CHAPTER 1.1. Disulfide Bonds in Protein Folding and Stability [PDF]
, 2018 Disulfide bonds are unique among post-translational modifications, as they add covalent crosslinks to the polypeptide chain. Accordingly, they can exert pronounced effects on protein folding and stability. This is of particular importance for secreted or
Sub Cellular Protein Chemistry +7 more
core +1 more source
Overexpression of thiol/disulfide isomerases enhances membrane fusion directed by the Newcastle disease virus fusion protein [PDF]
, 2009 Newcastle disease virus (NDV) fusion (F) protein directs membrane fusion, which is required for virus entry and cell-cell fusion. We have previously shown that free thiols are present in cell surface-expressed NDV F protein and that blocking the ...
Cullen, Lori McGinnes +2 more
core +1 more source
PLoS ONE, 2013 Protein disulfide isomerases comprise a large family of enzymes responsible for catalyzing the proper oxidation and folding of newly synthesized proteins in the endoplasmic reticulum (ER). Protein disulfide isomerase-related (PDIR) protein (also known as
Roohi Vinaik +2 more
doaj +1 more source
Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans. [PDF]
, 2007 Protein disulfide isomerase (PDI) is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum.
Page, Antony P. +5 more
core +1 more source
Redox Biology, 2023 Protein disulfide isomerases (PDIs) catalyze redox reactions that reduce, oxidize, or isomerize disulfide bonds and act as chaperones of proteins as they fold. The characteristic features of PDIs are the presence of one or more catalytic thioredoxin (TRX)
Natalia Zamorano Cuervo +1 more
doaj +1 more source
Engineering and characterization of disulfide bond isomerases in Escherichia coli [PDF]
, 2009 textDisulfide bond formation is an essential process for the folding and biological activity of most extracellular proteins; however, it may become the limiting step when the production of these proteins is attempted in heterologous hosts such as ...
Arredondo, Silvia A.
core +3 more sources
A Protein Disulfide Isomerase Controls Neuronal Migration through Regulation of Wnt Secretion
Cell Reports, 2019 Summary: Appropriate Wnt morphogen secretion is required to control animal development and homeostasis. Although correct Wnt globular structure is essential for secretion, proteins that directly mediate Wnt folding and maturation remain uncharacterized ...
Nanna Torpe +6 more
doaj +1 more source
Analysis of Disulfide Bond Formation [PDF]
, 2017 In this unit, protocols are provided for detection of disulfide bond formation in cultures of intact cells and in an in vitro translation system containing isolated microsomes or semi-permeabilized cells.
Sub Cellular Protein Chemistry +9 more
core +2 more sources
Endoplasmic reticulum H₂O₂ : Ero1-driven generation and GPx-mediated detoxification [PDF]
, 2014 Endoplasmic reticulum (ER) oxidoreductin 1 alpha (Ero1alpha) is an ER-resident oxidase, which utilizes molecular oxygen (O2) as terminal electron acceptor to produce disulfide bonds and hydrogen peroxide (H2O2).
Ramming, Thomas
core +1 more source
The physiological functions of mammalian endoplasmic oxidoreductin 1: on disulfides and more [PDF]
, 2012 Significance: The oxidative process of disulfide-bond formation is essential for the folding of most secretory and membrane proteins in the endoplasmic reticulum (ER).
Ramming, Thomas +1 more
core +1 more source