins are now known to be monomers, not dimers. The differences between SAH domains and coiled coils are described and the potential roles of SAH domains in molecular motors are discussed.
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Katzan, Irene L., Andrew Schuster, Christopher Newey, Ken Uchino, and Brittany Lapin. "Patient-reported outcomes across cerebrovascular event types." Neurology 91, no. 23 (October 31, 2018): e2182-e2191. http://dx.doi.org/10.1212/wnl.0000000000006626.

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ObjectivesTo compare the degrees to which 8 domains of health are affected across types of cerebrovascular events and to identify factors associated with domain scores in different event types.MethodsThis was an observational cohort study of 2,181 patients with ischemic stroke, intracerebral hemorrhage (ICH), subarachnoid hemorrhage (SAH), or TIA in a cerebrovascular clinic from February 17, 2015, to June 2, 2017 who completed Quality of Life in Neurologic Disorders executive function and the following Patient-Reported Outcomes Measurement Information System scales as part of routine care: physical function, satisfaction with social roles, fatigue, anxiety, depression, pain interference, and sleep disturbance.ResultsAll health domains were affected to similar degrees in patients with ICH, SAH, and ischemic stroke after adjustment for disability and other clinical factors, whereas patients with TIA had worse adjusted scores for 5 of the 8 domains of health. Female sex, younger age, lower income, and event <90 days were associated with worse scores in multiple domains. Factors associated with health domain scores were similar for all cerebrovascular events. Most affected domains for all were physical function, satisfaction with social roles, and executive function.ConclusionsThe subtype of stroke (ischemic stroke, ICH, and SAH) had similar effects in multiple health domains, while patients with TIA had worse adjusted outcomes, suggesting that the mechanisms for outcomes after TIA may differ from those of other cerebrovascular events. The most affected domains across all event types were physical function, satisfaction with social roles, and executive function, highlighting the need to develop effective interventions to improve these health domains in survivors of these cerebrovascular events.
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35

Sasaki, H., Y. Nishizaki, C. Hui, M. Nakafuku, and H. Kondoh. "Regulation of Gli2 and Gli3 activities by an amino-terminal repression domain: implication of Gli2 and Gli3 as primary mediators of Shh signaling." Development 126, no. 17 (September 1, 1999): 3915–24. http://dx.doi.org/10.1242/dev.126.17.3915.

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Gli family zinc finger proteins are mediators of Sonic hedgehog (Shh) signaling in vertebrates. The question remains unanswered, however, as to how these Gli proteins participate in the Shh signaling pathway. In this study, regulatory activities associated with the Gli2 protein were investigated in relation to the Shh signaling. Although Gli2 acts as a weak transcriptional activator, it is in fact a composite of positive and negative regulatory domains. In cultured cells, truncation of the activation domain in the C-terminal half results in a protein with repressor activity, while removal of the repression domain at the N terminus converts Gli2 into a strong activator. In transgenic mouse embryos, N-terminally truncated Gli2, unlike the full length protein, activates a Shh target gene, HNF3beta, in the dorsal neural tube, thus mimicking the effect of Shh signal. This suggests that unmasking of the strong activation potential of Gli2 through modulation of the N-terminal repression domain is one of the key mechanisms of the Shh signaling. A similar regulatory mechanism involving the N-terminal region was also found for Gli3, but not for Gli1. When the Shh signal derived from the notochord is received by the neural plate, the widely expressed Gli2 and Gli3 proteins are presumably converted to their active forms in the ventral cells, leading to activation of transcription of their target genes, including Gli1.
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Batchelor, Matthew, Marcin Wolny, Lorna Dougan, Emanuele Paci, Peter J. Knight, and Michelle Peckham. "Myosin tails and single α-helical domains." Biochemical Society Transactions 43, no. 1 (January 26, 2015): 58–63. http://dx.doi.org/10.1042/bst20140302.

