Artigos de revistas sobre o tema "DSBF"
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Um, Si-Hyeon, Jin-Sik Kim, Kangseok Lee e Nam-Chul Ha. "Structure of a DsbF homologue fromCorynebacterium diphtheriae". Acta Crystallographica Section F Structural Biology Communications 70, n.º 9 (29 de agosto de 2014): 1167–72. http://dx.doi.org/10.1107/s2053230x14016355.
Texto completo da fonteLin, Dongxia, Byoungkwan Kim e James M. Slauch. "DsbL and DsbI contribute to periplasmic disulfide bond formation in Salmonella enterica serovar Typhimurium". Microbiology 155, n.º 12 (1 de dezembro de 2009): 4014–24. http://dx.doi.org/10.1099/mic.0.032904-0.
Texto completo da fonteWalden, Patricia M., Andrew E. Whitten, Lakshmanane Premkumar, Maria A. Halili, Begoña Heras, Gordon J. King e 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, n.º 3 (26 de fevereiro de 2019): 283–95. http://dx.doi.org/10.1107/s2059798318018442.
Texto completo da fonteKang, Yun Qing, Guang Fu Yin, Ke Feng Wang, Lin Luo, Li Liao e Ya Dong Yao. "A Study of Bone-Like Apatite Formation on β-TCP/PLLA Scaffold in Static and Dynamic Simulated Body Fluid". Key Engineering Materials 330-332 (fevereiro de 2007): 483–86. http://dx.doi.org/10.4028/www.scientific.net/kem.330-332.483.
Texto completo da fonteStenson, Trevor H., e Alison A. Weiss. "DsbA and DsbC Are Required for Secretion of Pertussis Toxin by Bordetella pertussis". Infection and Immunity 70, n.º 5 (maio de 2002): 2297–303. http://dx.doi.org/10.1128/iai.70.5.2297-2303.2002.
Texto completo da fonteKurokawa, Yoichi, Hideki Yanagi e 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, n.º 9 (1 de setembro de 2000): 3960–65. http://dx.doi.org/10.1128/aem.66.9.3960-3965.2000.
Texto completo da fonteDeshmukh, Meenal, Serdar Turkarslan, Donniel Astor, Maria Valkova-Valchanova e 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, n.º 11 (1 de junho de 2003): 3361–72. http://dx.doi.org/10.1128/jb.185.11.3361-3372.2003.
Texto completo da fonteSkórko-Glonek, Joanna, Anna Sobiecka-Szkatuła e Barbara Lipińska. "Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli." Acta Biochimica Polonica 53, n.º 3 (1 de outubro de 2006): 585–89. http://dx.doi.org/10.18388/abp.2006_3331.
Texto completo da fonteAndersen, Catherine L., Anne Matthey‐Dupraz, Dominique Missiakas e 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, n.º 1 (outubro de 1997): 121–32. http://dx.doi.org/10.1046/j.1365-2958.1997.5581925.x.
Texto completo da fonteChim, Nicholas, Robert Riley, Juliana The, Soyeon Im, Brent Segelke, Tim Lekin, Minmin Yu et al. "An Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression Analysis". Journal of Molecular Biology 396, n.º 5 (março de 2010): 1211–26. http://dx.doi.org/10.1016/j.jmb.2009.12.060.
Texto completo da fonteTan, Jacqueline, Ying Lu e James C. A. Bardwell. "Mutational Analysis of the Disulfide Catalysts DsbA and DsbB". Journal of Bacteriology 187, n.º 4 (15 de fevereiro de 2005): 1504–10. http://dx.doi.org/10.1128/jb.187.4.1504-1510.2005.
Texto completo da fonteYu, Jun. "Inactivation of DsbA, but Not DsbC and DsbD, Affects the Intracellular Survival and Virulence ofShigella flexneri". Infection and Immunity 66, n.º 8 (1 de agosto de 1998): 3909–17. http://dx.doi.org/10.1128/iai.66.8.3909-3917.1998.
Texto completo da fonteRaczko, Anna M., Janusz M. Bujnicki, Marcin Pawłowski, Renata Godlewska, Magdalena Lewandowska e 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, n.º 1 (1 de janeiro de 2005): 219–31. http://dx.doi.org/10.1099/mic.0.27483-0.
Texto completo da fonteKadokura, Hiroshi, Lorenzo Nichols e 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, n.º 4 (15 de fevereiro de 2005): 1519–22. http://dx.doi.org/10.1128/jb.187.4.1519-1522.2005.
