Relevant bibliographies by topics / Proteine phos

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers
  5. Reports

Academic literature on the topic 'Proteine phos'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Proteine phos"

1

Vogel, K., W. Hörz, and A. Hinnen. "The two positively acting regulatory proteins PHO2 and PHO4 physically interact with PHO5 upstream activation regions." Molecular and Cellular Biology 9, no. 5 (May 1989): 2050–57. http://dx.doi.org/10.1128/mcb.9.5.2050.

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The repressible acid phosphatase gene PHO5 of Saccharomyces cerevisiae requires the two positively acting regulatory proteins PHO2 and PHO4 for expression. pho2 or pho4 mutants are not able to derepress the PHO5 gene under low-Pi conditions. Here we show that both PHO2 and PHO4 bind specifically to the PHO5 promoter in vitro. Gel retardation assays using promoter deletions revealed two regions involved in PHO4 binding. Further characterization by DNase I footprinting showed two protected areas, one located at -347 to -373 (relative to the ATG initiator codon) (UASp1) and the other located at -239 to -262 (UASp2). Exonuclease III footprint experiments revealed stops at -349 and -368 (UASp1) as well as at -245 and -260 (UASp2). Gel retardation assays with the PHO2 protein revealed a binding region that lay between the two PHO4-binding sites. DNase I footprint analysis suggested a PHO2-binding site covering the region between -277 and -296.
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Vogel, K., W. Hörz, and A. Hinnen. "The two positively acting regulatory proteins PHO2 and PHO4 physically interact with PHO5 upstream activation regions." Molecular and Cellular Biology 9, no. 5 (May 1989): 2050–57. http://dx.doi.org/10.1128/mcb.9.5.2050-2057.1989.

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The repressible acid phosphatase gene PHO5 of Saccharomyces cerevisiae requires the two positively acting regulatory proteins PHO2 and PHO4 for expression. pho2 or pho4 mutants are not able to derepress the PHO5 gene under low-Pi conditions. Here we show that both PHO2 and PHO4 bind specifically to the PHO5 promoter in vitro. Gel retardation assays using promoter deletions revealed two regions involved in PHO4 binding. Further characterization by DNase I footprinting showed two protected areas, one located at -347 to -373 (relative to the ATG initiator codon) (UASp1) and the other located at -239 to -262 (UASp2). Exonuclease III footprint experiments revealed stops at -349 and -368 (UASp1) as well as at -245 and -260 (UASp2). Gel retardation assays with the PHO2 protein revealed a binding region that lay between the two PHO4-binding sites. DNase I footprint analysis suggested a PHO2-binding site covering the region between -277 and -296.
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Barbaric, Slobodan, Martin Münsterkötter, Colin Goding, and Wolfram Hörz. "Cooperative Pho2-Pho4 Interactions at thePHO5 Promoter Are Critical for Binding of Pho4 to UASp1 and for Efficient Transactivation by Pho4 at UASp2." Molecular and Cellular Biology 18, no. 5 (May 1, 1998): 2629–39. http://dx.doi.org/10.1128/mcb.18.5.2629.

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ABSTRACT The activation of the PHO5 gene in Saccharomyces cerevisiae in response to phosphate starvation critically depends on two transcriptional activators, the basic helix-loop-helix protein Pho4 and the homeodomain protein Pho2. Pho4 acts through two essential binding sites corresponding to the regulatory elements UASp1 and UASp2. Mutation of either of them results in a 10-fold decrease in promoter activity, and mutation of both sites renders the promoter totally uninducible. The role of Pho4 appears relatively straightforward, but the mechanism of action of Pho2 had remained elusive. By in vitro footprinting, we have recently mapped multiple Pho2 binding sites adjacent to the Pho4 sites, and by mutating them individually or in combination, we now show that each of them contributes toPHO5 promoter activity. Their function is not only to recruit Pho2 to the promoter but to allow cooperative binding of Pho4 together with Pho2. Cooperativity requires DNA binding of Pho2 to its target sites and Pho2-Pho4 interactions. A Pho4 derivative lacking the Pho2 interaction domain is unable to activate the promoter, but testing of UASp1 and UASp2 individually in a minimal CYC1 promoter reveals a striking difference between the two UAS elements. UASp1 is fully inactive, presumably because the Pho4 derivative is not recruited to its binding site. In contrast, UASp2 activates strongly in a Pho2-independent manner. From in vivo footprinting experiments and activity measurements with a promoter variant containing two UASp2 elements, we conclude that at UASp2, Pho2 is mainly required for the ability of Pho4 to transactivate.
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Pondugula, Santhi, Daniel W. Neef, Warren P. Voth, Russell P. Darst, Archana Dhasarathy, M. Megan Reynolds, Shinya Takahata, David J. Stillman, and Michael P. Kladde. "Coupling Phosphate Homeostasis to Cell Cycle-Specific Transcription: Mitotic Activation of Saccharomyces cerevisiae PHO5 by Mcm1 and Forkhead Proteins." Molecular and Cellular Biology 29, no. 18 (July 13, 2009): 4891–905. http://dx.doi.org/10.1128/mcb.00222-09.

