Artykuły w czasopismach na temat „DSBF”
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Um, Si-Hyeon, Jin-Sik Kim, Kangseok Lee i Nam-Chul Ha. "Structure of a DsbF homologue fromCorynebacterium diphtheriae". Acta Crystallographica Section F Structural Biology Communications 70, nr 9 (29.08.2014): 1167–72. http://dx.doi.org/10.1107/s2053230x14016355.
Pełny tekst źródłaLin, Dongxia, Byoungkwan Kim i James M. Slauch. "DsbL and DsbI contribute to periplasmic disulfide bond formation in Salmonella enterica serovar Typhimurium". Microbiology 155, nr 12 (1.12.2009): 4014–24. http://dx.doi.org/10.1099/mic.0.032904-0.
Pełny tekst źródłaWalden, Patricia M., Andrew E. Whitten, Lakshmanane Premkumar, Maria A. Halili, Begoña Heras, Gordon J. King i 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, nr 3 (26.02.2019): 283–95. http://dx.doi.org/10.1107/s2059798318018442.
Pełny tekst źródłaKang, Yun Qing, Guang Fu Yin, Ke Feng Wang, Lin Luo, Li Liao i 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 (luty 2007): 483–86. http://dx.doi.org/10.4028/www.scientific.net/kem.330-332.483.
Pełny tekst źródłaStenson, Trevor H., i Alison A. Weiss. "DsbA and DsbC Are Required for Secretion of Pertussis Toxin by Bordetella pertussis". Infection and Immunity 70, nr 5 (maj 2002): 2297–303. http://dx.doi.org/10.1128/iai.70.5.2297-2303.2002.
Pełny tekst źródłaKurokawa, Yoichi, Hideki Yanagi i 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, nr 9 (1.09.2000): 3960–65. http://dx.doi.org/10.1128/aem.66.9.3960-3965.2000.
Pełny tekst źródłaDeshmukh, Meenal, Serdar Turkarslan, Donniel Astor, Maria Valkova-Valchanova i 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, nr 11 (1.06.2003): 3361–72. http://dx.doi.org/10.1128/jb.185.11.3361-3372.2003.
Pełny tekst źródłaSkórko-Glonek, Joanna, Anna Sobiecka-Szkatuła i Barbara Lipińska. "Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli." Acta Biochimica Polonica 53, nr 3 (1.10.2006): 585–89. http://dx.doi.org/10.18388/abp.2006_3331.
Pełny tekst źródłaAndersen, Catherine L., Anne Matthey‐Dupraz, Dominique Missiakas i 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, nr 1 (październik 1997): 121–32. http://dx.doi.org/10.1046/j.1365-2958.1997.5581925.x.
Pełny tekst źródłaChim, Nicholas, Robert Riley, Juliana The, Soyeon Im, Brent Segelke, Tim Lekin, Minmin Yu i in. "An Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression Analysis". Journal of Molecular Biology 396, nr 5 (marzec 2010): 1211–26. http://dx.doi.org/10.1016/j.jmb.2009.12.060.
Pełny tekst źródłaTan, Jacqueline, Ying Lu i James C. A. Bardwell. "Mutational Analysis of the Disulfide Catalysts DsbA and DsbB". Journal of Bacteriology 187, nr 4 (15.02.2005): 1504–10. http://dx.doi.org/10.1128/jb.187.4.1504-1510.2005.
Pełny tekst źródłaYu, Jun. "Inactivation of DsbA, but Not DsbC and DsbD, Affects the Intracellular Survival and Virulence ofShigella flexneri". Infection and Immunity 66, nr 8 (1.08.1998): 3909–17. http://dx.doi.org/10.1128/iai.66.8.3909-3917.1998.
Pełny tekst źródłaRaczko, Anna M., Janusz M. Bujnicki, Marcin Pawłowski, Renata Godlewska, Magdalena Lewandowska i 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, nr 1 (1.01.2005): 219–31. http://dx.doi.org/10.1099/mic.0.27483-0.
Pełny tekst źródłaKadokura, Hiroshi, Lorenzo Nichols i 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, nr 4 (15.02.2005): 1519–22. http://dx.doi.org/10.1128/jb.187.4.1519-1522.2005.
