Relevant bibliographies by topics / Maltose binding protein (MBP)

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Academic literature on the topic 'Maltose binding protein (MBP)'

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Published: 4 June 2021
Last updated: 6 September 2023

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Journal articles on the topic "Maltose binding protein (MBP)"

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Morón, Carlos, Enrique Tremps, Alfonso Garcia, and Jose Andrés Somolinos. "Development of an Electrochemical Maltose Biosensor." Key Engineering Materials 495 (November 2011): 116–19. http://dx.doi.org/10.4028/www.scientific.net/kem.495.116.

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In this work, electrochemical maltose biosensors based on mutants of the maltose binding protein (MBP) are developed. A rutheniumIIcomplex (RuII), which is covalently attached to MBP, serves as an electrochemical reporter of MBP conformational changes. Biosensors were made through direct attachment of RuIIcomplex modified MBP to gold electrode surfaces. The responses of some individual mutants were evaluated using square wave voltammetry. A maltose-dependent change in Faradic current and capacitance was observed. It is therefore demonstrated that biosensors using generically this family of bacterial periplasmic binding proteins (bPBP) can be made lending themselves to facile biorecognition element preparation and low cost electrochemical transduction.
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Reich-Slotky, Ronit, Cynthia Panagiotidis, Moraima Reyes, and Howard A. Shuman. "The Detergent-Soluble Maltose Transporter Is Activated by Maltose Binding Protein and Verapamil." Journal of Bacteriology 182, no. 4 (February 15, 2000): 993–1000. http://dx.doi.org/10.1128/jb.182.4.993-1000.2000.

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ABSTRACT The maltose transporter FGK2 complex of Escherichia coli was purified with the aid of a glutathioneS-transferase molecular tag. In contrast to the membrane-associated form of the complex, which requires liganded maltose binding protein (MBP) for ATPase activity, the purified detergent-soluble complex exhibited a very high level of ATPase activity. This uncoupled activity was not due to dissociation of the MalK ATPase subunit from the integral membrane protein MalF and MalG subunits. The detergent-soluble ATPase activity of the complex could be further stimulated by wild-type MBP but not by a signaling-defective mutant MBP. Wild-type MBP increased the V max of the ATPase 2.7-fold but had no effect on the Km of the enzyme for ATP. When the detergent-soluble complex was reconstituted in proteoliposomes, it returned to being dependent on MBP for activation of ATPase, consistent with the idea that the structural changes induced in the complex by detergent that result in activation of the ATPase are reversible. The uncoupled ATPase activity resembled the membrane-bound activity of the complex also with respect to sensitivity to NaN3, as well as a mercurial,p-chloromercuribenzosulfonic acid. Verapamil, a compound that activates the ATPase activity of the multiple drug resistance P-glycoprotein, activated the maltose transporter ATPase as well. The activation of this bacterial transporter by verapamil suggests that a structural feature that is conserved among both eukaryotic and prokaryotic ATP binding cassette transporters is responsible for this activation.
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Braitsch, Michaela, Hanspeter Kählig, Georg Kontaxis, Michael Fischer, Toshinari Kawada, Robert Konrat, and Walther Schmid. "Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR." Beilstein Journal of Organic Chemistry 8 (March 27, 2012): 448–55. http://dx.doi.org/10.3762/bjoc.8.51.

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A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces.
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Williard, Alexander C., Hannah J. Switzer, Christina A. Howard, Rui Yin, Brent L. Russell, Ritwik Sanyal, Shaun Yu, et al. "Protein Modification Employing Non-Canonical Amino Acids to Prepare SUMOylation Detecting Bioconjugates." Pharmaceutics 14, no. 12 (December 16, 2022): 2826. http://dx.doi.org/10.3390/pharmaceutics14122826.

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Protein modification with non-canonical amino acids (ncAAs) represents a useful technology to afford homogenous samples of bioconjugates with site-specific modification. This technique can be directly applied to the detection of aberrant SUMOylation patterns, which are often indicative of disease states. Modified SUMO-trapping proteins, consisting of a catalytically inactive ULP1 fragment (UTAG) fused to the maltose-binding protein MBP, are useful reagents for the binding and labeling of SUMOylated proteins. Mutation of this UTAG fusion protein to facilitate amber suppression technologies for the genetic incorporation of ncAAs was assessed to provide a functional handle for modification. Ultimately, two sites in the maltose-binding protein (MBP) fusion were identified as ideal for incorporation and bioconjugation without perturbation to the SUMO-trapping ability of the UTAG protein. This functionality was then employed to label SUMOylated proteins in HeLa cells and demonstrate their enrichment in the nucleus. This modified UTAG-MBP-ncAA protein has far-reaching applications for both diagnostics and therapeutics.
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Waugh, David S. "The remarkable solubility-enhancing power of Escherichia coli maltose-binding protein." Postępy Biochemii 62, no. 3 (November 15, 2016): 377–82. http://dx.doi.org/10.18388/pb.2016_41.

