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Literature DB >> 12564920

Disulfide bond isomerization in prokaryotes.

Annie Hiniker¹, James C A Bardwell.

Abstract

Entities: Chemical Gene

Mesh：

Substances：

Year: 2003 PMID： 12564920 DOI： 10.1021/bi027141t

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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9 in total

1. Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.

Authors: Anna Rozhkova; Christian U Stirnimann; Patrick Frei; Ulla Grauschopf; René Brunisholz; Markus G Grütter; Guido Capitani; Rudi Glockshuber
Journal: EMBO J Date: 2004-04-01 Impact factor: 11.598

2. Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues.

Authors: Annie Hiniker; Didier Vertommen; James C A Bardwell; Jean-Francois Collet
Journal: J Bacteriol Date: 2006-10 Impact factor: 3.490

3. TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.

Authors: Casey W Hemmis; Mehmet Berkmen; Markus Eser; Joel F Schildbach
Journal: J Bacteriol Date: 2011-07-08 Impact factor: 3.490

4. Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC.

Authors: Pauline Leverrier; Jean-Paul Declercq; Katleen Denoncin; Didier Vertommen; Annie Hiniker; Seung-Hyun Cho; Jean-François Collet
Journal: J Biol Chem Date: 2011-03-16 Impact factor: 5.157

5. Chemical shift assignments of a reduced N-terminal truncation mutant of the disulfide bond isomerase TrbB from plasmid F, TrbBΔ29.

Authors: Casey W Hemmis; Nathan T Wright; Ananya Majumdar; Joel F Schildbach
Journal: Biomol NMR Assign Date: 2014-04-26 Impact factor: 0.746

Disulfide bond isomerization in prokaryotes.

1. Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.

2. Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues.

3. TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.

4. Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC.

5. Chemical shift assignments of a reduced N-terminal truncation mutant of the disulfide bond isomerase TrbB from plasmid F, TrbBΔ29.

Review 6. Thioredoxin-like proteins in F and other plasmid systems.

7. The genomics of disulfide bonding and protein stabilization in thermophiles.

8. Rheostat re-wired: alternative hypotheses for the control of thioredoxin reduction potentials.

9. Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.