Texto completo da fonteSeo, Sang-Woo, Somi Yun, Myung-Gyu Kim, Mankyu Sung e Yejin Kim. "Screen-Based Sports Simulation Using Acoustic Source Localization". Applied Sciences 9, n.º 15 (24 de julho de 2019): 2970. http://dx.doi.org/10.3390/app9152970.
Texto completo da fonteTotsika, Makrina, Begoña Heras, Daniël J. Wurpel e Mark A. Schembri. "Characterization of Two Homologous Disulfide Bond Systems Involved in Virulence Factor Biogenesis in Uropathogenic Escherichia coli CFT073". Journal of Bacteriology 191, n.º 12 (17 de abril de 2009): 3901–8. http://dx.doi.org/10.1128/jb.00143-09.
Texto completo da fonteBessette, Paul H., Ji Qiu, James C. A. Bardwell, James R. Swartz e 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, n.º 3 (1 de fevereiro de 2001): 980–88. http://dx.doi.org/10.1128/jb.183.3.980-988.2001.
Texto completo da fonteKishigami, Satoshi, Eiko Kanaya, Masakazu Kikuchi e Koreaki Ito. "DsbA-DsbB Interaction through Their Active Site Cysteines". Journal of Biological Chemistry 270, n.º 29 (21 de julho de 1995): 17072–74. http://dx.doi.org/10.1074/jbc.270.29.17072.
Texto completo da fonteFeissner, Robert E., Caroline S. Beckett, Jennifer A. Loughman e Robert G. Kranz. "Mutations in Cytochrome Assembly and Periplasmic Redox Pathways in Bordetella pertussis". Journal of Bacteriology 187, n.º 12 (15 de junho de 2005): 3941–49. http://dx.doi.org/10.1128/jb.187.12.3941-3949.2005.
Texto completo da fonteJiang, Bo-Le, Jiao Liu, Li-Feng Chen, Ying-Ying Ge, Xiao-Hong Hang, Yong-Qiang He, Dong-Jie Tang, Guang-Tao Lu e Ji-Liang Tang. "DsbB Is Required for the Pathogenesis Process of Xanthomonas campestris pv. campestris". Molecular Plant-Microbe Interactions® 21, n.º 8 (agosto de 2008): 1036–45. http://dx.doi.org/10.1094/mpmi-21-8-1036.
Texto completo da fonteCho, Seung-Hyun, e 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, n.º 14 (15 de julho de 2006): 5066–76. http://dx.doi.org/10.1128/jb.00368-06.
Texto completo da fontePremkumar, Lakshmanane, Begoña Heras, Wilko Duprez, Patricia Walden, Maria Halili, Fabian Kurth, David P. Fairlie e Jennifer L. Martin. "Rv2969c, essential for optimal growth inMycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases". Acta Crystallographica Section D Biological Crystallography 69, n.º 10 (20 de setembro de 2013): 1981–94. http://dx.doi.org/10.1107/s0907444913017800.
Texto completo da fonteUrban, Andreas, Martina Leipelt, Thorsten Eggert e Karl-Erich Jaeger. "DsbA and DsbC Affect Extracellular Enzyme Formation in Pseudomonas aeruginosa". Journal of Bacteriology 183, n.º 2 (15 de janeiro de 2001): 587–96. http://dx.doi.org/10.1128/jb.183.2.587-596.2001.
Texto completo da fonteGoldstone, D., P. W. Haebel, F. Katzen, M. W. Bader, J. C. A. Bardwell, J. Beckwith e P. Metcalf. "DsbC activation by the N-terminal domain of DsbD". Proceedings of the National Academy of Sciences 98, n.º 17 (7 de agosto de 2001): 9551–56. http://dx.doi.org/10.1073/pnas.171315498.
Texto completo da fontePanchakshari, Rohit A., Xuefei Zhang, Vipul Kumar, Zhou Du, Pei-Chi Wei, Jennifer Kao, Junchao Dong e Frederick W. Alt. "DNA double-strand break response factors influence end-joining features of IgH class switch and general translocation junctions". Proceedings of the National Academy of Sciences 115, n.º 4 (8 de janeiro de 2018): 762–67. http://dx.doi.org/10.1073/pnas.1719988115.