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A common problem encountered during the production of recombinant proteins, particularly in bacteria, is their tendency to accumulate in an insoluble and inactive form (i.e., as inclusion bodies). Although sometimes it is possible to convert the aggregated material into native, biologically active protein, this is a time-consuming, costly, and uncertain undertaking. Consequently, a general means of circumventing the formation of inclusion bodies is highly desirable. During the 1990s, it was serendipitously discovered that certain highly soluble proteins have the ability to enhance the solubility of their fusion partners, thereby preventing them from forming insoluble aggregates. In the ensuing years, Escherichia coli maltose-binding protein (MBP) has emerged as one of the most effective solubility enhancers. Moreover, once rendered soluble by fusion to MBP, many proteins are able to fold into their biologically active conformations. This brief review article focuses on our current understanding of what makes MBP such an effective solubility enhancer and how it facilitates the proper folding of its fusion partners.
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Carter, Eric L., and Robert P. Hausinger. "Characterization of the Klebsiella aerogenes Urease Accessory Protein UreD in Fusion with the Maltose Binding Protein." Journal of Bacteriology 192, no. 9 (March 5, 2010): 2294–304. http://dx.doi.org/10.1128/jb.01426-09.

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ABSTRACT Assembly of the Klebsiella aerogenes urease metallocenter requires four accessory proteins, UreD, UreE, UreF, and UreG, to effectively deliver and incorporate two Ni2+ ions into the nascent active site of the urease apoprotein (UreABC). Each accessory protein has been purified and characterized with the exception of UreD due to its insolubility when it is overproduced in recombinant cells. In this study, a translational fusion was made between the maltose binding protein (MBP) and UreD, with the resulting MBP-UreD found to be soluble in Escherichia coli cell extracts and able to complement a ΔureD-urease cluster in this host microorganism. MBP-UreD was purified as a large multimer (>670 kDa) that bound approximately 2.5 Ni2+ ions (Kd of ∼50 μM, where Kd is the dissociation constant) per UreD protomer according to equilibrium dialysis measurements. Zn2+ directly competes with 10-fold higher affinity (∼4 Zn2+ ions per protomer; Kd of 5 μM) for the Ni2+ binding sites. MBP pulldown experiments demonstrated that the UreD domain of MBP-UreD formed in vivo complexes with UreF, UreG, UreF plus UreG, or UreABC when these proteins were overproduced in the same E. coli cells. In addition, a UreABC-(MBP-UreD)-UreFG complex was observed in cells producing all urease components. Comparative in vitro binding experiments with purified proteins demonstrated an approximate 1:1 binding ratio between the UreD domain of MBP-UreD and the UreF domain of the UreEF fusion, only weak or transient interaction between MBP-UreD and UreG, and no binding with UreABC. These studies are the first to describe the properties of purified UreD, and they extend our understanding of its binding partners both in vitro and in the cell.
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Munson, George P., Lisa G. Holcomb, Heather L. Alexander, and June R. Scott. "In Vitro Identification of Rns-Regulated Genes." Journal of Bacteriology 184, no. 4 (February 15, 2002): 1196–99. http://dx.doi.org/10.1128/jb.184.4.1196-1199.2002.

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ABSTRACT To identify Rns-regulated genes, a maltose binding protein (MBP)-Rns fusion protein was used to isolate DNA fragments from enterotoxigenic Escherichia coli genomic DNA that carry Rns binding sites. In vivo transcription fusion analysis shows that Rns positively regulates the expression of the open reading frame of yiiS, which lies immediately downstream of one MBP-Rns-bound fragment.
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Li, B. W., R. Chandrashekar, and G. J. Weil. "Vaccination with recombinant filarial paramyosin induces partial immunity to Brugia malayi infection in jirds." Journal of Immunology 150, no. 5 (March 1, 1993): 1881–85. http://dx.doi.org/10.4049/jimmunol.150.5.1881.