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The human genome contains 39 myosin genes, divided up into 12 different classes. The structure, cellular function and biochemical properties of many of these isoforms remain poorly characterized and there is still some controversy as to whether some myosin isoforms are monomers or dimers. Myosin isoforms 6 and 10 contain a stable single α-helical (SAH) domain, situated just after the canonical lever. The SAH domain is stiff enough to be able to lengthen the lever allowing the myosin to take a larger step. In addition, atomic force microscopy and atomistic simulations show that SAH domains unfold at relatively low forces and have a high propensity to refold. These properties are likely to be important for protein function, enabling motors to carry cargo in dense actin networks, and other proteins to remain attached to binding partners in the crowded cell.
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Hinata, K., M. Watanabe, S. Yamakawa, Y. Satta, and A. Isogai. "Evolutionary aspects of the S-related genes of the Brassica self-incompatibility system: synonymous and nonsynonymous base substitutions." Genetics 140, no. 3 (July 1, 1995): 1099–104. http://dx.doi.org/10.1093/genetics/140.3.1099.

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Abstract In the Brassicaceae, self-vs. nonself-recognition in self-incompatibility is controlled by sporophytic S-alleles. Haplotypes specifying both SRK (S-receptor kinase) and SLG (S-locus glycoprotein) are considered to play an important role in the recognition reactions. We compared the nucleotide sequences of SRK9(Bc) and SRK6(Bo). The number of nonsynonymous substitutions per site (Pn) was lower, constrained, in the kinase than the receptor domain, while the numbers of synonymous substitutions (Ps) in the two domains were largely comparable. Pairwise values for Ps and Pn were calculated among 17 operational taxonomic units, including eight SLGs, the receptor domains of two SRKs, four SRAs (S-related A) and three SRBs (S-related B), which have high homologies with each other. The values of Ps and Pn of SLG were mostly comparable to those of the receptor domain of SRK. Dendrograms constructed on the basis of Pn and Ps indicated that SRA differentiated first, followed by SRB. The differentiation of SLG alleles is one of prerequisite factors for the establishment of self-incompatibility, and the allelic differentiation has occurred more than tens of million years ago.
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Böhm, Sebastian W., Elisa Eckroth, Marija Backovic, Barbara G. Klupp, Felix A. Rey, Thomas C. Mettenleiter, and Walter Fuchs. "Structure-Based Functional Analyses of Domains II and III of Pseudorabies Virus Glycoprotein H." Journal of Virology 89, no. 2 (November 12, 2014): 1364–76. http://dx.doi.org/10.1128/jvi.02765-14.

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ABSTRACTEnveloped viruses utilize membrane fusion for entry into, and release from, host cells. For entry, members of theHerpesviridaerequire at least three envelope glycoproteins: the homotrimeric gB and a heterodimer of gH and gL. The crystal structures of three gH homologues, including pseudorabies virus (PrV) gH, revealed four conserved domains. Domain II contains a planar β-sheet (“fence”) and a syntaxin-like bundle of three α-helices (SLB), similar to those found in eukaryotic fusion proteins, potentially executing an important role in gH function. To test this hypothesis, we introduced targeted mutations into the PrV gH gene, which either disrupt the helices of the SLB by introduction of proline residues or covalently join them by artificial intramolecular disulfide bonds between themselves, to the adjacent fence region, or to domain III. Disruption of either of the three α-helices of the SLB (A250P, V275P, V298P) severely affected gH function inin vitrofusion assays and replication of corresponding PrV mutants. Considerable defects in fusion activity of gH, as well as in penetration kinetics and cell-to-cell spread of PrV mutants, were also observed after disulfide linkage of two α-helices within the SLB (A284C-S291C) or between SLB and domain III (H251C-L432C), as well as by insertions of additional cysteine pairs linking fence, SLB, and domain III.In vitrofusion activity of mutated gH could be partly restored by reduction of the artificial disulfide bonds. Our results indicate that the structure and flexibility of the SLB are relevant for the function of PrV gH in membrane fusion.IMPORTANCEMutational analysis based on crystal structures of proteins is a powerful tool to understand protein function. Here, we continued our study of pseudorabies virus gH, a part of the core fusion machinery of herpesviruses. We previously showed that the “flap” region in domain IV of PrV gH is important for its function. We now demonstrate that mutations within domain II that interfere with integrity or flexibility of a syntaxin-like three-helix bundle also significantly impair gH function during fusion. These studies provide important insights into the structural requirements of gH for function in fusion.
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LAI, JIN-SHEI, JENNIFER L. BEAUMONT, SARIKA OGALE, PAUL BRUNETTA, and DAVID CELLA. "Validation of the Functional Assessment of Chronic Illness Therapy-Fatigue Scale in Patients with Moderately to Severely Active Systemic Lupus Erythematosus, Participating in a Clinical Trial." Journal of Rheumatology 38, no. 4 (January 15, 2011): 672–79. http://dx.doi.org/10.3899/jrheum.100799.