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ABSTRACT Cells devote considerable resources to nutrient homeostasis, involving nutrient surveillance, acquisition, and storage at physiologically relevant concentrations. Many Saccharomyces cerevisiae transcripts coding for proteins with nutrient uptake functions exhibit peak periodic accumulation during M phase, indicating that an important aspect of nutrient homeostasis involves transcriptional regulation. Inorganic phosphate is a central macronutrient that we have previously shown oscillates inversely with mitotic activation of PHO5. The mechanism of this periodic cell cycle expression remains unknown. To date, only two sequence-specific activators, Pho4 and Pho2, were known to induce PHO5 transcription. We provide here evidence that Mcm1, a MADS-box protein, is essential for PHO5 mitotic activation. In addition, we found that cells simultaneously lacking the forkhead proteins, Fkh1 and Fkh2, exhibited a 2.5-fold decrease in PHO5 expression. The Mcm1-Fkh2 complex, first shown to transactivate genes within the CLB2 cluster that drive G2/M progression, also associated directly at the PHO5 promoter in a cell cycle-dependent manner in chromatin immunoprecipitation assays. Sds3, a component specific to the Rpd3L histone deacetylase complex, was also recruited to PHO5 in G1. These findings provide (i) further mechanistic insight into PHO5 mitotic activation, (ii) demonstrate that Mcm1-Fkh2 can function combinatorially with other activators to yield late M/G1 induction, and (iii) couple the mitotic cell cycle progression machinery to cellular phosphate homeostasis.
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Antelmann, Haike, Christian Scharf, and Michael Hecker. "Phosphate Starvation-Inducible Proteins ofBacillus subtilis: Proteomics and Transcriptional Analysis." Journal of Bacteriology 182, no. 16 (August 15, 2000): 4478–90. http://dx.doi.org/10.1128/jb.182.16.4478-4490.2000.

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ABSTRACT The phosphate starvation response in Bacillus subtiliswas analyzed using two-dimensional (2D) polyacrylamide gel electrophoresis of cell extracts and supernatants from phosphate-starved cells. Most of the phosphate starvation-induced proteins are under the control of ςB, the activity of which is increased by energy depletion. In order to define the proteins belonging to the Pho regulon, which is regulated by the two-component regulatory proteins PhoP and PhoR, the 2D protein pattern of the wild type was compared with those of a sigB mutant and aphoR mutant. By matrix-assisted laser desorption ionization–time of flight mass spectrometry, two alkaline phosphatases (APases) (PhoA and PhoB), an APase-alkaline phosphodiesterase (PhoD), a glycerophosphoryl diester phosphodiesterase (GlpQ), and the lipoprotein YdhF were identified as very strongly induced PhoPR-dependent proteins secreted into the extracellular medium. In the cytoplasmic fraction, PstB1, PstB2, and TuaD were identified as already known PhoPR-dependent proteins, in addition to PhoB, PhoD, and the previously described PstS. Transcriptional studies of glpQ and ydhFconfirmed the strong PhoPR dependence. Northern hybridization and primer extension experiments showed that glpQ is transcribed monocistronically from a ςA promoter which is overlapped by four putative TT(A/T)ACA-like PhoP binding sites. Furthermore, ydhF might be cotranscribed withphoB initiating from the phoB promoter. Only a small group of proteins remained phosphate starvation inducible in bothphoR and sigB mutant and did not form a unique regulation group. Among these, YfhM and YjbC were controlled by ςB-dependent and unknown PhoPR-independent mechanisms. Furthermore, YtxH and YvyD seemed to be induced after phosphate starvation in the wild type in a ςB-dependent manner and in the sigB mutant probably via ςH. YxiE was induced by phosphate starvation independently of ςB and PhoPR.
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Teng, Fang, Ling Wang, Kavindra V. Singh, Barbara E. Murray, and George M. Weinstock. "Involvement of PhoP-PhoS Homologs in Enterococcus faecalis Virulence." Infection and Immunity 70, no. 4 (April 2002): 1991–96. http://dx.doi.org/10.1128/iai.70.4.1991-1996.2002.