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Abstract Vaccination with irradiated infective larvae induces partial protective immunity to infection with the filarial nematode Brugia malayi in jirds. Prior studies have shown that such immunization stimulates a much stronger antibody response to recombinant and native filarial paramyosin than that seen after normal infection. To determine whether vaccination with recombinant paramyosin could induce protective immunity to larval challenge, jirds were immunized with either B. malayi paramyosin and maltose binding protein (BM5-MBP) (fusion protein of B. malayi paramyosin and maltose-binding protein), MBP alone, or recombinant Dirofilaria immitis paramyosin. Animals were challenged with 100 infective larvae s.c. 8 wk after the second immunization. Necropsies were performed 16 wk after challenge. Vaccination with BM5-MBP induced significant protective immunity; adult worm recoveries, worm lengths, and blood microfilaria counts were reduced in the BM5-MBP group relative to the MBP control group. The reductions in adult worm recoveries (43%) and female worm lengths (10%) were statistically significant (p < 0.05). Interestingly, protective immunity was not induced by immunization with D. immitis paramyosin. Additional studies are needed to identify mechanisms involved in protective immunity induced by BM5-MBP and to understand the differential activity of the two closely related recombinant paramyosin proteins in this model.
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THOMAS, Stephen, Salvador SORIANO, Clive d'SANTOS, and George BANTING. "Expression of recombinant rat myo-inositol 1,4,5-trisphosphate 3-kinase B suggests a regulatory role for its N-terminus." Biochemical Journal 319, no. 3 (November 1, 1996): 713–16. http://dx.doi.org/10.1042/bj3190713.

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We have expressed rat myo-inositol 1,4,5-trisphosphate (IP3) 3-kinase B as both a full-length, recombinant, non-fusion protein and a full-length, recombinant, fusion protein with maltose-binding protein (MBP) in Escherichia coli. The fusion protein with MBP is soluble, binds calmodulin and is enzymically active whereas the non-fusion protein is insoluble and does not bind calmodulin unless co-expressed with bacterial chaperone proteins (either GroES and GroEL, or DnaK, DnaJ and GrpE). However, soluble, calmodulin-binding non-fusion IP3 3-kinase B is enzymically inactive. The catalytic domain of the enzyme has previously been shown to reside near the C-terminus; the results we present suggest an auto-regulatory role for the N-terminus.
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Fernandez, Stefan, Dupeh R. Palmer, Monika Simmons, Peifang Sun, John Bisbing, Sasha McClain, Sachin Mani, Timothy Burgess, Vicky Gunther, and Wellington Sun. "Potential Role for Toll-Like Receptor 4 in Mediating Escherichia coli Maltose-Binding Protein Activation of Dendritic Cells." Infection and Immunity 75, no. 3 (January 12, 2007): 1359–63. http://dx.doi.org/10.1128/iai.00486-06.

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ABSTRACT The Escherichia coli maltose-binding protein (MBP) is used to increase the stability and solubility of proteins in bacterial protein expression systems and is increasingly being used to facilitate the production and delivery of subunit vaccines against various pathogenic bacteria and viruses. The MBP tag is presumed inert, with minimum effects on the bioactivity of the tagged protein or its biodistribution. However, few studies have characterized the immunological attributes of MBP. Here, we analyze the phenotypic and functional outcomes of MBP-treated dendritic cells (DCs) and show that MBP induces DC activation and production of proinflammatory cytokines (interleukin-1β [IL-1β], IL-6, IL-8, tumor necrosis factor alpha, and IL-12p70) within 24 h and strongly increases Iκβ phosphorylation in treated cells. Interestingly, phosphorylation of Iκβ was largely abrogated by the addition of anti-human Toll-like receptor 4 (TLR4) antibodies, indicating that MBP activates signaling for DC maturation via TLR4. Consistent with this hypothesis, MBP activated the TLR4-expressing cell line 293-hTLR4A but not control cultures to secrete IL-8. The observed data were independent of lipopolysaccharide contamination and support a role for TLR4 in mediating the effects of MBP. These results provide insight into a mechanism by which MBP might enhance immune responses to vaccine fusion proteins.
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Dissertations / Theses on the topic "Maltose binding protein (MBP)"

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Li, Zhiguo. "Structure, secretion, and proteolysis study of MBP-containing heterologous proteins in Pichia pastoris." Scholarly Commons, 2010. https://scholarlycommons.pacific.edu/uop_etds/2415.

