Статті в журналах з теми "DsbD"
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Cho, Seung-Hyun, and Jon Beckwith. "Mutations of the Membrane-Bound Disulfide Reductase DsbD That Block Electron Transfer Steps from Cytoplasm to Periplasm in Escherichia coli." Journal of Bacteriology 188, no. 14 (July 15, 2006): 5066–76. http://dx.doi.org/10.1128/jb.00368-06.
Повний текст джерелаWalden, Patricia M., Andrew E. Whitten, Lakshmanane Premkumar, Maria A. Halili, Begoña Heras, Gordon J. King та Jennifer L. Martin. "The atypical thiol–disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase". Acta Crystallographica Section D Structural Biology 75, № 3 (26 лютого 2019): 283–95. http://dx.doi.org/10.1107/s2059798318018442.
Повний текст джерелаLin, Dongxia, Byoungkwan Kim, and James M. Slauch. "DsbL and DsbI contribute to periplasmic disulfide bond formation in Salmonella enterica serovar Typhimurium." Microbiology 155, no. 12 (December 1, 2009): 4014–24. http://dx.doi.org/10.1099/mic.0.032904-0.
Повний текст джерелаSkórko-Glonek, Joanna, Anna Sobiecka-Szkatuła, and Barbara Lipińska. "Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli." Acta Biochimica Polonica 53, no. 3 (October 1, 2006): 585–89. http://dx.doi.org/10.18388/abp.2006_3331.
Повний текст джерелаKurokawa, Yoichi, Hideki Yanagi, and Takashi Yura. "Overexpression of Protein Disulfide Isomerase DsbC Stabilizes Multiple-Disulfide-Bonded Recombinant Protein Produced and Transported to the Periplasm in Escherichia coli." Applied and Environmental Microbiology 66, no. 9 (September 1, 2000): 3960–65. http://dx.doi.org/10.1128/aem.66.9.3960-3965.2000.
Повний текст джерелаGoldstone, D., P. W. Haebel, F. Katzen, M. W. Bader, J. C. A. Bardwell, J. Beckwith, and P. Metcalf. "DsbC activation by the N-terminal domain of DsbD." Proceedings of the National Academy of Sciences 98, no. 17 (August 7, 2001): 9551–56. http://dx.doi.org/10.1073/pnas.171315498.
Повний текст джерелаSmith, Roxanne P., Biswaranjan Mohanty, Shakeel Mowlaboccus, Jason J. Paxman, Martin L. Williams, Stephen J. Headey, Geqing Wang, et al. "Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens." Journal of Biological Chemistry 293, no. 43 (September 4, 2018): 16559–71. http://dx.doi.org/10.1074/jbc.ra118.004847.
Повний текст джерелаYu, Jun. "Inactivation of DsbA, but Not DsbC and DsbD, Affects the Intracellular Survival and Virulence ofShigella flexneri." Infection and Immunity 66, no. 8 (August 1, 1998): 3909–17. http://dx.doi.org/10.1128/iai.66.8.3909-3917.1998.
Повний текст джерелаKimball, Richard A., Laetitia Martin, and Milton H. Saier Jr. "Reversing Transmembrane Electron Flow: The DsbD and DsbB Protein Families." Journal of Molecular Microbiology and Biotechnology 5, no. 3 (2003): 133–49. http://dx.doi.org/10.1159/000070263.
Повний текст джерелаSmith, Roxanne P., Andrew E. Whitten, Jason J. Paxman, Charlene M. Kahler, Martin J. Scanlon, and Begoña Heras. "Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme inNeisseria meningitidis." Acta Crystallographica Section F Structural Biology Communications 74, no. 1 (January 1, 2018): 31–38. http://dx.doi.org/10.1107/s2053230x17017800.
Повний текст джерелаBushweller, John H. "Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA." Journal of Molecular Biology 432, no. 18 (August 2020): 5091–103. http://dx.doi.org/10.1016/j.jmb.2020.04.008.
Повний текст джерелаDeshmukh, Meenal, Serdar Turkarslan, Donniel Astor, Maria Valkova-Valchanova, and Fevzi Daldal. "The Dithiol:Disulfide Oxidoreductases DsbA and DsbB of Rhodobacter capsulatus Are Not Directly Involved in Cytochrome c Biogenesis, but Their Inactivation Restores the Cytochrome c Biogenesis Defect of CcdA-Null Mutants." Journal of Bacteriology 185, no. 11 (June 1, 2003): 3361–72. http://dx.doi.org/10.1128/jb.185.11.3361-3372.2003.