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ABSTRACT Eleven PhoP-PhoS homolog pairs were identified by searching the Enterococcus faecalis V583 genome sequence database at The Institute for Genomic Research with the Bacillus subtilis PhoP-PhoS sequences. Each pair appears to be a potential two-component system composed of a response regulator and a sensor kinase. Seven of the homologs were disrupted in E. faecalis strain OG1RF. TX10293, a mutant disrupted in one of these genes (etaR, the first gene of the gene pair designated etaRS), showed delayed killing and a higher 50% lethal dose in a mouse peritonitis model. The predicted EtaR protein sequence showed greatest similarity to LisR of Listeria monocytogenes (77%) and CsrR of Streptococcus pyogenes (70%); EtaS is 53% similar to LisK and 54% similar to CsrS. When grown in vitro, the TX10293 mutant was more sensitive to low pH (pH 3.4) and more resistant to high temperature (55°C) than wild-type OG1RF. In conclusion, many potential two-component systems are identified for E. faecalis, one of which, EtaRS, was shown to be involved in stress response and virulence.
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Barbaric, S., M. Munsterkotter, J. Svaren, and W. Horz. "The Homeodomain Protein Pho2 and the Basic-Helix-Loop-Helix Protein Pho4 Bind DNA Cooperatively at the Yeast PHO5 Promoter." Nucleic Acids Research 24, no. 22 (November 1, 1996): 4479–86. http://dx.doi.org/10.1093/nar/24.22.4479.

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Ogawa, N., and Y. Oshima. "Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae." Molecular and Cellular Biology 10, no. 5 (May 1990): 2224–36. http://dx.doi.org/10.1128/mcb.10.5.2224.

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The PHO4 gene encodes a positive regulatory factor involved in regulating transcription of various genes in the phosphatase regulon of Saccharomyces cerevisiae. Besides its own coding region, the 1.8-kilobase PHO4 transcript contains a coding region for a mitochondrial protein which does not appear to be translated. Four functional domains were found in the PHO4 protein, which consists of 312 amino acid (aa) residues as deduced from the open reading frame of PHO4. A gel retardation assay with beta-galactosidase::PHO4 fused protein revealed that the 85-aa C terminus is the domain responsible for binding to the promoter DNA of PHO5, a gene under the control of PHO4. This region has similarities with the amphipathic helix-loop-helix motif of c-myc protein. Determination of the nucleotide sequences of four PHO4c mutant alleles and insertion and deletion analyses of PHO4 DNA indicated that a region from aa 163 to 202 is involved in interaction with a negative regulatory factor PHO80. Complementation of a pho4 null allele with the modified PHO4 DNAs suggested that the N-terminal region (1 to 109 aa), which is rich in acidic aa, is the transcriptional activation domain. The deleterious effects of various PHO4 mutations on the constitutive transcription of PHO5 in PHO4c mutant cells suggested that the region from aa 203 to 227 is involved in oligomerization of the PHO4 protein.
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Ogawa, N., and Y. Oshima. "Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae." Molecular and Cellular Biology 10, no. 5 (May 1990): 2224–36. http://dx.doi.org/10.1128/mcb.10.5.2224-2236.1990.