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The E. coli maltose binding protein (MBP) has been utilized as a translational fusion partner to improve the expression of foreign proteins made in E. coli. When located N -terminal to its cargo protein, MBP increases the solubility of intracellular proteins and improves the export of secreted proteins in bacterial systems. We initially explored whether MBP would have the same effect in the methylotrophic yeast Pichia pastoris , a popular eukaryotic host for heterologous protein expression. When MBP was fused as an N -terminal partner to several C -terminal cargo proteins expressed in this yeast, proteolysis occurred between the two peptides, and MBP reached the extracellular region unattached to its cargo. However, in two of three instances, the cargo protein reached the extracellular region as well, and its initial attachment to MBP enhanced its secretion from the cell. Extensive mutagenesis of the spacer region between MBP and its C -terminal cargo protein could not inhibit the cleavage although it did cause changes in the protease target sites in the fusion proteins, as determined by mass spectrometry. Taken together, these results suggested that an uncharacterized P. pastoris protease attacked at different locations in the region C -terminal of the MBP domain, including the spacer and cargo regions, but the MEP domain could still act to enhance the secretion of certain cargo proteins. The attempt to identify the unknown protease was unsuccessful. However, in contrast to other fusion partners, MBP was secreted with the cargo when it was fused as a C -terminal peptide to an N -terminal cargo protein. These studies provide insights into the role of proteases and fusion partners in the secretory mechanism of P. pastoris , suggesting new strategies to optimize this expression system.
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Gomes, Pâmela Oliveira Martins. "Imobilização de Galectina-1 e Galectina-1 fusionada com Maltose Binding Protein (MBP-Gal-1) sobre superfície eletropolimerizada com [N-(3-Pirrol-1-il-propil)-4,4\'-bipiridina] (PPB) para a construção de um biossensor de lactose." Universidade de São Paulo, 2018. http://www.teses.usp.br/teses/disponiveis/59/59138/tde-11102018-100311/.

