About: Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

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About: Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells Goto Sponge NotDistinct Permalink

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) im November 1999 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Nature (en) наукова стаття, опублікована в Nature в листопаді 1999 (uk)
publication date	wds:Q59098658-50DE5EE1-EEF8-4F57-9F6E-E54AB581482A
publication date	1999-11-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59098658-30FBFE2D-DF60-4A86-8777-8990BB02F580
language of work or name	English
exact match	wds:Q59098658-49D5CB10-67A7-421B-A4E2-13A255A7832E
exact match	https://scigraph.springernature.com/pub.10.1038/47062
cites work	wds:Q59098658-047CE2AA-1CBF-4737-A840-145FAE629172 wds:Q59098658-0E098AF6-D319-43F9-8F1A-E587D40D3CBB wds:Q59098658-3223B481-F850-4AFB-A8E8-4149B595BED9 wds:Q59098658-4328C6F2-3190-497C-956E-A18497BEDEC7 wds:Q59098658-51F72F5A-D176-4FBD-A962-7B25DB28A7C4 wds:Q59098658-5EC56F0E-1115-4236-9E60-53B44F80C674 wds:Q59098658-61507DF9-188D-4221-8D29-6A9D6647EB70 wds:Q59098658-89F1611D-186E-48DB-8878-C7AFEA7818C1 wds:Q59098658-A81570D7-ED32-4373-9134-17373216A882 wds:Q59098658-B5FC028F-52AE-464B-82F0-3DA4702EFC11 wds:Q59098658-C5828565-F92D-4FE7-A8D8-DB6A7CF65F87 wds:Q59098658-CA2CDE2C-B632-412E-BDA4-CA1AACCE92A6 wds:Q59098658-DF7915A0-45FB-4892-B424-E99F9BCD7767 wds:Q59098658-E5591A3A-5E1F-4790-9A85-71344C1C97FE wds:Q59098658-ED86040A-36FB-45DF-9F33-D72A51BC3BA6 wds:Q59098658-FC63E7F8-DB09-4696-8AC8-BDD3CA9A26BF
cites work	Protein folding in the cell Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum Protein disulphide isomerase: building bridges in protein folding ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin The endoplasmic reticulum as a protein-folding compartment Cotranslational folding and calnexin binding during glycoprotein synthesis An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins Assembly of the Semliki Forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitro Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase Assisted protein folding Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes The eS-Sence of -SH in the ER. Reexamination of the folding of BPTI: predominance of native intermediates. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins Diagonal polyacrylamide-dodecyl sulfate gel electrophoresis for the identification of ribosomal proteins crosslinked with methyl-4-mercaptobutyrimidate
author name string	wds:Q59098658-D74AAE32-316A-40AC-AAA8-6220DD6CBBFC
author name string	Helenius A
rdfs:label	Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells (en) Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells (nl)
skos:prefLabel	Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells (en) Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells (nl)
name	Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells (en) Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells (nl)
author	wds:Q59098658-77836A87-B6F5-4B3D-8483-2B226BC0CCC8
author	Maurizio Molinari
title	wds:Q59098658-E44434E3-A492-420A-8815-FB8ED8178149
title	Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells (en)
page(s)	wds:Q59098658-4630D8F9-6893-4C66-A21F-8394039E2890
page(s)	90-93
instance of	wds:Q59098658-DBC89296-340C-4477-8FF8-6CD4BED5C82D
instance of	scholarly article
PubMed ID	wds:Q59098658-1DB3294D-517C-4962-8ABD-D13F35CFE6E1
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10573423
PubMed ID	10573423
published in	wds:Q59098658-A1D45743-80A3-4205-A634-A764937CFAFD
published in	Nature
issue	wds:Q59098658-87BFDCB6-7268-46C3-8B53-2DD2D7220F0B
volume	wds:Q59098658-7B8D1D56-B0F2-45BF-8078-74EEE62075A0
issue	6757
volume	402
DOI	wds:Q59098658-D565D7B2-BCA0-4F24-9C21-7C0485C41A80
DOI	http://dx.doi.org/10.1038/47062
DOI	10.1038/47062
Dimensions Publication ID	wds:Q59098658-2045A676-28FC-4256-BCA0-D3FC5799C430
Dimensions Publication ID	1052299772
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59098658
is cites work of	Chaperones and folding of MHC class I molecules in the endoplasmic reticulum Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum Determinants in the envelope E protein and viral RNA helicase NS3 that influence the induction of apoptosis in response to infection with dengue type 1 virus. Manipulation of oxidative protein folding and PDI redox state in mammalian cells ERp57 is essential for efficient folding of glycoproteins sharing common structural domains Potential protein post-translational modification in ERp57: A phenotype marker for male fertility Folding and dimerization of hepatitis C virus E1 and E2 glycoproteins in stably transfected CHO cells Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity Processing, stability, and receptor binding properties of oligomeric envelope glycoprotein from a primary HIV-1 isolate Oxidative protein folding in eukaryotes: mechanisms and consequences Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex Substrate recognition by the protein disulfide isomerases The cotranslational maturation program for the type II membrane glycoprotein influenza neuraminidase Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility [corrected]. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57 Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase. Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface Quality Control and Protein Folding in the Secretory Pathway Search and destroy: ER quality control and ER-associated protein degradation Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. Protein disulfide bond formation in the cytoplasm during oxidative stress Sep15, a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase. Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells

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