Stability and Conformational Resilience of Protein Disulfide Isomerase
Biochemistry, 2019 Protein disulfide isomerase (PDI) is a redox-dependent protein with oxidoreductase and chaperone activities. It is a U-shaped protein with an abb'xa' structural organization in which the a and a' domains have CGHC active sites, the b and b' domains are involved with substrate binding, and x is a flexible linker. PDI exhibits substantial flexibility and
Jessica Guyette +3 more
openaire +3 more sources
AntioxidantsThiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie +3 more
doaj +1 more source
FEBS Open Bio, 2014 Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1,
Yayoi Onda, Yohei Kobori
doaj +1 more source
ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor [PDF]
, 2013 ERdj5 is a member of the protein disulfide isomerase family of proteins localized to the endoplasmic reticulum (ER) of mammalian cells. To date, only a limited number of substrates for ERdj5 are known.
Braakman, Ineke +4 more
core +1 more source
Folding of peptides and proteins: role of disulfide bonds, recent developments
Biomolecular Concepts, 2013 Disulfide-containing proteins are ideal models for studies of protein folding as the folding intermediates can be observed, trapped, and separated by HPLC during the folding reaction.
Hidaka Yuji, Shimamoto Shigeru
doaj +1 more source
nDsbD: a redox interaction hub in the Escherichia coli periplasm [PDF]
, 2018 .: DsbD is a redox-active protein of the inner Escherichia coli membrane possessing an N-terminal (nDsbD) and a C-terminal (cDsbD) periplasmic domain. nDsbD interacts with four different redox proteins involved in the periplasmic disulfide isomerization ...
Capitani, G. +3 more
core
Protein Disulfide Isomerase Is Required for Platelet-derived Growth Factor-induced Vascular Smooth Muscle Cell Migration, Nox1 NADPH Oxidase Expression, and RhoGTPase Activation [PDF]
, 2012 L Pescatore +5 more
openalex +1 more source
Structural and functional characterization of the oxidoreductase a-DsbA1 from wolbachia pipientis
, 2009 The α-proteobacterium Wolbachia pipientis is a highly successful intracellular endosymbiont of invertebrates that manipulates its host\u27s reproductive biology to facilitate its own maternal transmission. The fastidious nature of Wolbachia and the
Frei, Patrick +9 more
core +1 more source
Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide [PDF]
, 1999 Adrian Zai +3 more
openalex +1 more source
RETRACTED ARTICLE: Protein disulfide-isomerase A3 knockdown attenuates oxidized low-density lipoprotein-induced oxidative stress, inflammation and endothelial dysfunction in human umbilical vein endothelial cells by downregulating activating transcription factor 2 [PDF]
, 2022 Jing Jia +6 more
openalex +1 more source