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As galectinas são proteínas que se ligam a -galactosídeos por meio do domínio de reconhecimento de carboidratos (CRD do inglês, Carbohydrate Recognition Domain) e que participam de vários processos de reconhecimento celular, sinalização, adesão e destinação intracelular de proteínas recém-sintetizadas. A primeira galectina, Galectina-1 (Gal-1), foi identificada em 1976 e possui um papel importante na progressão e proliferação tumoral, angiogênese, resistência a drogas e processos inflamatórios. Assim, é interessante a construção de dispositivos com Galectinas imobilizadas, preservando o CRD para o estudo de mecanismos e/ou detecção destas doenças. Neste trabalho a produção e caracterização de uma proteína recombinante fusionada, a MBP-Gal-1, foi descrita. A proposta do projeto foi pautada na hipótese de que a fusão da MBP à Gal-1 seria uma excelente estratégia para imobilização orientada da proteína de interesse, (Gal-1), sobre eletrodos modificados com filme polimérico, auxiliando na preservação da atividade da biomolécula imobilizada para posterior desenvolvimento de biossensor. A MBP-Gal-1 foi purificada utilizando 2 colunas com resinas diferentes: sepharose/lactose e amilose onde foi possível comprovar a atividade/preservação dos sítios ativos da Gal-1 e MBP, respectivamente. A proteína fusionada teve seu estado oligomérico estimado e seu raio hidrodinâmico determinado pela técnica Espalhamento Dinâmico da Luz sendo que a mesma se encontrava na forma monomérica com raio hidrodinâmico de 4 nm ± 1,26. A massa molecular de 57,834 kDa para a MBP-Gal-1 foi obtida através da técnica de Espectrometria de Massas MALDI-TOF/TOF. O PPB, material polimérico empregado na modificação dos eletrodos de carbono vítreo e ouro, foi sintetizado e teve sua estrutura confirmada pela técnica de Ressonância Magnética Nuclear; este material foi utilizado para a realização dos ensaios de Espectroscopia de Impedância Eletroquímica (EIE) e Ressonância de Plásmons de Superfície (SPR) para a construção do biossensor. Os ensaios EIE utilizando eletrodo de carbono vítreo modificado com PPB mostraram a importância da imobilização orientada da sonda (MBP-Gal-1) para garantir a preservação da atividade biológica da mesma, uma vez que os resultados relativos ao aumento da Resistência à Transferência de Carga (Rtc), após adição do alvo (lactose), foram da ordem de 80% a mais para a proteína fusionada MBP-Gal-1 quando comparados à proteína nativa Gal-1. Os ensaios de SPR revelaram maior SPR efetiva para a MBP-Gal-1 imobilizada sobre superfície de eletrodo Au-SPR modificado com PPB o qual apresentou bom desempenho na detecção de lactose.
Galectins are proteins that bind to -galactosides by the Carbohydrate Recognition Domain (CRD) and participate in various processes of cell recognition, signaling, adhesion and intracellular destination of newly synthesized proteins. The first galectin, Galectin-1 (Gal-1), was identified in 1976 and plays an important role in tumor progression and proliferation, angiogenesis, drug resistance and inflammatory processes. Thus, it is interesting to desing devices with immobilized Galectins, preserving its CRD for the study of mechanisms and /or detection of such diseases. In this work the production and characterization of a fused recombinant protein, MBP-Gal-1, has been described. The project goal was based on the hypothesis that the fusion of the MBP to Gal-1 would be an excellent strategy for oriented immobilization of the protein of interest, (Gal-1), onto PPB- modified electrodes, promoting the preservation of the biomolecule activity immobilized for further development of a biosensor. MBP-Gal-1 was purified using 2 columns with different resins: sepharose/lactose and amylose and it was possible to prove the activity/preservation of both CRDs from Gal-1 and MBP, respectively. Dynamic Light Scattering showed that MBP-Gal-1 was in a monomeric form and with a hydrodynamic radius of 4 nm ± 1,26. The molecular mass of 57.834 kDa for MBP-Gal-1 was obtained by the technique of MALDI-TOF/TOF Mass Spectrometry. The PPB, a polymeric material used in the modification of glassy carbon and gold electrodes, was synthesized and its structure was confirmed by the Nuclear Magnetic Resonance (NMR); this material was used to carry out the Electrochemical Impedance Spectroscopy (EIS) and Surface Plasmon Resonance (SPR) tests for the construction of the biosensor. EIS assays using PPB-modified glassy carbon electrode showed the importance of probe-immobilization (MBP-Gal-1) to ensure the preservation of the biological activity of the protein, since the results related to the increase in Resistance of Charge Transfer (Rct), after addition of the target (lactose), were 80% higher for the fused protein MBP-Gal-1 when compared to the Gal-1 native-form protein. The SPR assays revealed a greater effective SPR for MBP-Gal-1 immobilized onto PPB-modified Au-SPR electrode surface which showed good performance in the detection of lactose.
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Zhang, Xiaochen. "The binding modes of maltose binding protein with different ligands studied by NMR." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp04/mq29813.pdf.

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Zhang, Xiaochen 1969. "The binding modes of maltose binding protein with different ligands studied by NMR /." Thesis, McGill University, 1997. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=27438.

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Maltose Binding Protein (MBP) of Escherichia Coli, a kind of periplasmic protein, can bind its ligands interacting predominantly either with their anomeric end (end-on binding) or with the middle of the maltodextrin chain (middle binding). Using NMR spectroscopy, we have studied the modes by which maltose, linear maltodextrin and some derivatives like $ beta$-cyclodextrin bind to MBP. 1D proton difference spectra and 2D HSQC proton-nitrogen correlation spectra were acquired of MBP in the presence of different ligands. Spectra with linear maltodextrins showed many common features and were distinctly different from those of MBP with $ beta$-cyclodextrin. 2D HSQC spectra suggest further that MBP- $ beta$-cyclodextrin adopts an open form conformation similar to that of ligand free MBP because of the surprisingly similarity of their spectra. Ligands such as $ beta$-cyclodextrin, can not be transported into the cyto-plasm but have high affinity for MBP, multiple $ alpha$(1-4) linkages and no reducing end. These ligands bind to MBP mainly by the middle binding mode. This suggests that this mode determines high affinity binding of ligand to MBP, but doesn't produce a physiologically active complex.
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Shahir, Shafinaz. "Engineering and the maltose binding protein for metal ions sensing." Thesis, Imperial College London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.434921.

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Tabona, Peter. "The role and regulation of mannose binding protein : studies in transgenic mice." Thesis, Imperial College London, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.297298.

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Day, Matthew. "Production and analysis of escherichia coli groE chaperonins." Thesis, Birkbeck (University of London), 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.243960.

