About: Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 01 January 1997

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1997 (uk) articolo scientifico (pubblicato il 1997) (it) article scientifique publié en 1997 (fr) im Januar 1997 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 1997 (ast) artikull shkencor i botuar më 01 janar 1997 (sq) scientific article published on 01 January 1997 (en)
publication date	wds:Q73009348-62564653-A05F-4401-9FFE-97858B6A1214
publication date	1997-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73009348-04C46993-8711-49A5-B37A-92B643F72769
language of work or name	English
cites work	wds:Q73009348-01F1F28D-ACD1-4265-A766-55ECF11E47D8 wds:Q73009348-1EE32720-97C6-4EB7-B402-5762DBFBE486 wds:Q73009348-2A489DA9-F15A-4D32-93C7-A98E353488A5 wds:Q73009348-495CEBF0-7054-44DD-9F00-9055A398D434 wds:Q73009348-5516BC33-ABAD-46C5-B5EA-D2D2C1173436 wds:Q73009348-5559B528-1583-4719-98EF-F72A89D380E8 wds:Q73009348-567B53B0-5B7E-4DE4-908A-012154C97353 wds:Q73009348-60AA1FC2-C0DD-4FBD-A468-9857C7CF28C2 wds:Q73009348-64DF4F3D-ADAF-48C0-BDE9-CF7B2E69E42E wds:Q73009348-70E5F20B-99B8-400D-A304-ACAA0D92FA97 wds:Q73009348-7231CA79-7F87-4E28-81C0-CA4022185E67 wds:Q73009348-778869C4-23E2-4038-99E7-7CBC2F183968 wds:Q73009348-7E2F98D9-25D1-4300-84D2-4B1C1A0DC156 wds:Q73009348-84843599-E388-4331-A71A-B7F02FE5899D wds:Q73009348-87A0DF8E-3870-4C3B-AD46-8231FC578F86 wds:Q73009348-9654EB76-E7D9-4133-816F-4DC803F55E34 wds:Q73009348-A0B6171F-9132-4BC5-BB6F-0C5A79A6618F wds:Q73009348-B01E32D4-7C37-403D-9C7F-F48E91C8936B wds:Q73009348-B1CF6992-C564-4F14-B200-3130607B0F85 wds:Q73009348-BAFF0E8F-2DF7-4A99-9915-39681112F08E wds:Q73009348-C213D941-0CA1-4B12-B3D0-1ED4345E7E34 wds:Q73009348-C27ACC53-351D-421C-BDFC-D64D7AAF4D6F wds:Q73009348-CBB68B0B-98E5-4EF8-BEF2-776DACDBEFEE wds:Q73009348-D0E06302-D701-4AA1-9E0C-9E96FC7352A9 wds:Q73009348-D1C2034C-1366-431C-A39B-D77F78AE759C wds:Q73009348-D9D6E197-37F8-4136-ACA7-DCD2DC1DB3B7 wds:Q73009348-D9E3AEBD-055D-4FC8-B131-43C02B24E8F8 wds:Q73009348-DC983888-F72D-4970-840C-F69C7AB7CF78 wds:Q73009348-E1621B7F-D62E-4E12-AC99-423EE4A61574 wds:Q73009348-E485DA15-CC7C-4438-BC81-558227C1B156 wds:Q73009348-E5CA5491-D5F8-4380-B24E-4086BB5FDA3C wds:Q73009348-E5E7AAA2-DFF7-4D53-A3C6-AC11CE54BD6E wds:Q73009348-EB7F0E46-FDE7-4983-8037-20A00387F886 wds:Q73009348-FD69DABB-7708-4A96-AFD8-4066C989CE34 wds:Q73009348-FE7A2498-5898-4CB0-A5B5-13C480F70D15
cites work	Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents Protein folding in the cell Retrieval of transmembrane proteins to the endoplasmic reticulum Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum Collagens: molecular biology, diseases, and potentials for therapy Association of folding intermediates of glycoproteins with calnexin during protein maturation Characterization of the oligosaccharides of prolyl hydroxylase, a microsomal glycoprotein Oxidized redox state of glutathione in the endoplasmic reticulum Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network Folding of VSV G protein: sequential interaction with BiP and calnexin A C-terminal signal prevents secretion of luminal ER proteins The bonds that tie: catalyzed disulfide bond formation Perturbation of cellular calcium induces secretion of luminal ER proteins Recycling of proteins between the endoplasmic reticulum and Golgi complex Protein folding and the regulation of signaling pathways On the preparation of cryosections for immunocytochemistry Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase Folding and association of proteins A human homologue of the yeast HDEL receptor Protein disaggregation mediated by heat-shock protein Hsp104. Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment Retention of membrane proteins by the endoplasmic reticulum The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase Condensation-sorting events in the rough endoplasmic reticulum of exocrine pancreatic cells Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone, BiP Monoclonal antibodies to human prolyl 4-hydroxylase A 115-kD polypeptide immunologically related to erythrocyte band 3 is present in Golgi membranes Protein folding. Folding helpers and unhelpful folders
author name string	wds:Q73009348-999C50BF-1266-493E-BD38-4071A8FE325E wds:Q73009348-9E5B0814-7C48-42AA-B26F-293F1B9D71AD wds:Q73009348-C7E2BD26-71BC-4B0D-97D9-F04BD176711C wds:Q73009348-CA8536ED-C1E4-4905-B993-8F22174A7C2D
author name string	R Myllylä M Suokas L Risteli S Kellokumpu
rdfs:label	Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum (en) Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum (nl) Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum (sq)
skos:prefLabel	Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum (en) Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum (nl) Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum (sq)
name	Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum (en) Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum (nl) Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum (sq)

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 190 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software