Повний текст джерелаHiniker, Annie, Didier Vertommen, James C. A. Bardwell, and Jean-Francois Collet. "Evidence for Conformational Changes within DsbD: Possible Role for Membrane-Embedded Proline Residues." Journal of Bacteriology 188, no. 20 (October 1, 2006): 7317–20. http://dx.doi.org/10.1128/jb.00383-06.
Повний текст джерелаKumar, Pradeep, Soma Sannigrahi, Jessica Scoullar, Charlene M. Kahler, and Yih-Ling Tzeng. "Characterization of DsbD in Neisseria meningitidis." Molecular Microbiology 79, no. 6 (January 24, 2011): 1557–73. http://dx.doi.org/10.1111/j.1365-2958.2011.07546.x.
Повний текст джерелаFeissner, Robert E., Caroline S. Beckett, Jennifer A. Loughman, and Robert G. Kranz. "Mutations in Cytochrome Assembly and Periplasmic Redox Pathways in Bordetella pertussis." Journal of Bacteriology 187, no. 12 (June 15, 2005): 3941–49. http://dx.doi.org/10.1128/jb.187.12.3941-3949.2005.
Повний текст джерелаRozhkova, Anna, and Rudi Glockshuber. "Thermodynamic Aspects of DsbD-Mediated Electron Transport." Journal of Molecular Biology 380, no. 5 (July 2008): 783–88. http://dx.doi.org/10.1016/j.jmb.2008.05.050.
Повний текст джерелаBrot, Nathan, Jean-François Collet, Lynnette C. Johnson, Thomas J. Jönsson, Herbert Weissbach, and W. Todd Lowther. "The Thioredoxin Domain of Neisseria gonorrhoeae PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases." Journal of Biological Chemistry 281, no. 43 (August 22, 2006): 32668–75. http://dx.doi.org/10.1074/jbc.m604971200.
Повний текст джерелаStenson, Trevor H., and Alison A. Weiss. "DsbA and DsbC Are Required for Secretion of Pertussis Toxin by Bordetella pertussis." Infection and Immunity 70, no. 5 (May 2002): 2297–303. http://dx.doi.org/10.1128/iai.70.5.2297-2303.2002.
Повний текст джерелаHaebel, P. W., D. Goldstone, and P. Metcalf. "The disulfide bond isomerase DsbC is specifically activated by the IG fold domain of the electron transporter DsbD." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (August 6, 2002): c5. http://dx.doi.org/10.1107/s010876730208529x.
Повний текст джерелаREID, Eleanor, Jeff COLE, and Deborah J. EAVES. "The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly." Biochemical Journal 355, no. 1 (February 26, 2001): 51–58. http://dx.doi.org/10.1042/bj3550051.
Повний текст джерелаStirnimann, Christian U., Anna Rozhkova, Ulla Grauschopf, Markus G. Grütter, Rudi Glockshuber, and Guido Capitani. "Structural Basis and Kinetics of DsbD-Dependent Cytochrome c Maturation." Structure 13, no. 7 (July 2005): 985–93. http://dx.doi.org/10.1016/j.str.2005.04.014.
Повний текст джерелаKrupp, Rebecca, Cecilia Chan, and Dominique Missiakas. "DsbD-catalyzed Transport of Electrons across the Membrane ofEscherichia coli." Journal of Biological Chemistry 276, no. 5 (November 20, 2000): 3696–701. http://dx.doi.org/10.1074/jbc.m009500200.
Повний текст джерелаMavridou, Despoina A. I., Julie M. Stevens, Alan D. Goddard, Antony C. Willis, Stuart J. Ferguson, and Christina Redfield. "Control of Periplasmic Interdomain Thiol:Disulfide Exchange in the Transmembrane Oxidoreductase DsbD." Journal of Biological Chemistry 284, no. 5 (November 12, 2008): 3219–26. http://dx.doi.org/10.1074/jbc.m805963200.
Повний текст джерелаUm, Si-Hyeon, Jin-Sik Kim, Kangseok Lee, and Nam-Chul Ha. "Structure of a DsbF homologue fromCorynebacterium diphtheriae." Acta Crystallographica Section F Structural Biology Communications 70, no. 9 (August 29, 2014): 1167–72. http://dx.doi.org/10.1107/s2053230x14016355.
Повний текст джерелаRozhkova, Anna, and Rudi Glockshuber. "Kinetics of the Intramolecular Disulfide Exchange Between the Periplasmic Domains of DsbD." Journal of Molecular Biology 367, no. 4 (April 2007): 1162–70. http://dx.doi.org/10.1016/j.jmb.2006.12.033.