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Objective.Fatigue is a common symptom of systemic lupus erythematosus (SLE). Our objective was to validate the 13-item Functional Assessment of Chronic Illness Therapy (FACIT)-Fatigue scale in patients with SLE.Methods.The FACIT-Fatigue, Medical Outcomes Study Short-Form-36 (SF-36) questionnaire, Brief Pain Inventory (BPI), and Patient Global Assessment Visual Analog Scale (Patient-GA) were completed at baseline and at Weeks 12, 24, and 52 by patients with moderately to severely active extrarenal SLE. The patients were participating in a rituximab clinical trial. The British Isles Lupus Assessment Group (BILAG) disease activity index and the Physician Global Assessment Visual Analog Scale (Physician-GA) were completed by physicians at the same visits.Results.At baseline, 254 patients completed the FACIT-Fatigue scale. Cronbach’s α was > 0.95 at all visits. In cross-sectional analyses, FACIT-Fatigue scores differentiated between groups defined by BILAG General domain ratings. FACIT-Fatigue had moderate-high correlations (r = 0.5–0.8) with SF-36, BPI, and Patient-GA, but poor correlations with BILAG total score and Physician-GA (r = 0.1–0.3). At Weeks 12, 24, and 52, mean FACIT-Fatigue scale improvement was higher in patients who improved versus those who remained unchanged on the BILAG General domain. FACIT-Fatigue scale scores remained stable for patients with worsened BILAG General domain ratings compared to baseline. Distribution and anchor-based estimates suggested a minimally important difference (MID) range of 3–6 points.Conclusion.The FACIT-Fatigue scale is a valid and responsive measure of fatigue in patients with SLE. MID in this SLE sample is similar to that derived previously in other populations. Since few patients experienced worsening BILAG General and Musculoskeletal domains in this study, further research is warranted to evaluate the responsiveness of FACIT-Fatigue to worsening of these domains.
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Mankidy, Rishikesh, Jeremy Hastings, and Justin R. Thackeray. "Distinct Phospholipase C-γ-Dependent Signaling Pathways in the Drosophila Eye and Wing Are Revealed by a New small wing Allele." Genetics 164, no. 2 (June 1, 2003): 553–63. http://dx.doi.org/10.1093/genetics/164.2.553.

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Abstract The Drosophila genome contains a single phospholipase C-γ (PLC-γ) homolog, encoded by small wing (sl), that acts as an inhibitor of receptor tyrosine kinase (RTK) signaling during photoreceptor R7 development. Although the existing sl alleles behave genetically as nulls, they may still produce truncated Sl products that could in theory still provide limited PLC-γ function. Both to identify a true null allele and to probe structure-function relationships in Sl, we carried out an F1 screen for new sl mutations and identified seven new alleles. Flies homozygous for any of these alleles are viable, with the same short-wing phenotype described previously; however, two of the alleles differ from any of those previously isolated in the severity of the eye phenotype: sl9 homozygotes have a slightly more extreme extra-R7 phenotype, whereas sl7 homozygotes have an almost wild-type eye. We determined the mutant defect in all seven alleles, revealing that sl9 is a molecular null due to a very early stop codon, while sl7 has a missense mutation in the highly conserved Y catalytic domain. Together with in vitro mutagenesis of the residue affected by the sl7 mutation, these results confirm the role of Sl in RTK signaling and provide evidence for two genetically separable PLC-γ-dependent pathways affecting the development of the eye and the wing.
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Pinto, B., M. Jolly, A. Dhooria, S. Grover, J. M. Raj, H. Devilliers, and A. Sharma. "Hindi LupusPRO: cross cultural validation of disease specific patient reported outcome measure of lupus." Lupus 28, no. 13 (October 21, 2019): 1534–40. http://dx.doi.org/10.1177/0961203319880340.