Pełny tekst źródłaSeo, Sang-Woo, Somi Yun, Myung-Gyu Kim, Mankyu Sung i Yejin Kim. "Screen-Based Sports Simulation Using Acoustic Source Localization". Applied Sciences 9, nr 15 (24.07.2019): 2970. http://dx.doi.org/10.3390/app9152970.
Pełny tekst źródłaTotsika, Makrina, Begoña Heras, Daniël J. Wurpel i Mark A. Schembri. "Characterization of Two Homologous Disulfide Bond Systems Involved in Virulence Factor Biogenesis in Uropathogenic Escherichia coli CFT073". Journal of Bacteriology 191, nr 12 (17.04.2009): 3901–8. http://dx.doi.org/10.1128/jb.00143-09.
Pełny tekst źródłaBessette, Paul H., Ji Qiu, James C. A. Bardwell, James R. Swartz i 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, nr 3 (1.02.2001): 980–88. http://dx.doi.org/10.1128/jb.183.3.980-988.2001.
Pełny tekst źródłaKishigami, Satoshi, Eiko Kanaya, Masakazu Kikuchi i Koreaki Ito. "DsbA-DsbB Interaction through Their Active Site Cysteines". Journal of Biological Chemistry 270, nr 29 (21.07.1995): 17072–74. http://dx.doi.org/10.1074/jbc.270.29.17072.
Pełny tekst źródłaFeissner, Robert E., Caroline S. Beckett, Jennifer A. Loughman i Robert G. Kranz. "Mutations in Cytochrome Assembly and Periplasmic Redox Pathways in Bordetella pertussis". Journal of Bacteriology 187, nr 12 (15.06.2005): 3941–49. http://dx.doi.org/10.1128/jb.187.12.3941-3949.2005.
Pełny tekst źródłaJiang, Bo-Le, Jiao Liu, Li-Feng Chen, Ying-Ying Ge, Xiao-Hong Hang, Yong-Qiang He, Dong-Jie Tang, Guang-Tao Lu i Ji-Liang Tang. "DsbB Is Required for the Pathogenesis Process of Xanthomonas campestris pv. campestris". Molecular Plant-Microbe Interactions® 21, nr 8 (sierpień 2008): 1036–45. http://dx.doi.org/10.1094/mpmi-21-8-1036.
Pełny tekst źródłaCho, Seung-Hyun, i 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, nr 14 (15.07.2006): 5066–76. http://dx.doi.org/10.1128/jb.00368-06.
Pełny tekst źródłaPremkumar, Lakshmanane, Begoña Heras, Wilko Duprez, Patricia Walden, Maria Halili, Fabian Kurth, David P. Fairlie i 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, nr 10 (20.09.2013): 1981–94. http://dx.doi.org/10.1107/s0907444913017800.
Pełny tekst źródłaUrban, Andreas, Martina Leipelt, Thorsten Eggert i Karl-Erich Jaeger. "DsbA and DsbC Affect Extracellular Enzyme Formation in Pseudomonas aeruginosa". Journal of Bacteriology 183, nr 2 (15.01.2001): 587–96. http://dx.doi.org/10.1128/jb.183.2.587-596.2001.
Pełny tekst źródłaGoldstone, D., P. W. Haebel, F. Katzen, M. W. Bader, J. C. A. Bardwell, J. Beckwith i P. Metcalf. "DsbC activation by the N-terminal domain of DsbD". Proceedings of the National Academy of Sciences 98, nr 17 (7.08.2001): 9551–56. http://dx.doi.org/10.1073/pnas.171315498.
Pełny tekst źródłaPanchakshari, Rohit A., Xuefei Zhang, Vipul Kumar, Zhou Du, Pei-Chi Wei, Jennifer Kao, Junchao Dong i 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, nr 4 (8.01.2018): 762–67. http://dx.doi.org/10.1073/pnas.1719988115.
Pełny tekst źródłaPuts, Gemma, Stuart Jarrett, Mary Leonard, Nicolette Matsangos, Devin Snyder, Ying Wang, Richard Vincent i in. "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, nr 16 (17.08.2020): 5896. http://dx.doi.org/10.3390/ijms21165896.