Повний текст джерелаKurokawa, Yoichi, Hideki Yanagi, and Takashi Yura. "Overproduction of Bacterial Protein Disulfide Isomerase (DsbC) and Its Modulator (DsbD) Markedly Enhances Periplasmic Production of Human Nerve Growth Factor inEscherichia coli." Journal of Biological Chemistry 276, no. 17 (January 22, 2001): 14393–99. http://dx.doi.org/10.1074/jbc.m100132200.
Повний текст джерелаHaebel, Peter W., Steven Wichman, David Goldstone та Peter Metcalf. "Crystallization and Initial Crystallographic Analysis of the Disulfide Bond Isomerase DsbC in Complex with the α Domain of the Electron Transporter DsbD". Journal of Structural Biology 136, № 2 (листопад 2001): 162–66. http://dx.doi.org/10.1006/jsbi.2001.4430.
Повний текст джерелаCho, Seung-Hyun, Amir Porat, Jiqing Ye, and Jon Beckwith. "Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility." EMBO Journal 26, no. 15 (July 19, 2007): 3509–20. http://dx.doi.org/10.1038/sj.emboj.7601799.
Повний текст джерелаKatzen, F. "Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD." EMBO Journal 21, no. 15 (August 1, 2002): 3960–69. http://dx.doi.org/10.1093/emboj/cdf405.
Повний текст джерелаAndersen, Catherine L., Anne Matthey‐Dupraz, Dominique Missiakas, and Satish Raina. "A new Escherichia coli gene, dsbG , encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins." Molecular Microbiology 26, no. 1 (October 1997): 121–32. http://dx.doi.org/10.1046/j.1365-2958.1997.5581925.x.
Повний текст джерелаKatzen, Federico, and Jon Beckwith. "Transmembrane Electron Transfer by the Membrane Protein DsbD Occurs via a Disulfide Bond Cascade." Cell 103, no. 5 (November 2000): 769–79. http://dx.doi.org/10.1016/s0092-8674(00)00180-x.
Повний текст джерелаMissiakas, D., F. Schwager, and S. Raina. "Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli." EMBO Journal 14, no. 14 (July 1995): 3415–24. http://dx.doi.org/10.1002/j.1460-2075.1995.tb07347.x.
Повний текст джерелаMavridou, Despoina A. I., Martin Braun, Linda Thöny-Meyer, Julie M. Stevens, and Stuart J. Ferguson. "Avoidance of the cytochrome c biogenesis system by periplasmic CXXCH motifs." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1124–28. http://dx.doi.org/10.1042/bst0361124.
Повний текст джерелаPorat, Amir, Seung-Hyun Cho, and Jon Beckwith. "The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases." Research in Microbiology 155, no. 8 (October 2004): 617–22. http://dx.doi.org/10.1016/j.resmic.2004.05.005.
Повний текст джерелаRozhkova, Anna, Christian U. Stirnimann, Patrick Frei, Ulla Grauschopf, René Brunisholz, Markus G. Grütter, Guido Capitani, and Rudi Glockshuber. "Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD." EMBO Journal 23, no. 8 (April 1, 2004): 1709–19. http://dx.doi.org/10.1038/sj.emboj.7600178.
Повний текст джерелаSmith, Roxanne P., Biswaranjan Mohanty, Martin L. Williams, Martin J. Scanlon та Begoña Heras. "HN, N, Cα and Cβ assignments of the two periplasmic domains of Neisseria meningitidis DsbD". Biomolecular NMR Assignments 11, № 2 (6 червня 2017): 181–86. http://dx.doi.org/10.1007/s12104-017-9743-x.
Повний текст джерелаTan, Jacqueline, Ying Lu, and James C. A. Bardwell. "Mutational Analysis of the Disulfide Catalysts DsbA and DsbB." Journal of Bacteriology 187, no. 4 (February 15, 2005): 1504–10. http://dx.doi.org/10.1128/jb.187.4.1504-1510.2005.
Повний текст джерелаGoulding, Celia W., Michael R. Sawaya, Angineh Parseghian, Vincent Lim, David Eisenberg, and Dominique Missiakas. "Thiol−Disulfide Exchange in an Immunoglobulin-like Fold: Structure of the N-Terminal Domain of DsbD†,‡." Biochemistry 41, no. 22 (June 2002): 6920–27. http://dx.doi.org/10.1021/bi016038l.
Повний текст джерелаHemmis, Casey, Mehmet Berkmen, Markus Eser, and Joel Schildbach. "TrbB from Conjugative Plasmid F: A Representative of a New Class of Dsbd-Dependent Disulfide Isomerases." Biophysical Journal 100, no. 3 (February 2011): 193a. http://dx.doi.org/10.1016/j.bpj.2010.12.1271.
