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protein disulfide isomerase activity

Known as: disulphide bond formation, protein thiol-disulphide exchange, protein thiol-disulfide exchange 
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins. [EC:5.3.4.1, GOC:vw, http://en.wikipedia.org/wiki… 
National Institutes of Health

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Protein Disulfide-Isomerases

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2006
2006
Defects in a quinol oxidase lead to loss of KatC catalase activity in Pseudomonas aeruginosa: KatC activity is temperature dependent and it requires an intact disulphide bond formation system.
2002
2002
Controlling pore assembly of staphylococcal γ‐haemolysin by low temperature and by disulphide bond formation in double‐cysteine LukF mutants
Staphylococcal LukF and Hlg2 are water‐soluble monomers of γ‐haemolysin that assemble into oligomeric pores on the erythrocyte… 
Highly Cited
1999
Highly Cited
1999
A single amino acid change in the plant alternative oxidase alters the specificity of organic acid activation
1999
1999
Homozygous Cys542→Arg substitution in GPIIIa in a Swiss patient with type I Glanzmann's thrombasthenia
Glanzmann's thrombasthenia (GT) arises from a qualitative or quantitative defect in the GPIIb–IIIa complex (integrin αIIbβ3), the… 
Review
1997
Review
1997
Protein folding coupled to disulphide bond formation.
Protein folding that is coupled to disulphide bond formation has many experimental advantages. In particular, the kinetic roles… 
Highly Cited
1996
Highly Cited
1996
Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c‐type cytochrome except in the presence of disulphide compounds
1993
1993
Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo.
DsbA is a 21 kDa protein that facilitates disulphide bond formation and is required for the correct folding and stability of a… 
1993
1993
A model catalyst of protein disulphide bond formation
Highly Cited
1984
Highly Cited
1984
Protein disulphide-isomerase and the formation of native disulphide bonds.
Disulphide bonds are found in practically every class of extracellular protein, and the formation of disulphide bonds must be… 
Highly Cited
1983
Highly Cited
1983
The roles of sugar phosphates and thiol-reducing systems in the control of reticulocyte protein synthesis.
The study of gel-filtered rabbit reticulocyte lysates and lysates which have been passed through 2′5′ ADP-Sepharose columns has… 
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