Pełny tekst źródłaKimball, Richard A., Laetitia Martin i Milton H. Saier Jr. "Reversing Transmembrane Electron Flow: The DsbD and DsbB Protein Families". Journal of Molecular Microbiology and Biotechnology 5, nr 3 (2003): 133–49. http://dx.doi.org/10.1159/000070263.
Pełny tekst źródłaJoly, John C., i James R. Swartz. "In Vitroandin VivoRedox States of theEscherichia coliPeriplasmic Oxidoreductases DsbA and DsbC". Biochemistry 36, nr 33 (sierpień 1997): 10067–72. http://dx.doi.org/10.1021/bi9707739.
Pełny tekst źródłaBushweller, John H. "Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA". Journal of Molecular Biology 432, nr 18 (sierpień 2020): 5091–103. http://dx.doi.org/10.1016/j.jmb.2020.04.008.
Pełny tekst źródłaInaba, Kenji, i Koreaki Ito. "Structure and mechanisms of the DsbB–DsbA disulfide bond generation machine". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, nr 4 (kwiecień 2008): 520–29. http://dx.doi.org/10.1016/j.bbamcr.2007.11.006.
Pełny tekst źródłaElton, Trevor C., Samantha J. Holland, Laura S. Frost i Bart Hazes. "F-Like Type IV Secretion Systems Encode Proteins with Thioredoxin Folds That Are Putative DsbC Homologues". Journal of Bacteriology 187, nr 24 (15.12.2005): 8267–77. http://dx.doi.org/10.1128/jb.187.24.8267-8277.2005.
Pełny tekst źródłaBader, M. W. "Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA". EMBO Journal 20, nr 7 (1.04.2001): 1555–62. http://dx.doi.org/10.1093/emboj/20.7.1555.
Pełny tekst źródłaInaba, K. "Structure and mechanism of the DsbB-DsbA protein disulfide generation system inE. coli". Acta Crystallographica Section A Foundations of Crystallography 64, a1 (23.08.2008): C111—C112. http://dx.doi.org/10.1107/s0108767308096426.
Pełny tekst źródłaSperling, Lindsay J., Ming Tang, Deborah A. Berthold, Anna E. Nesbitt, Robert B. Gennis i Chad M. Rienstra. "Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB". Journal of Physical Chemistry B 117, nr 20 (9.05.2013): 6052–60. http://dx.doi.org/10.1021/jp400795d.
Pełny tekst źródłaManchope, Marília F., Mariana M. Bertozzi, Sergio M. Borghi, Cíntia L. Handa, Mariana A. Queiroz-Cancian, Camila R. Ferraz, Sandra S. Mizokami i in. "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, nr 2 (11.02.2023): 167. http://dx.doi.org/10.3390/fermentation9020167.
Pełny tekst źródłaREID, Eleanor, Jeff COLE i Deborah J. EAVES. "The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly". Biochemical Journal 355, nr 1 (26.02.2001): 51–58. http://dx.doi.org/10.1042/bj3550051.
Pełny tekst źródłaDebarbieux, Laurent, i Jon Beckwith. "On the Functional Interchangeability, Oxidant versus Reductant, of Members of the Thioredoxin Superfamily". Journal of Bacteriology 182, nr 3 (1.02.2000): 723–27. http://dx.doi.org/10.1128/jb.182.3.723-727.2000.
Pełny tekst źródłaShevchik, Vladimir E., Isabelle Bortoli-Gernnan, Janine Robert-Baudouy, Sandrine Robinet, Frederic Barras i Guy Condemine. "Differential effect of dsbA and dsbC mutations on extracellular enzyme secretion in Erwinia chrysanthemi". Molecular Microbiology 16, nr 4 (maj 1995): 745–53. http://dx.doi.org/10.1111/j.1365-2958.1995.tb02435.x.
Pełny tekst źródłaInaba, K. "Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade". EMBO Journal 21, nr 11 (3.06.2002): 2646–54. http://dx.doi.org/10.1093/emboj/21.11.2646.