Повний текст джерелаStevens, Julie M., Euan H. Gordon, and Stuart J. Ferguson. "Overproduction of CcmABCDEFGH restores cytochromecmaturation in a DsbD deletion strain ofE. coli: another route for reductant?" FEBS Letters 576, no. 1-2 (September 11, 2004): 81–85. http://dx.doi.org/10.1016/j.febslet.2004.08.067.
Повний текст джерелаStelzl, Lukas S., Despoina A. I. Mavridou, Stuart J. Ferguson, Andrew J. Baldwin, Mark S. P. Sansom, and Christina Redfield. "Studying the Conformational Equilibrium of the N-Terminal Domain of Dsbd by NMR and Computer Simulation." Biophysical Journal 108, no. 2 (January 2015): 184a. http://dx.doi.org/10.1016/j.bpj.2014.11.1017.
Повний текст джерелаMavridou, Despoina A. I., Julie M. Stevens, Stuart J. Ferguson, and Christina Redfield. "Active-site Properties of the Oxidized and Reduced C-terminal Domain of DsbD Obtained by NMR Spectroscopy." Journal of Molecular Biology 370, no. 4 (July 2007): 643–58. http://dx.doi.org/10.1016/j.jmb.2007.04.038.
Повний текст джерелаRaczko, Anna M., Janusz M. Bujnicki, Marcin Pawłowski, Renata Godlewska, Magdalena Lewandowska, and Elżbieta K. Jagusztyn-Krynicka. "Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria." Microbiology 151, no. 1 (January 1, 2005): 219–31. http://dx.doi.org/10.1099/mic.0.27483-0.
Повний текст джерелаKadokura, Hiroshi, Lorenzo Nichols, and Jon Beckwith. "Mutational Alterations of the Key cis Proline Residue That Cause Accumulation of Enzymatic Reaction Intermediates of DsbA, a Member of the Thioredoxin Superfamily." Journal of Bacteriology 187, no. 4 (February 15, 2005): 1519–22. http://dx.doi.org/10.1128/jb.187.4.1519-1522.2005.
Повний текст джерелаHemmis, C. W., M. Berkmen, M. Eser, and J. F. Schildbach. "TrbB from Conjugative Plasmid F Is a Structurally Distinct Disulfide Isomerase That Requires DsbD for Redox State Maintenance." Journal of Bacteriology 193, no. 18 (July 8, 2011): 4588–97. http://dx.doi.org/10.1128/jb.00351-11.
Повний текст джерелаSardesai, Abhijit A., and J. Gowrishankar. "trans-Acting Mutations in Loci Other than kdpDE That Affect kdp Operon Regulation inEscherichia coli: Effects of Cytoplasmic Thiol Oxidation Status and Nucleoid Protein H-NS on kdpExpression." Journal of Bacteriology 183, no. 1 (January 1, 2001): 86–93. http://dx.doi.org/10.1128/jb.183.1.86-93.2001.
Повний текст джерелаTotsika, Makrina, Begoña Heras, Daniël J. Wurpel, and Mark A. Schembri. "Characterization of Two Homologous Disulfide Bond Systems Involved in Virulence Factor Biogenesis in Uropathogenic Escherichia coli CFT073." Journal of Bacteriology 191, no. 12 (April 17, 2009): 3901–8. http://dx.doi.org/10.1128/jb.00143-09.
Повний текст джерелаQuinternet, Marc, Pascale Tsan, Laure Selme-Roussel, Christophe Jacob, Sandrine Boschi-Muller, Guy Branlant, and Manh-Thong Cung. "Formation of the Complex between DsbD and PilB N-Terminal Domains from Neisseria meningitidis Necessitates an Adaptability of nDsbD." Structure 17, no. 7 (July 2009): 1024–33. http://dx.doi.org/10.1016/j.str.2009.05.011.
Повний текст джерелаKatzen, F., and J. Beckwith. "Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD." Proceedings of the National Academy of Sciences 100, no. 18 (August 18, 2003): 10471–76. http://dx.doi.org/10.1073/pnas.1334136100.
Повний текст джерелаBessette, Paul H., Ji Qiu, James C. A. Bardwell, James R. Swartz, and George Georgiou. "Effect of Sequences of the Active-Site Dipeptides of DsbA and DsbC on In Vivo Folding of Multidisulfide Proteins inEscherichia coli." Journal of Bacteriology 183, no. 3 (February 1, 2001): 980–88. http://dx.doi.org/10.1128/jb.183.3.980-988.2001.
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