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Merstorf, Céline. "Stabilité conformationnelle et dépliement de la protéine MalE : Étude par nanopore et par spectroscopie RMN." Thesis, Cergy-Pontoise, 2011. http://www.theses.fr/2011CERG0571/document.

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Nous avons étudié le couplage dépliement-transport de la Maltose Binding Protein (MBP ou MalE), une protéine périplasmique d'E. Coli et d'un mutant instable, le MalE219, en fonction de la concentration d'un agent dénaturant, le chlorure de guanidium (GdnHCl) à l'échelle de la molécule unique. La technique utilisée est basée sur la détection électrique du transport de macromolécules à travers un nanopore protéique (l'Aérolysine d'Aeromonas Hydrophila) inséré dans une bicouche lipidique plane. Les résultats obtenus ont été comparés à ceux obtenus lors d'une précédente étude réalisée à travers un autre nanopore protéique, l'alpha-hémolysine du Staphylocoque doré, de géométrie et de charge nette différente. Nous avons montré l'existence de temps courts et longs de blocage du courant associés à des protéines dépliées ou partiellement repliées. La fréquence des blocages du courant permet d'obtenir la fraction de protéine dépliée passant à travers le pore en fonction de la concentration en GdnHCl. Les courbes de dénaturation obtenues avec les deux pores montrent un comportement sigmoïdale très similaire. Le type de pore n'influence donc pas la dénaturation des protéines, mais uniquement leur dynamique de transport. En revanche, la courbe de dénaturation du mutant instable présente un déplacement vers les concentrations plus faibles en GdnHCl. Il a été montré également que la présence du maltose comme ligand sur le MalE219 stabilise nettement sa structure. Pour La MBP, les temps de blocages longs diminuent avec l'augmentation de la concentration de GdnHCl montrant une dynamique de transition vitreuse . Cette technique est appropriée à l'étude du dépliement et des changements de conformation de protéines, mais ne permet pas d'obtenir des informations structurales sur les états intermédiaires de repliement. Ainsi, la spectroscopie RMN a été utilisée pour tenter de caractériser ces états intermédiaires de repliement, notamment par la méthode d'échange proton-deutérium. Elle consiste à suivre les cinétiques d'échange des résidus de la protéine sur des spectres 2D 1H-15N HSQC à différentes concentrations de GdnHCl.Ainsi 180 résidus sur les 370 que compte la MBP ont été suivis lors de la dénaturation en présence de GdnHCl. Les deux hélices en C-terminal sont très accessibles au solvant et se dénaturent facilement. La MBP est composée de deux domaines globulaires, le domaine N-ter et le domaine C-ter. Les éléments de structures secondaires situés dans la zone intermédiaire entre les deux domaines (principalement des brins β) sont particulièrement affectés par l'agent dénaturant. D'autres structures secondaires dans les domaines globulaires sont très protégées et plutôt stables. Il est donc proposé que les protéines partiellement dépliées s'insèrent dans le pore par l'extrémité C-terminal et que des parties de structuration tertiaire restent stable entraînant le blocage du pore
We study the unfolding-transport mechanism of the Maltose Binding Protein (MBP or MalE), a periplasm protein of E. Coli and a destabilised variant, the MalE219, as the function of the concentration of denaturing agent, Guanidine Hydrochloride(GdnHCl) at the single molecule level. The technique is based on the electrical detection of the macromolecule transport through a nanometer-scale channel, Aerolysin channel, inserted into a planar lipid bilayer. Results obtained were compared to previous data with another channel, the alpha-Hemolysin. Both channels have different geometry and net charge.We show that we can distinguish unfolded states from partially folded ones with aerolysin pore.Unfolded proteins induce short current blockades, their duration is constant as a function of the concentration of denaturing agent. Partially folded proteins exhibit long blockades whose life times decrease as the concentration of GdnHCl increase, this indicates a possible glassy dynamics.The frequency of the short current blockades increases as the concentration of denaturing agent increases, following a sigmoidal denaturation curve.The unfolding curve of native MBP with Aerolysin pore is similar to the one previously measured with Hemolysin channel. The denaturation curve of the destabilized variant obtained with Aerolysin is shifted towards lower value of GdnHCl concentration in agreement with bulk measurements. We show also that the addition of maltose stabilizes the structure of MalE219. This nanopore recording technique is also suitable for the study of unfolding and conformation changes of proteins.In order to obtain structural informations that nanopore recording cannot provides, the structure of MBP along its denaturation curve was studied by NMR spectroscopy. The Hydrogen-exchange method known to be sensitive to folding intermediates was specially used. It consists in tracking hydrogen-deuterium exchange rates for amino on the 2D 1H-15N HSQC spectra.Thus, 180 residus of 370 for MBP was followed during denaturation in the presence of GdnHCl. The two last helices in C-terminal of MBP are accessible to the solvent and are denaturated easily. MBP is a two domains protein, N-ter domain and C-ter domain. It was found out that the C- and D-domain of MBP (mainly alpha-helices) could be relatively stable in presence of denaturing agent and that beta strands which make the link between the two domains would be affected by the denaturing agent. It was proposed that partially unfolded proteins enter the pore by the C-terminal end and that stable tertiary structure still present block the pore
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Sanchez, Lecaros Luis. "Cloning and expression of superoxide dismutase from Sarcoptes scabiei in Escherichia coli." Thesis, Uppsala University, Department of Medical Biochemistry and Microbiology, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-7428.