Pełny tekst źródłaYeh, Shin-Mei, Nayden Koon, Christopher Squire i Peter Metcalf. "Structures of the dimerization domains of theEscherichia colidisulfide-bond isomerase enzymes DsbC and DsbG". Acta Crystallographica Section D Biological Crystallography 63, nr 4 (16.03.2007): 465–71. http://dx.doi.org/10.1107/s0907444907003320.
Pełny tekst źródłaSone, Michio, Yoshinori Akiyama i Koreaki Ito. "Differentialin VivoRoles Played by DsbA and DsbC in the Formation of Protein Disulfide Bonds". Journal of Biological Chemistry 272, nr 16 (18.04.1997): 10349–52. http://dx.doi.org/10.1074/jbc.272.16.10349.
Pełny tekst źródłaInaba, Kenji, Satoshi Murakami, Mamoru Suzuki, Atsushi Nakagawa, Eiki Yamashita, Kengo Okada i Koreaki Ito. "Crystal Structure of the DsbB-DsbA Complex Reveals a Mechanism of Disulfide Bond Generation". Cell 127, nr 4 (listopad 2006): 789–801. http://dx.doi.org/10.1016/j.cell.2006.10.034.
Pełny tekst źródłaInaba, Kenji, Yoh-hei Takahashi i Koreaki Ito. "DsbB Elicits a Red-shift of Bound Ubiquinone during the Catalysis of DsbA Oxidation". Journal of Biological Chemistry 279, nr 8 (20.11.2003): 6761–68. http://dx.doi.org/10.1074/jbc.m310765200.
Pełny tekst źródłaBashirova, Anna, Subrata Pramanik, Pavel Volkov, Aleksandra Rozhkova, Vitaly Nemashkalov, Ivan Zorov, Alexander Gusakov, Arkady Sinitsyn, Ulrich Schwaneberg i Mehdi Davari. "Disulfide Bond Engineering of an Endoglucanase from Penicillium verruculosum to Improve Its Thermostability". International Journal of Molecular Sciences 20, nr 7 (30.03.2019): 1602. http://dx.doi.org/10.3390/ijms20071602.
Pełny tekst źródłaKadokura, H. "Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA". EMBO Journal 21, nr 10 (15.05.2002): 2354–63. http://dx.doi.org/10.1093/emboj/21.10.2354.
Pełny tekst źródłaHalili, Maria A., Prabhakar Bachu, Fredrik Lindahl, Chérine Bechara, Biswaranjan Mohanty, Robert C. Reid, Martin J. Scanlon, Carol V. Robinson, David P. Fairlie i Jennifer L. Martin. "Small Molecule Inhibitors of Disulfide Bond Formation by the Bacterial DsbA–DsbB Dual Enzyme System". ACS Chemical Biology 10, nr 4 (27.01.2015): 957–64. http://dx.doi.org/10.1021/cb500988r.
Pełny tekst źródłaYazawa, Kenjiro, Hiroyuki Furusawa i Yoshio Okahata. "Mechanism of Thiol–Disulfide Exchange Reactions between DsbA and DsbB over a Wide pH Range". Chemistry Letters 42, nr 3 (5.03.2013): 241–43. http://dx.doi.org/10.1246/cl.2013.241.
Pełny tekst źródłaBlasiak, Janusz, Joanna Szczepańska, Anna Sobczuk, Michal Fila i Elzbieta Pawlowska. "RIF1 Links Replication Timing with Fork Reactivation and DNA Double-Strand Break Repair". International Journal of Molecular Sciences 22, nr 21 (23.10.2021): 11440. http://dx.doi.org/10.3390/ijms222111440.
Pełny tekst źródłaCarrer, D., S. Lafont, J. L. Roujean, J. C. Calvet, C. Meurey, P. Le Moigne i 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, nr 2 (1.04.2012): 504–20. http://dx.doi.org/10.1175/jhm-d-11-059.1.
Pełny tekst źródłaSone, Michio, Yoshinori Akiyama i Koreaki Ito. "Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds." Journal of Biological Chemistry 273, nr 42 (październik 1998): 27756. http://dx.doi.org/10.1016/s0021-9258(19)59734-4.
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