Results 41 to 50 of about 174,472 (299)
The N-terminal shuttle domain of Erv1 determines the affinity for Mia40 and mediates electron transfer to the catalytic Erv1 core in yeast mitochondria [PDF]
, 2010 Erv1 and Mia40 constitute the two important components of the disulfide relay system that mediates oxidative protein folding in the mitochondrial intermembrane space. Mia40 is the import receptor that recognizes the substrates introducing disulfide bonds
Aivaliotis, M. +3 more
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Molecules, 2020 The polypeptide backbone of proteins is held together by two main types of covalent bonds: the peptide bonds that link the amino acid residues and the disulfide bonds that link pairs of cysteine amino acids. Disulfide bonds form as a protein folds in the
Philip J. Hogg
doaj +1 more source
The quiescin sulfhydryl oxidase (hQSOX1b) tunes the expression of resistin-like molecule alpha (RELM-α or mFIZZ1) in a wheat germ cell-free extract. [PDF]
PLoS ONE, 2013 Although disulfide bond formation in proteins is one of the most common types of post-translational modifications, the production of recombinant disulfide-rich proteins remains a challenge.
Wael Gad +9 more
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NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra Naja naja atra [PDF]
, 2013 The Taiwan cobra (Naja naja atra) chymotrypsin inhibitor (NACI) consists of 57 amino acids and is related to other Kunitz-type inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and Bungarus fasciatus fraction IX (BF9), another chymotrypsin ...
Chang, Long-Sen +3 more
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Disulfide bond isomerization in prokaryotes
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2008 Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase.
Gleiter, Stefan, Bardwell, James C.A.
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Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]
, 2006 During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Andrew C. Gill +44 more
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Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space [PDF]
, 2017 Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways.
Cardenas-Rodriguez, Mauricio +1 more
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Native disulfide bond formation in proteins [PDF]
Current Opinion in Chemical Biology, 2000 Native disulfide bond formation is critical for the proper folding of many proteins. Recent studies using newly identified protein oxidants, folding catalysts, and mutant cells provide insight into the mechanism of oxidative protein folding in vivo. This insight promises new strategies for more efficient protein production.
K J, Woycechowsky, R T, Raines
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, 2015 The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formation in eukaryotic cells lacking endoplasmic reticulum oxidase 1 (ERO1).
Araki +33 more
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Bioengineering, 2021 Glucose oxidase (GOx) holds considerable advantages for various applications. Nevertheless, the thermal instability of the enzyme remains a grand challenge, impeding the success in applications outside the well-controlled laboratories, particularly in ...
Sirawit Ittisoponpisan +1 more
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