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Background LupusPRO is a SLE specific patient reported outcomes measure developed and validated in the USA. This study aimed to validate the Hindi version of LupusPRO in systemic lupus erythematosus (SLE) patients in India. Methods Disease activity and damage were assessed using SELENA–SLEDAI and SLICC/ACR damage Index respectively. Demographic and clinical features were recorded. The Hindi Version of LupusPRO and 36-Item Short Form Health Survey (SF-36) were administered for assessment of quality of life. Depression, anxiety and fatigue were assessed using Patient Health Questionnaire 9 (PHQ9), Generalized Anxiety Disorder 7 (GAD7) and Fatigue Severity Scale (FSS) respectively. Internal consistency reliability, test-retest reliability, convergent and discriminant validity (against corresponding domains of the SF-36, fatigue, depression and anxiety), criterion validity (against disease activity and damage) and known group validity were tested. Results A total of 144 (140 females) patients with SLE with a mean age of 32.48 ± 7.26 years participated in the study. The median (interquartile range) SELENA SLEDAI was 2 (5.5). The internal consistency reliability of the LupusPRO domains was >0.7 for most domains (except for lupus symptoms, lupus medication, procreation and social support).We noted good convergent validity of LupusPRO domains with corresponding domains of SF-36, pain vitality with fatigue (FSS) and emotional health domain with depression (PHQ9) and anxiety (GAD7). Criterion validity of lupus symptoms with disease activity was observed. Known group validity of the LupusPRO domains with patient reported health status was observed. Confirmatory factor analysis showed a good fit. Conclusion The Hindi LupusPRO has fair psychometric properties among Indian patients with SLE.
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Simm, Dominic, and Martin Kollmar. "Waggawagga-CLI: A command-line tool for predicting stable single α-helices (SAH-domains), and the SAH-domain distribution across eukaryotes." PLOS ONE 13, no. 2 (February 14, 2018): e0191924. http://dx.doi.org/10.1371/journal.pone.0191924.

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Johnson, Mark D. "Planning in L1 and L2 writing: Working memory, process, and product." Language Teaching 53, no. 4 (June 23, 2020): 433–45. http://dx.doi.org/10.1017/s0261444820000191.

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The study of planning in second language (L2) writing research is heavily influenced by two research domains: (a) early research on cognition in first language (L1) composing processes and (b) second language acquisition (SLA) research. The first research domain has been instrumental in determining the specific systems and processes involved in composing and has led to widely accepted models of L1 writing (Bereiter & Scardamalia, 1987*; Flower & Hayes, 1980*; Hayes, 1996, 2012) as well as a widely accepted model of the interaction between working memory and L1 writing systems (Kellogg, 1996*; Kellogg, Whiteford, Turner, Cahill, & Mertens, 2013). The influence of these early studies is still felt in process approaches to composition instruction commonly implemented in L1 and L2 writing classes. The second research domain—SLA and more specifically task-based language teaching/learning—has come to view planning as a feature of task complexity that can be manipulated to facilitate the production of language that is complex (syntactically and/or lexically), accurate, and/or fluent (Robinson, 2011*; Skehan, 1998*; Skehan & Foster, 2001). This research timeline traces the study of planning in L2 writing in each of these domains by reviewing key L1 and L2 writing research over the last 30-plus years and by highlighting each study's findings. Prior to presenting the timeline, the following sections provide backgrounds in each of the domains noted above and situate planning within those domains.
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Pokorná, Jarmila, and Eva Večerková. "Trade name and trademark versus domain." Acta Universitatis Agriculturae et Silviculturae Mendelianae Brunensis 61, no. 4 (2013): 1069–76. http://dx.doi.org/10.11118/actaun201361041069.

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Internet domains have become an integral part of our lives, so one can easily understand that during their use, conflicts can arise, whose participants will search for rules enabling resolution of conflicts. Since the domain name is a replacement of the computer IP address, in the technical sense of the word, this does not concern for domain names a commercial name or brand, because it primarily does not belong to a person in the legal sense of the word and does not serve for its individualization. The average user regularly affiliates domain names with a person offering goods or services on the relevant Website. Domain names used by entrepreneurs in their business activity are often chosen so that the second-level domain (SLD) would use words that form the trade name of corporations formed of trading companies. This fact brings domain names close to such designations that serve the individualization of persons or products, especially the trademarks and the commercial name. Domains can come into conflict with the rights to designations, especially trademarks and commercial names. Court practice is resolving these conflicts using rules for unfair competition, or rules for protection of commercial names and trademarks, but it is not ruled out that in the future, special legal regulation of domain names could be established.
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Zirkzee, E. J. M., M. E. Ndosi, T. P. M. Vliet Vlieland, and J. J. L. Meesters. "Measuring educational needs among patients with systemic lupus erythematosus (SLE) using the Dutch version of the Educational Needs Assessment Tool (D-ENAT)." Lupus 23, no. 13 (July 24, 2014): 1370–76. http://dx.doi.org/10.1177/0961203314544188.