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The PHO4 gene encodes a positive regulatory factor involved in regulating transcription of various genes in the phosphatase regulon of Saccharomyces cerevisiae. Besides its own coding region, the 1.8-kilobase PHO4 transcript contains a coding region for a mitochondrial protein which does not appear to be translated. Four functional domains were found in the PHO4 protein, which consists of 312 amino acid (aa) residues as deduced from the open reading frame of PHO4. A gel retardation assay with beta-galactosidase::PHO4 fused protein revealed that the 85-aa C terminus is the domain responsible for binding to the promoter DNA of PHO5, a gene under the control of PHO4. This region has similarities with the amphipathic helix-loop-helix motif of c-myc protein. Determination of the nucleotide sequences of four PHO4c mutant alleles and insertion and deletion analyses of PHO4 DNA indicated that a region from aa 163 to 202 is involved in interaction with a negative regulatory factor PHO80. Complementation of a pho4 null allele with the modified PHO4 DNAs suggested that the N-terminal region (1 to 109 aa), which is rich in acidic aa, is the transcriptional activation domain. The deleterious effects of various PHO4 mutations on the constitutive transcription of PHO5 in PHO4c mutant cells suggested that the region from aa 203 to 227 is involved in oligomerization of the PHO4 protein.
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Allen, Mindy P., Kimberly B. Zumbrennen, and William R. McCleary. "Genetic Evidence that the α5 Helix of the Receiver Domain of PhoB Is Involved in Interdomain Interactions." Journal of Bacteriology 183, no. 7 (April 1, 2001): 2204–11. http://dx.doi.org/10.1128/jb.183.7.2204-2211.2001.

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ABSTRACT Two-component signaling proteins are involved in transducing environmental stimuli into intracellular signals. Information is transmitted through a phosphorylation cascade that consists of a histidine protein kinase and a response regulator protein. Generally, response regulators are made up of a receiver domain and an output domain. Phosphorylation of the receiver domain modulates the activity of the output domain. The mechanisms by which receiver domains control the activities of their respective output domains are unknown. To address this question for the PhoB protein from Escherichia coli, we have employed two separate genetic approaches, deletion analysis and domain swapping. In-frame deletions were generated within the phoB gene, and the phenotypes of the mutants were analyzed. The output domain, by itself, retained significant ability to activate transcription of the phoA gene. However, another deletion mutant that contained the C-terminal α-helix of the receiver domain (α5) in addition to the entire output domain was unable to activate transcription of phoA. This result suggests that the α5 helix of the receiver domain interacts with and inhibits the output domain. We also constructed two chimeric proteins that join various parts of the chemotaxis response regulator, CheY, to PhoB. A chimera that joins the N-terminal ∼85% of CheY's receiver domain to the β5-α5 loop of PhoB's receiver domain displayed phosphorylation-dependent activity. The results from both sets of experiments suggest that the regulation of PhoB involves the phosphorylation-mediated modulation of inhibitory contacts between the α5 helix of its unphosphorylated receiver domain and its output domain.
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Dissertations / Theses on the topic "Proteine phos"

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Anba, Jamila. "Biosynthese et exportation d'une proteine periplasmique, phos, chez escherichia coli k-12." Aix-Marseille 2, 1987. http://www.theses.fr/1987AIX22062.

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La surproduction par escherichia coli de la proteine periplasmique affine pour le phosphate (phos) provoque l'accumulation du precurseur de phos a la fois dans la membrane interne et le cytoplasme. Seul le precurseur membranaire peut etre mature et exporte, alors que le precurseur cytoplasmique subit une coupure lente de sa sequence signal et donne naissance a une forme "pseudo-mature" cytoplasmique. Existence d'un captage entre la synthese et l'exportation. Une application du systeme phos a ete realisee pour la production du facteur de liberation de l'hormone de croissance humaine (hgrf) chez e. Coli. En carence de phosphate, la proteine hybride phos-hgrf est synthetisee et exportee vers le periplasme
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Loney, Erica. "PhoR, PhoP and MshC: Three essential proteins of Mycobacterium tuberculosis." University of Toledo / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1396606314.

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Gardner, Stewart G. "Studies of PhoU in Escherichia coli: Metal Binding, Dimerization,Protein/Protein Interactions, and a Signaling Complex Model." BYU ScholarsArchive, 2014. https://scholarsarchive.byu.edu/etd/5685.