Texto completo da fontePuts, Gemma, Stuart Jarrett, Mary Leonard, Nicolette Matsangos, Devin Snyder, Ying Wang, Richard Vincent et al. "Metastasis Suppressor NME1 Modulates Choice of Double-Strand Break Repair Pathways in Melanoma Cells by Enhancing Alternative NHEJ while Inhibiting NHEJ and HR". International Journal of Molecular Sciences 21, n.º 16 (17 de agosto de 2020): 5896. http://dx.doi.org/10.3390/ijms21165896.
Texto completo da fonteKimball, Richard A., Laetitia Martin e Milton H. Saier Jr. "Reversing Transmembrane Electron Flow: The DsbD and DsbB Protein Families". Journal of Molecular Microbiology and Biotechnology 5, n.º 3 (2003): 133–49. http://dx.doi.org/10.1159/000070263.
Texto completo da fonteJoly, John C., e James R. Swartz. "In Vitroandin VivoRedox States of theEscherichia coliPeriplasmic Oxidoreductases DsbA and DsbC". Biochemistry 36, n.º 33 (agosto de 1997): 10067–72. http://dx.doi.org/10.1021/bi9707739.
Texto completo da fonteBushweller, John H. "Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA". Journal of Molecular Biology 432, n.º 18 (agosto de 2020): 5091–103. http://dx.doi.org/10.1016/j.jmb.2020.04.008.
Texto completo da fonteInaba, Kenji, e Koreaki Ito. "Structure and mechanisms of the DsbB–DsbA disulfide bond generation machine". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, n.º 4 (abril de 2008): 520–29. http://dx.doi.org/10.1016/j.bbamcr.2007.11.006.
Texto completo da fonteElton, Trevor C., Samantha J. Holland, Laura S. Frost e Bart Hazes. "F-Like Type IV Secretion Systems Encode Proteins with Thioredoxin Folds That Are Putative DsbC Homologues". Journal of Bacteriology 187, n.º 24 (15 de dezembro de 2005): 8267–77. http://dx.doi.org/10.1128/jb.187.24.8267-8277.2005.
Texto completo da fonteBader, M. W. "Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA". EMBO Journal 20, n.º 7 (1 de abril de 2001): 1555–62. http://dx.doi.org/10.1093/emboj/20.7.1555.
Texto completo da fonteInaba, K. "Structure and mechanism of the DsbB-DsbA protein disulfide generation system inE. coli". Acta Crystallographica Section A Foundations of Crystallography 64, a1 (23 de agosto de 2008): C111—C112. http://dx.doi.org/10.1107/s0108767308096426.
Texto completo da fonteSperling, Lindsay J., Ming Tang, Deborah A. Berthold, Anna E. Nesbitt, Robert B. Gennis e Chad M. Rienstra. "Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB". Journal of Physical Chemistry B 117, n.º 20 (9 de maio de 2013): 6052–60. http://dx.doi.org/10.1021/jp400795d.
Texto completo da fonteManchope, Marília F., Mariana M. Bertozzi, Sergio M. Borghi, Cíntia L. Handa, Mariana A. Queiroz-Cancian, Camila R. Ferraz, Sandra S. Mizokami et al. "Fermented (By Monascus purpureus or Aspergillus oryzae) and Non-Fermented Defatted Soybean Flour Extracts: Biological Insight and Mechanism Differences in Inflammatory Pain and Peritonitis". Fermentation 9, n.º 2 (11 de fevereiro de 2023): 167. http://dx.doi.org/10.3390/fermentation9020167.
Texto completo da fonteREID, Eleanor, Jeff COLE e Deborah J. EAVES. "The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly". Biochemical Journal 355, n.º 1 (26 de fevereiro de 2001): 51–58. http://dx.doi.org/10.1042/bj3550051.
Texto completo da fonteDebarbieux, Laurent, e Jon Beckwith. "On the Functional Interchangeability, Oxidant versus Reductant, of Members of the Thioredoxin Superfamily". Journal of Bacteriology 182, n.º 3 (1 de fevereiro de 2000): 723–27. http://dx.doi.org/10.1128/jb.182.3.723-727.2000.
Texto completo da fonteShevchik, Vladimir E., Isabelle Bortoli-Gernnan, Janine Robert-Baudouy, Sandrine Robinet, Frederic Barras e Guy Condemine. "Differential effect of dsbA and dsbC mutations on extracellular enzyme secretion in Erwinia chrysanthemi". Molecular Microbiology 16, n.º 4 (maio de 1995): 745–53. http://dx.doi.org/10.1111/j.1365-2958.1995.tb02435.x.
Texto completo da fonteInaba, K. "Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade". EMBO Journal 21, n.º 11 (3 de junho de 2002): 2646–54. http://dx.doi.org/10.1093/emboj/21.11.2646.