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Objective The Educational Needs Assessment Tool (ENAT) was developed in the United Kingdom (UK) to systematically assess the educational needs of patients with rheumatic diseases. The aim of the present study was to describe the educational needs of Dutch patients with systemic lupus erythematosus (SLE) by means of a Dutch version of the ENAT (D-ENAT). Methods The D-ENAT was sent to a random sample of 244 SLE patients registered at the outpatient clinic of a university hospital. D-ENAT consists of 39 items in seven domains. The D-ENAT domain scores range from 0–16 to 0–28 (higher scoring equals higher educational needs) depending of the number of items in the domain. A total D-ENAT score (0–156) is calculated by summing all 39 items. In addition, age, disease duration, gender, educational level, present information need (yes/no) and the extent of information need (1–4: nothing–everything) were recorded. Univariate regression analysis was used to examine the D-ENAT’s potential determinants. Results The response rate was 122 out of 244 (50%). The mean (% of maximum score) educational needs scores were 56% for ‘D-ENAT total score’, 62% for ‘Self-help measures’, 60% for ‘Disease process’, 58% for ‘Feelings’, 56% for ‘Treatments’, 50% for ‘Movement’, 49% for ‘Support systems’ and 46% for ‘Managing pain’. Being female was significantly associated with higher scoring on the D-ENAT total score (β 23.0; 95% CI 5.9, 40.3). Conclusion SLE patients demonstrated substantial educational needs, especially in the domains: ‘Self-help measures’, ‘Disease process’ and ‘Feelings’. The validity and practical applicability of the D-ENAT to make an inventory of SLE patients’ educational needs requires further investigation.
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Weber, Mary M., Nicholas F. Noriea, Laura D. Bauler, Jennifer L. Lam, Janet Sager, Jordan Wesolowski, Fabienne Paumet, and Ted Hackstadt. "A Functional Core of IncA Is Required for Chlamydia trachomatis Inclusion Fusion." Journal of Bacteriology 198, no. 8 (February 16, 2016): 1347–55. http://dx.doi.org/10.1128/jb.00933-15.

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ABSTRACTChlamydia trachomatisis an obligate intracellular pathogen that is the etiological agent of a variety of human diseases, including blinding trachoma and sexually transmitted infections. Chlamydiae replicate within a membrane-bound compartment, termed an inclusion, which they extensively modify by the insertion of type III secreted proteins called Inc proteins. IncA is an inclusion membrane protein that encodes two coiled-coil domains that are homologous to eukaryotic SNARE (solubleN-ethylmaleimide-sensitive factor attachment receptor) motifs. Recent biochemical evidence suggests that a functional core, composed of SNARE-like domain 1 (SLD-1) and part of SNARE-like domain 2 (SLD-2), is required for the characteristic homotypic fusion ofC. trachomatisinclusions in multiply infected cells. To verify the importance of IncA in homotypic fusion inChlamydia, we generated anincA::blamutant. Insertional inactivation ofincAresulted in the formation of nonfusogenic inclusions, a phenotype that was completely rescued by complementation with full-length IncA. Rescue of homotypic inclusion fusion was dependent on the presence of the functional core consisting of SLD-1 and part of SLD-2. Collectively, these results confirmin vitromembrane fusion assays identifying functional domains of IncA and expand the genetic tools available for identification of chlamydia with a method for complementation of site-specific mutants.IMPORTANCEChlamydia trachomatisreplicates within a parasitophorous vacuole termed an inclusion. The chlamydial inclusions are nonfusogenic with vesicles in the endocytic pathway but, in multiply infected cells, fuse with each other to form a single large inclusion. This homotypic fusion is dependent upon the presence of a chlamydial inclusion membrane-localized protein, IncA. Specificity of membrane fusion in eukaryotic cells is regulated by SNARE (solubleN-ethylmaleimide sensitive factor attachment receptor) proteins on the cytosolic face of vesicles and target membranes. IncA contains two SNARE-like domains. Newly developed genetic tools for the complementation of targeted mutants inC. trachomatisare used to confirm the minimal requirement of SNARE-like motifs necessary to promote the homotypic fusion of inclusions.
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JOLLY, MEENAKSHI, SIMON A. PICKARD, RACHEL A. MIKOLAITIS, ROGER A. RODBY, WINSTON SEQUEIRA, and JOEL A. BLOCK. "LupusQoL-US Benchmarks for US Patients with Systemic Lupus Erythematosus." Journal of Rheumatology 37, no. 9 (August 17, 2010): 1828–33. http://dx.doi.org/10.3899/jrheum.091443.

