Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member. - Wikidata - wikimedia - TriplyDB

Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.

Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.

http://www.wikidata.org/entity/Q34199026

about

The human protein disulfide isomerase gene family ERp16, an endoplasmic reticulum-resident thiol-disulfide oxidoreductase: biochemical properties and role in apoptosis induced by endoplasmic reticulum stress Identification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulum The human protein disulphide isomerase family: substrate interactions and functional properties Orphan proteins of unknown function in the mitochondrial intermembrane space proteome: New pathways and metabolic cross-talk Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.ERp57 is a multifunctional thiol-disulfide oxidoreductase ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57 The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)Genome-wide linkage analysis of global gene expression in loin muscle tissue identifies candidate genes in pigs.Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.On the molecular basis of D-bifunctional protein deficiency type III.Molecular mechanisms of HMW glutenin subunits from 1S(l) genome of Aegilops longissima positively affecting wheat breadmaking quality.A molecular specificity code for the three mammalian KDEL receptors.Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization.AGR3 in breast cancer: prognostic impact and suitable serum-based biomarker for early cancer detection.Versatility of the endoplasmic reticulum protein folding factory.Gene-based meta-analysis of genome-wide association studies implicates new loci involved in obesity Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A.ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations.Participation of the endoplasmic reticulum protein chaperone thio-oxidoreductase in gonadotropin-releasing hormone receptor expression at the plasma membrane Emerging roles for the pro-oncogenic anterior gradient-2 in cancer development.Chromatin immunoprecipitation (ChIP) on chip experiments uncover a widespread distribution of NF-Y binding CCAAT sites outside of core promoters.The primary substrate binding site in the b' domain of ERp57 is adapted for endoplasmic reticulum lectin association.Catalysis of protein disulfide bond isomerization in a homogeneous substrate Measuring protein reduction potentials using 15N HSQC NMR spectroscopy Emerging roles of protein disulfide isomerase in cancer.Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins.Purification and biochemical characterization of native ERp29 from rat liver.Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase.Biophysical characterization of ERp29. Evidence for a key structural role of cysteine 125.

P2860

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P2860

Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.

http://www.wikidata.org/entity/Q34199026

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2003 nî lūn-bûn

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2003 թուականի Մայիսին հրատարակուած գիտական յօդուած

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Journal of Biological Chemistry

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Functional characterization of ...... hioredoxin superfamily member.

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P2093

Anna-Kaisa Lappi

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Heli I Alanen

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Heli P Jäntti

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Lloyd W Ruddock

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Mark J Howard

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Richard A Williamson

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Sakari Kellokumpu

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Sini M Rautio

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P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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

ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif

Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum

High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae

Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization

NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism

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28912-28920

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278

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endoplasmic reticulum