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Phosphate is an essential nutrient for all forms of life. Escherichia coli has a PhoR/PhoB two component regulatory system that controls the expression of various genes whose products allow the cell to thrive in low phosphate environments. The signaling mechanism of the PhoR/PhoB system has been studied and the phosphorylation cascade that controls gene expression is well understood. What is still unknown is how PhoR senses the phosphate level of the environment. The PstS, PstC, PstA, PstB, and PhoU proteins play a role in this signal sensing. This work confirms the hypothesis that the PstSCAB complex senses the environmental phosphate and that phosphate signal is passed through PhoU to PhoR. Further, this work characterizes residues important for interaction on PhoU and PhoR and identifies a structural model for interaction. This model points to a potential mechanism for PhoU mediated signaling to PhoR. We tested this model with direct coupling analysis and obtained further confirmation. Further use of these techniques may elucidate more of the interactions necessary for proper phosphate signaling.
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Anba, Jamila. "Biosynthèse et exportation d'une protéine périplasmique, PhoS, chez Escherichia coli K-12." Grenoble 2 : ANRT, 1987. http://catalogue.bnf.fr/ark:/12148/cb37602327q.

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Johns, Kristine Dawn. "Evidences for Protein-Protein Interactions Between PstB and PhoU in the Phosphate Signaling Complex of Escherichia coli." BYU ScholarsArchive, 2013. https://scholarsarchive.byu.edu/etd/3932.

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The PstSCAB2 complex serves the dual function of being a phosphate transporter as well as the primary sensor of phosphate for the Pho regulon. PhoU is an integral protein required for the signal from PstSCAB2 to be transmitted to PhoR. Our hypothesis is that conformational changes of PstSCAB2 during the phosphate transport process are the mechanism by which information about environmental phosphate levels are transduced to the cell. Additionally, we propose that direct protein-protein interactions between PhoU and the alternating conformations of PstSCAB2 mediate PhoU interactions with PhoR. By means of genetic and biochemical approaches, we have found substantial evidence supporting both these hypotheses.
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Cho, Uhn-Soo. "Structural studies of protein phosphatase 2A, simian virus 40 small t antigen, and the PhoQ sensor domain /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/5677.

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Ghimire, Jenisha. "Role of Ime4 Protein in PHO Regulon of S.cerevisiae." ScholarWorks@UNO, 2015. http://scholarworks.uno.edu/td/2037.

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In the yeast Saccharomyces cerevisiae, the IME4 methyltransferase, interacts genetically with methyl binding protein, Pho92, to affect the expression of PHO regulon target genes. Cells mutant in IME4 or PHO92 show increases in the RNA abundance of PHO regulon target genes. The increase in the RNA abundance of the PHO regulon target genes is not additive in the cells double mutant in IME4 and PHO92. Hence, Ime4 and Pho92 interact in a single pathway in PHO regulon. Surprisingly, cells overexpressing IME4 and MUM2 shows increase in some PHO regulon target genes, indicating that IME4 affects the PHO regulon target genes through multiple mechanisms in different conditions. A promoter swap experiment revealed that one of the PHO regulon mRNAs that codes for phosphatase, PHO5, is a direct target of Ime4. Further experiments are required to examine whether the same is true for all PHO regulon mRNAs.
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Gardner, Stewart G. "Genetic analysis of conserved residues in PhoU of Escherichia coli." Diss., CLICK HERE for online access, 2005. http://contentdm.lib.byu.edu/ETD/image/etd934.pdf.

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Pang, Tin Yau. "Study of the surface structures and patterns of the hydrophobic-polar model of protein /." View abstract or full-text, 2007. http://library.ust.hk/cgi/db/thesis.pl?PHYS%202007%20PANG.

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Ma, Chun-Wai. "Aboav-Weaire law in complex network and its applications in bioinformatics /." View abstract or full-text, 2005. http://library.ust.hk/cgi/db/thesis.pl?PHYS%202005%20MA.

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Book chapters on the topic "Proteine phos"

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Kinoshita, Eiji, Emiko Kinoshita-Kikuta, and Tohru Koike. "Phos-tag Affinity Electrophoresis for Protein Kinase Profiling." In Protein Kinase Technologies, 13–34. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-824-5_2.