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Objective.The LupusQoL-US instrument was recently validated in the US. We studied the benchmarks for a US patient cohort with systemic lupus erythematosus (SLE) and relevant demographic and disease correlates.Methods.LupusQoL-US was administered to 185 patients with SLE. Demographic data (age, sex, ethnicity, marital status) and disease features (duration, disease activity and damage) were assessed simultaneously. Descriptive statistics were obtained. LupusQoL-US domain scores were calculated, and compared by sex, ethnicity, and marital status using nonparametric tests. Correlation between LupusQoL-US domains and age, disease duration, disease activity, and disease damage were obtained.Results.Mean age of patients was 42.2 ± 14.5 years; 94% of subjects were women. African American patients comprised 60% of the study cohort. The most affected domains were Fatigue and Physical Health. The least affected was Intimate Relationships. Age correlated with Physical Health, Pain, and Body Image (r = 0.15–0.18). Differences were observed based on sex and marital status, but not by ethnicity; there the LupusQoL-US correlated inversely with disease activity (r = −0.001 to −0.36) and damage (r = −0.003 to −0.40).Conclusion.All domains of the LupusQoL-US based health related quality of life (HRQOL) were affected adversely. HRQOL varied by age, sex, and marital status in our SLE cohort.
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Eckhoff, Hanne Martine, Olga A. Thomason, and Peter de Swart. "Mapping out the Source domain." Studies in Language 37, no. 2 (June 7, 2013): 302–55. http://dx.doi.org/10.1075/sl.37.2.03eck.

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This paper takes a strictly empirical approach to the encoding of spatial notions in the four ancient Indo-European languages Ancient Greek, Latin, Gothic and Old Church Slavonic. By generating semantic maps on the basis of parallel corpus data, without any semantic pre-analysis, we use methods well tested in typology to study the basic divisions in the spatial domain in the four closely-related languages, and to determine the finer subdivisions within the Source domain. We find that the four languages are similar, but clearly independent of each other, each carving up the spatial domain in different ways. We also find substantial encoding overlaps between the Source and Location domains.
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Shi, Jian, and Weihong Qian. "Connection between Anomalous Zonal Activities of the South Asian High and Eurasian Summer Climate Anomalies." Journal of Climate 29, no. 22 (November 1, 2016): 8249–67. http://dx.doi.org/10.1175/jcli-d-15-0823.1.

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Abstract Using the daily mean anomalies of atmospheric variables from the NCEP Reanalysis-1 (NCEP R1), this study reveals the connection between anomalous zonal activities of the South Asian high (SAH) and Eurasian climate anomalies in boreal summer. An analysis of variance identifies two major domains with larger geopotential height variability located in the eastern and western flanks of the SAH at around 100 and 150 hPa, respectively. For both eastern and western domains, extreme events are selected during 1981–2014 when normalized height anomalies are greater than 1.0 (less than −1.0) standard deviation for at least 10 consecutive days. Based on these events, four SAH modes that include strong and weak Tibetan modes (STM and WTM, respectively) and strong and weak Iranian modes (SIM and WIM, respectively) are defined to depict the zonal SAH features. The positive composite in the eastern (western) domain indicates the STM (SIM) manifests a robust wavelike pattern with an anomalous low at 150 hPa, and surface cold and wet anomalies over Mongolia and northern China (Kazakhstan and western Siberia) are surrounded by three anomalous highs at 150 hPa and surface warm and dry anomalies over Eurasia. Opposite distributions are also evident in the negative composites of the two domains (WTM and WIM). The surface air temperature anomalies are the downward extension of an anomalous air column aloft while the precipitation anomalies are directly associated with the height anomalies above the air column.
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Kern, Justin, Rosemarie Wilton, Rongguang Zhang, T. Andrew Binkowski, Andrzej Joachimiak, and Olaf Schneewind. "Structure of Surface Layer Homology (SLH) Domains fromBacillus anthracisSurface Array Protein." Journal of Biological Chemistry 286, no. 29 (May 13, 2011): 26042–49. http://dx.doi.org/10.1074/jbc.m111.248070.

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