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Sarcoptes scabiei is a disease-causing parasitic mite of humans and animals that is prevalent worldwide. The parasite lives in burrows in the epidermis of its host. These burrows are formed by a combination of mechanical destruction by the mite and secretion of various factors.

The enzyme superoxide dismutase (SOD) catalyzes the dismutation of superoxide into oxygen and hydrogen peroxide. As such, it is an important antioxidant defense in nearly all cells exposed to oxygen. In this project, the enzyme was expressed in transformed Escherichia coli cells. The SOD cDNA from S. scabiei was ligated into two different expression vectors: pPU16 and pET-14b. The S. scabiei SOD open reading frame reported here is 696 nucleotides long and yields a protein with a molecular weight of  69.5 kDa. Only one of the constructs was successfully created, using pPU16. The construct was designated pPU110 and has a sequence coding for a hexahistidine tag downstream of the SOD cDNA and has a sequence coding for the maltose binding protein (MBP) upstream.

The expression plasmid pPU110 was verified by DNA-sequencing and the tested in different expression experiments. Analysis using SDS-PAGE showed that recombinant fusion SOD could be readily expressed in E.coli.

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Nickolaus, Chen [Verfasser], and Wolfgang E. [Akademischer Betreuer] Trommer. "The Molten Globule State of Maltose-Binding Protein: Structural Characterization by Electron Paramagnetic Resonance Spectroscopy / Chen Nickolaus ; Betreuer: Wolfgang E. Trommer." Kaiserslautern : Technische Universität Kaiserslautern, 2017. http://d-nb.info/1123572135/34.

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Book chapters on the topic "Maltose binding protein (MBP)"

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Berger, David K., Heung-Shick Lee, and Sydney Kustu. "A Maltose-Binding Protein-NIFA (MBP-NIFA) Fusion Activates Transcription from the Klebsiella Pneumoniae nifH Promoter in a Purified System: Stimulation by IHF." In New Horizons in Nitrogen Fixation, 435–41. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-017-2416-6_46.

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Pattenden, Leonard K., and Walter G. Thomas. "Amylose Affinity Chromatography of Maltose-Binding Protein." In Affinity Chromatography, 169–90. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-582-4_12.

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Lebendiker, Mario, and Tsafi Danieli. "Purification of Proteins Fused to Maltose-Binding Protein." In Methods in Molecular Biology, 281–93. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-913-0_15.

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Lebendiker, Mario, and Tsafi Danieli. "Purification of Proteins Fused to Maltose-Binding Protein." In Methods in Molecular Biology, 257–73. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6412-3_13.

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Kawasaki, Toshisuke, Motohiro Nonaka, and Nobuko Kawasaki. "Mannan-Binding Protein (MBP)-Ligand Glycans: A Novel Tissue Marker for Colorectal Carcinomas." In Glycoscience: Biology and Medicine, 1–8. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54836-2_60-1.

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Króliczewski, Jaroslaw, Udo Johanningmeier, and Andrzej Szczepaniak. "Heme Binding to an Apocytochrome b 6 Fused to Maltose-binding Protein Overexpressed in Escherichia coli." In Photosynthesis: Mechanisms and Effects, 1561–64. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_367.

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Betton, Jean-Michel. "Using Maltose-Binding Protein Fragment Complementation to Probe Protein-Protein Interactions by Co Expression in the RTS System." In Cell-Free Protein Expression, 143–49. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-59337-6_17.