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Chandra, Mintu, and Brett M. Collins. "The Phox Homology (PX) Domain." In Protein Reviews – Purinergic Receptors, 1–17. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/5584_2018_185.

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Kinoshita, Eiji, Emiko Kinoshita-Kikuta, and Tohru Koike. "Phos-tag-Based Affinity Chromatography Techniques for Enrichment of the Phosphoproteome." In Protein Modifications in Pathogenic Dysregulation of Signaling, 17–30. Tokyo: Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55561-2_2.

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Kinoshita, Eiji, Emiko Kinoshita-Kikuta, and Tohru Koike. "Determining Protein Phosphorylation Status Using Antibody Arrays and Phos-Tag Biotin." In Methods in Molecular Biology, 217–24. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-1064-0_18.

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Horinouchi, Takahiro, Koji Terada, Tsunehito Higashi, and Soichi Miwa. "Using Phos-Tag in Western Blotting Analysis to Evaluate Protein Phosphorylation." In Methods in Molecular Biology, 267–77. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-3353-2_18.

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Örd, Mihkel, and Mart Loog. "Detection of Multisite Phosphorylation of Intrinsically Disordered Proteins Using Phos-tag SDS-PAGE." In Methods in Molecular Biology, 779–92. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0524-0_40.

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Karimova, Gouzel, and Daniel Ladant. "Defining Membrane Protein Topology Using pho-lac Reporter Fusions." In Methods in Molecular Biology, 129–42. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7033-9_10.

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Kinoshita-Kikuta, Emiko, Eiji Kinoshita, and Tohru Koike. "Phos-Tag Fluorescent Gel Staining for the Quantitative Detection of His- and Asp-Phosphorylated Proteins." In Methods in Molecular Biology, 73–78. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1186-9_6.

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Jansen, Carmen, Hans de Cock, Patrick Van Gelder, and Jan Tommassen. "In vitro assembly of outer membrane protein PhoE of E. coli." In Molecular Dynamics of Biomembranes, 71–78. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61126-1_7.

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Kumar, Gaurav. "A Simple Method for Detecting Phosphorylation of Proteins by Using Zn2+-Phos-Tag SDS-PAGE at Neutral pH." In Methods in Molecular Biology, 223–29. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8745-0_25.

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Conference papers on the topic "Proteine phos"

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Peterson, C. B., C. M. Noyes, J. M. Pecon, F. C. Church, and M. N. Blackburn. "LYSINE-125 IS ESSENTIAL FOR HEPARIN BINDING TO ANTITHROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643769.

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Identification of lysyl residue(s) in human plasma antithrombin required for binding of heparin was approached using chemical modification with the amino-group reagent, pyridoxal-5'-phosphate. Modification of antithrombin (AT) with limiting amounts of reagent yields an average incorporation of the phos-phopyridoxyl label into one lysine per protein molecule. Fractionation of the labeled AT by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated AT species devoid of heparin binding (Pool I) from modified protein which retained affinity for heparin (Pool II). Pool I contained an average of 1.6 mol phosphopyridoxyl label per mol AT, whereas Pool II was labeled to a lesser extent, with a ratio of 1.0 mol phosphopyridoxyl per mol protein. To generate peptide maps of the two AT species, the proteins were reductively denatured, S-carboxymethylated, and digested with trypsin. Fractionation of the tryptic digests by reverse-phase HPLC indicated one peak in the chromatogram of the non-heparin-binding species to be clearly different when compared to the chromatogram of the heparin-binding species. Upon sequencing of the unique peptide by automated Edman degradation, the modified residue was identified as Lys-125 in the primary sequence of AT. Additionally, AT was reacted with pyridoxal-5 ′-phosphate in the presence of added heparin for comparison with protein modified in the absence of heparin. Overall incorporation of the phosphopyridoxyl label was 3-4 mol reagent per mol protein, without inclusion of heparin during the modification reaction, and only 2-3 mol pyridoxyl per mol protein with heparin added. Tryptic peptide maps of these two modified ATs indicated that eight lysine residues are "protected" from modification by addition of heparin. The "protected" lysines identified, in addition to the essential Lys-125, are residues 11, 39, 133, 136, 257, 275, and 287. Identification of Lys-125 as the critical lysine for heparin binding strongly supports previous data which indicates that the heparin-binding domain of AT is located at the N-termi-nus within one of the disulfide cross-linked loops of the protein.
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Yanik, Ahmet Ali, Arif E. Cetin, Min Huang, Alp Artar, S. Hossein Mousavi, Alexander Khanikaev, John Connor, Gennady Shvets, and Hatice Altug. "Ultrasensitive plasmonic fano sensor enables seeing protein monolayers with naked eye." In 2011 IEEE Photonics Conference (IPC). IEEE, 2011. http://dx.doi.org/10.1109/pho.2011.6110608.

