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Keyword

DsbA

Description: A bacterial thiol-disulfide oxidoreductase that catalyzes disulfide bond formation in proteins, particularly in the periplasm of Gram-negative bacteria.
Wikidata ID: wiki/Q127783164
OpenAlex ID: keywords/dsba
Identification of a protein required for disulfide bond formation in vivo
1991 · James C.A. Bardwell, Karen McGovern, et al. · Cell · 979
Thiolate ligands in metallothionein confer redox activity on zinc clusters
1998 · Wolfgang Maret, Bert L. Vallee · Proceedings of the National Academy of Sciences · 577
Protein Disulfide Bond Formation in Prokaryotes
2003 · Hiroshi Kadokura, Federico Katzen, et al. · Annual Review of Biochemistry · 539
Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria
1997 · Fredrik Åslund, Kurt D. Berndt, et al. · Journal of Biological Chemistry · 415
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A pathway for disulfide bond formation in vivo.
1993 · J C Bardwell, J O Lee, et al. · Proceedings of the National Academy of Sciences · 409
Crystal structure of the DsbA protein required for disulphide bond formation in vivo
1993 · Jennifer L. Martin, James C. A. Bardwell, et al. · Nature · 390
Oxidative Protein Folding Is Driven by the Electron Transport System
1999 · Martin Bader, Wilson Muse, et al. · Cell · 385
Two GacA-Dependent Small RNAs Modulate the Quorum-Sensing Response in Pseudomonas aeruginosa
2006 · Elisabeth Kay, Bérénice Humair, et al. · Journal of Bacteriology · 321
pH-Dependent Expression of Periplasmic Proteins and Amino Acid Catabolism in Escherichia coli
2002 · Lauren M. Stancik, Dawn M. Stancik, et al. · Journal of Bacteriology · 318
Ionisation of Cysteine Residues at the Termini of Model α-Helical Peptides. Relevance to Unusual Thiol pKaValues in Proteins of the Thioredoxin Family
1995 · Tanja Kortemme, Thomas E. Creighton · Journal of Molecular Biology · 317
Why is DsbA such an oxidizing disulfide catalyst?
1995 · Ulla Grauschopf, Jakob R. Winther, et al. · Cell · 309
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Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system.
1997 · J Pogliano, A S Lynch, et al. · Genes & Development · 306
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An in vivo pathway for disulfide bond isomerization in Escherichia coli
1996 · Arne Rietsch, Dominique Belin, et al. · Proceedings of the National Academy of Sciences · 281
The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
1993 · Andre Zapun, James C. A. Bardwell, et al. · Biochemistry · 275
The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli.
1997 · P N Danese, T J Silhavy · Genes & Development · 273
Crystal Structure of the DsbB-DsbA Complex Reveals a Mechanism of Disulfide Bond Generation
2006 · Kenji Inaba, Satoshi Murakami, et al. · Cell · 258
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Structural and Functional Characterization of DsbC, a Protein Involved in Disulfide Bond Formation in Escherichia coli
1995 · Andre Zapun, Dominique Missiakas, et al. · Biochemistry · 257
The CXXC Motif: A Rheostat in the Active Site
1997 · Peter T. Chivers, Kenneth E. Prehoda, et al. · Biochemistry · 255
Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.
1993 · F E Dailey, H C Berg · Proceedings of the National Academy of Sciences · 247
Redox properties of protein disulfide isomerase (dsba) from escherichia coli
1993 · Martina Wunderlich, Rudi Glockshuber · Protein Science · 244
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Reactivity and Ionization of the Active Site Cysteine Residues of DsbA, a Protein Required for Disulfide Bond Formation in vivo
1994 · Jeffrey W. Nelson, Thomas E. Creighton · Biochemistry · 242
Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
1997 · Taeko Kobayashi, Satoshi Kishigami, et al. · Proceedings of the National Academy of Sciences · 240
The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.
1994 · D. Missiakas, C. Georgopoulos, et al. · The EMBO Journal · 240
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Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo.
1993 · D Missiakas, C Georgopoulos, et al. · Proceedings of the National Academy of Sciences · 237
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Snapshots of DsbA in Action: Detection of Proteins in the Process of Oxidative Folding
2004 · Hiroshi Kadokura, Hongping Tian, et al. · Science · 234
Works count: 872
Citation count: 30,060
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