Texto completo da fonteYeh, Shin-Mei, Nayden Koon, Christopher Squire e Peter Metcalf. "Structures of the dimerization domains of theEscherichia colidisulfide-bond isomerase enzymes DsbC and DsbG". Acta Crystallographica Section D Biological Crystallography 63, n.º 4 (16 de março de 2007): 465–71. http://dx.doi.org/10.1107/s0907444907003320.
Texto completo da fonteSone, Michio, Yoshinori Akiyama e Koreaki Ito. "Differentialin VivoRoles Played by DsbA and DsbC in the Formation of Protein Disulfide Bonds". Journal of Biological Chemistry 272, n.º 16 (18 de abril de 1997): 10349–52. http://dx.doi.org/10.1074/jbc.272.16.10349.
Texto completo da fonteInaba, Kenji, Satoshi Murakami, Mamoru Suzuki, Atsushi Nakagawa, Eiki Yamashita, Kengo Okada e Koreaki Ito. "Crystal Structure of the DsbB-DsbA Complex Reveals a Mechanism of Disulfide Bond Generation". Cell 127, n.º 4 (novembro de 2006): 789–801. http://dx.doi.org/10.1016/j.cell.2006.10.034.
Texto completo da fonteInaba, Kenji, Yoh-hei Takahashi e Koreaki Ito. "DsbB Elicits a Red-shift of Bound Ubiquinone during the Catalysis of DsbA Oxidation". Journal of Biological Chemistry 279, n.º 8 (20 de novembro de 2003): 6761–68. http://dx.doi.org/10.1074/jbc.m310765200.
Texto completo da fonteBashirova, Anna, Subrata Pramanik, Pavel Volkov, Aleksandra Rozhkova, Vitaly Nemashkalov, Ivan Zorov, Alexander Gusakov, Arkady Sinitsyn, Ulrich Schwaneberg e Mehdi Davari. "Disulfide Bond Engineering of an Endoglucanase from Penicillium verruculosum to Improve Its Thermostability". International Journal of Molecular Sciences 20, n.º 7 (30 de março de 2019): 1602. http://dx.doi.org/10.3390/ijms20071602.
Texto completo da fonteKadokura, H. "Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA". EMBO Journal 21, n.º 10 (15 de maio de 2002): 2354–63. http://dx.doi.org/10.1093/emboj/21.10.2354.
Texto completo da fonteHalili, Maria A., Prabhakar Bachu, Fredrik Lindahl, Chérine Bechara, Biswaranjan Mohanty, Robert C. Reid, Martin J. Scanlon, Carol V. Robinson, David P. Fairlie e Jennifer L. Martin. "Small Molecule Inhibitors of Disulfide Bond Formation by the Bacterial DsbA–DsbB Dual Enzyme System". ACS Chemical Biology 10, n.º 4 (27 de janeiro de 2015): 957–64. http://dx.doi.org/10.1021/cb500988r.
Texto completo da fonteYazawa, Kenjiro, Hiroyuki Furusawa e Yoshio Okahata. "Mechanism of Thiol–Disulfide Exchange Reactions between DsbA and DsbB over a Wide pH Range". Chemistry Letters 42, n.º 3 (5 de março de 2013): 241–43. http://dx.doi.org/10.1246/cl.2013.241.
Texto completo da fonteBlasiak, Janusz, Joanna Szczepańska, Anna Sobczuk, Michal Fila e Elzbieta Pawlowska. "RIF1 Links Replication Timing with Fork Reactivation and DNA Double-Strand Break Repair". International Journal of Molecular Sciences 22, n.º 21 (23 de outubro de 2021): 11440. http://dx.doi.org/10.3390/ijms222111440.
Texto completo da fonteCarrer, D., S. Lafont, J. L. Roujean, J. C. Calvet, C. Meurey, P. Le Moigne e I. F. Trigo. "Incoming Solar and Infrared Radiation Derived from METEOSAT: Impact on the Modeled Land Water and Energy Budget over France". Journal of Hydrometeorology 13, n.º 2 (1 de abril de 2012): 504–20. http://dx.doi.org/10.1175/jhm-d-11-059.1.
Texto completo da fonteSone, Michio, Yoshinori Akiyama e Koreaki Ito. "Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds." Journal of Biological Chemistry 273, n.º 42 (outubro de 1998): 27756. http://dx.doi.org/10.1016/s0021-9258(19)59734-4.
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