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Article

Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene.

Molecular biology of the cell - 1 Feb 1992

Ng D T, Watowich S S, Lamb R A

Abstract excerpt

The endoplasmic reticulum (ER)-localized chaperone protein, GRP78-BiP, is involved in the folding and oligomerization of secreted and membrane proteins, including the simian virus 5 hemagglutinin-neuraminidase (HN) glycoprotein. To understand this interaction better, we have constructed a series...

Topics

Animals
Biological Transport
Carrier Proteins
Cell Line
DNA, Recombinant
Endoplasmic Reticulum
Endoplasmic Reticulum Chaperone BiP
Gene Expression Regulation
HN Protein
Heat-Shock Proteins
Molecular Chaperones
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Peptide Mapping

Protein Binding

RNA, Messenger

Source

Open in PubMed Open full text

Identifiers

PMID: 1550958
DOI: 10.1091/mbc.3.2.143
PMCID: PMC275514

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1550958-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene.PMID 1550958Read ↗

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