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Kawasaki, Toshisuke, Motohiro Nonaka, and Nobuko Kawasaki. "Mannan-Binding Protein (MBP)-Ligand Glycans: Novel Tissue Marker Tissue tumor marker for Colorectal Carcinomas." In Glycoscience: Biology and Medicine, 1021–28. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_60.

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Króliczewski, Jarosław, and Andrzej Szczepaniak. "Localisation of Apocytochrome b 6 Fused to Expressed Periplasmic Maltose-binding Protein in Escherichia coli." In Photosynthesis: Mechanisms and Effects, 1557–60. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_366.

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Gubernator, Beata, Udo Johanningmeier, and Andrzej Szczepaniak. "Overproduction of a Spinach Rieske Fe-S Polypeptide Fused to Maltose-binding Protein in Escherichia coli." In Photosynthesis: Mechanisms and Effects, 1553–56. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_365.

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Conference papers on the topic "Maltose binding protein (MBP)"

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Toda, Atsushi, Kuriko Yamada, Shigeo Shibatani, Susumu Nishiguchi, Hiroaki Nakagawa, Masaki Kurogochi, and Shin-Ichiro Nishimura. "EXPRESSION OF BETA 1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE FROM STREPTOCOCCUS AGALACTIAE TYPE IA IN ESCHERICHIA COLI AS A FUSION WITH MALTOSE-BINDING PROTEIN." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.765.

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Wang, W., Y. Guo, H. Xing, and G. Tai. "Abstract P6-09-04: M2 macrophages induced by mammary carcinoma are switched to M1 macrophages by Escherichia coli maltose-binding protein." In Abstracts: Thirty-Sixth Annual CTRC-AACR San Antonio Breast Cancer Symposium - Dec 10-14, 2013; San Antonio, TX. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/0008-5472.sabcs13-p6-09-04.

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Reports on the topic "Maltose binding protein (MBP)"

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Gershoni, Jonathan M., David E. Swayne, Tal Pupko, Shimon Perk, Alexander Panshin, Avishai Lublin, and Natalia Golander. Discovery and reconstitution of cross-reactive vaccine targets for H5 and H9 avian influenza. United States Department of Agriculture, January 2015. http://dx.doi.org/10.32747/2015.7699854.bard.

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Research objectives: Identification of highly conserved B-cell epitopes common to either H5 or H9 subtypes of AI Reconstruction of conserved epitopes from (1) as recombinantimmunogens, and testing their suitability to be used as universal vaccine components by measuring their binding to Influenza vaccinated sera of birds Vaccination of chickens with reconstituted epitopes and evaluation of successful vaccination, clinical protection and viral replication Development of a platform to investigate the dynamics of immune response towards infection or an epitope based vaccine Estimate our ability to focus the immune response towards an epitope-based vaccine using the tool we have developed in (D) Summary: This study is a multi-disciplinary study of four-way collaboration; The SERPL, USDA, Kimron-Israel, and two groups at TAU with the purpose of evaluating the production and implementation of epitope based vaccines against avian influenza (AI). Systematic analysis of the influenza viral spike led to the production of a highly conserved epitope situated at the hinge of the HA antigen designated “cluster 300” (c300). This epitope consists of a total of 31 residues and was initially expressed as a fusion protein of the Protein 8 major protein of the bacteriophagefd. Two versions of the c300 were produced to correspond to the H5 and H9 antigens respectively as well as scrambled versions that were identical with regard to amino acid composition yet with varied linear sequence (these served as negative controls). The recombinantimmunogens were produced first as phage fusions and then subsequently as fusions with maltose binding protein (MBP) or glutathioneS-transferase (GST). The latter were used to immunize and boost chickens at SERPL and Kimron. Furthermore, vaccinated and control chickens were challenged with concordant influenza strains at Kimron and SEPRL. Polyclonal sera were obtained for further analyses at TAU and computational bioinformatics analyses in collaboration with Prof. Pupko. Moreover, the degree of protection afforded by the vaccination was determined. Unfortunately, no protection could be demonstrated. In parallel to the main theme of the study, the TAU team (Gershoni and Pupko) designed and developed a novel methodology for the systematic analysis of the antibody composition of polyclonal sera (Deep Panning) which is essential for the analyses of the humoral response towards vaccination and challenge. Deep Panning is currently being used to monitor the polyclonal sera derived from the vaccination studies conducted at the SEPRL and Kimron.
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