Formation and transfer of disulphide bonds in living cells. - sprookjes - yvandenbroek - TriplyDB

Formation and transfer of disulphide bonds in living cells.

Formation and transfer of disulphide bonds in living cells.

http://www.wikidata.org/entity/Q34157680

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N-acetylcysteine in agriculture, a novel use for an old molecule: focus on controlling the plant-pathogen Xylella fastidiosa Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1 ERp16, an endoplasmic reticulum-resident thiol-disulfide oxidoreductase: biochemical properties and role in apoptosis induced by endoplasmic reticulum stress ERp57 is essential for efficient folding of glycoproteins sharing common structural domains Ascorbate as seen through plant evolution: the rise of a successful molecule?Insect prophenoloxidase: the view beyond immunity Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency A strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome c Cross-Link Formation of the Cysteine 228−Tyrosine 272 Catalytic Cofactor of Galactose Oxidase Does Not Require Dioxygen † ‡Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB Structural Insights into the Molecular Mechanisms of Cauliflower Mosaic Virus Transmission by Its Insect Vector Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer Structural basis for the redox sensitivity of the Mycobacterium tuberculosis SigK-RskA σ-anti-σ complex Crystal structure of the zinc-bound HhoA protease from Synechocystis sp. PCC 6803 NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance.Substrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase family Atp23 biogenesis reveals a chaperone-like folding activity of Mia40 in the IMS of mitochondria.Cellular disulfide bond formation in bioactive peptides and proteins ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins ERp57 is a multifunctional thiol-disulfide oxidoreductase Characterisation and expression of secretory phospholipase A2 group IB during ontogeny of Atlantic cod ( Gadus morhua)Endoplasmic reticulum redox state is not perturbed by pharmacological or pathological endoplasmic reticulum stress in live pancreatic β-cells The effect of tensile stress on the conformational free energy landscape of disulfide bonds Differential cooperative enzymatic activities of protein disulfide isomerase family in protein folding.Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding The unfolded protein response in immunity and inflammation Reversible Morphological Transformation between Polymer Nanocapsules and Thin Films through Dynamic Covalent Self-Assembly Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.Comparability of a three-dimensional structure in biopharmaceuticals using spectroscopic methods.Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.From structure to redox: The diverse functional roles of disulfides and implications in disease.The evolution of logic circuits for the purpose of protein contact map prediction Novel covalent bond in proteins: calculations on model systems question the bond stability.Electrochemistry-assisted top-down characterization of disulfide-containing proteins.

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P2860

Formation and transfer of disulphide bonds in living cells.

http://www.wikidata.org/entity/Q34157680

description

2002 nî lūn-bûn

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2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Formation and transfer of disulphide bonds in living cells.

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Formation and transfer of disulphide bonds in living cells.

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Formation and transfer of disulphide bonds in living cells.

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type

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Formation and transfer of disulphide bonds in living cells.

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Formation and transfer of disulphide bonds in living cells.

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Formation and transfer of disulphide bonds in living cells.

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Formation and transfer of disulphide bonds in living cells.

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Formation and transfer of disulphide bonds in living cells.

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Formation and transfer of disulphide bonds in living cells.

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Nature Reviews Molecular Cell Biology

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Formation and transfer of disulphide bonds in living cells.

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P2093

Carolyn S Sevier

http://www.w3.org/2001/XMLSchema#string

Chris A Kaiser

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P2860

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29

Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response

Manipulation of oxidative protein folding and PDI redox state in mammalian cells

ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family

Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR)

Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas

ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase

TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.

Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum

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836-847

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scholarly article

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10.1038/NRM954

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11

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3

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2002-11-01T00:00:00Z

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11050693

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1050543947

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12415301

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