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Wang, Shau-Chun, Hsiao-Ping Chen, and Hsueh-Chia Chang. "Entrainment of DNA and Charged Nano-Particles Using AC Electrospray." In ASME 2009 Second International Conference on Micro/Nanoscale Heat and Mass Transfer. ASMEDC, 2009. http://dx.doi.org/10.1115/mnhmt2009-18207.

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We examine our earlier finding that AC electrospray cone can preferentially entrain and concentrate low-mobility ions generated at the cone tip [Chetwani, Maheshwari and Chang, Phys Rev Lett., 101, 204501 (2008)]. Instead of tip ionization, we scrutinize entrainment effects on dispersed ionic species in the spray solution. Fluorescence images of ejected ionic species, including anionic oxide ions, organic dyes, charged nano-particles, and stained DNA from AC electrospray cone generated with a 4–5 kV source. Negatively charged species such as anionic dyes concentrate at the tip of AC spray cone before ejection. Cationic dyes are more homogeneously distributed in the cone during ejection. Larger particles with negative charges, including fluorescence dye-tagged nano-particles (about 50 nm) and dye-stained DNA, have similar spatio-temporal evolutions of anioic dyes within the cone before ejection. These observations extend our previous entrainment and concentration effect to AC spray without ionization. The images will be correlated with tandem Mass Spectrometry and will be used to selectively gate either cationic (protein) or anionic polymers (DNA).
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4

Skjonsberg, O. H., K. Gravem, P. Kierulf, and H. C. Godal. "A LOW pH PREVENTS DENATURATION OF HEAT TREATED ANT I -HAEMOPHILIC CRYOPRECIPITATE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643968.

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The AIDS epidemic has necessitated heat treatment of FVIII:C products in order to inactivate HIV-virus. When antihaemophilic cryoprecipitate (CP) is heated (68°C, 24 hours), the solubility and the concentration of FVIIIrC, von Willebrand factor and fibrinogen are substantially reduced. Such heat denaturation is prevented by addition of synthetic amino acids (SyntaminR 17) prior to lyophilization and heat treatment (Ref.rMargolis and Eisen, Skjønsberg et al.). The exact mechanism of this protective effect is not known, but in our opinion, the large buffering capacity of Syntamin is of major importance. Thus, in the presence of Syntamin (4 mg/unit FVIIIrC), a pH of 7.4 was maintained during lyophilization and heat treatment, while in ordinary CP, pH rose from 7.8 to 8.6 during the same procedure. Moreover, heat denaturation of CP was prevented by replacing Syntamin with a phosphate buffer, keeping a stable pH below 7.4. It is of interest to notice that apart from the effect on pH, we were unable to observe any influence of Syntamin on heat denaturation of plasma proteins in solution, on degradation of FVIII:C and fibrinogen by thrombin or plssmin or on the solubility of fibrin in plasma and CP.Heat treatment of CP at various pHs indicated that the :est product was obtained when pH .was kept between 6.5 and 6.3. By using an acidic buffer instead of Syntamin, the disadvantages of the latter, such as increased residual moisture leading tc discolouration, a probable stabilizing effect on virus and increased costs, may be avoided.
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Reports on the topic "Proteine phos"

1

Walian, P. J. Electron crystallography of PhoE porin, an outer membrane, channel- forming protein from E. coli. Office of Scientific and Technical Information (OSTI), November 1989. http://dx.doi.org/10.2172/6365889.

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