Analysis of endoproteolytic cleavage and intracellular transport of human immunodeficiency virus type 1 envelope glycoproteins using mutant CD4 molecules bearing the transmembrane endoplasmic reticulum retention signal.

doi:10.1099/0022-1317-74-10-2085

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Article

Analysis of endoproteolytic cleavage and intracellular transport of human immunodeficiency virus type 1 envelope glycoproteins using mutant CD4 molecules bearing the transmembrane endoplasmic reticulum retention signal.

The Journal of general virology - 1 Oct 1993

Raja N U, Vincent M J, Jabbar M A

Abstract excerpt

We investigated endoproteolytic processing of the human immunodeficiency virus (HIV) envelope glycoprotein precursor, gp160, as well as envelope-mediated membrane fusion in the presence of CD4 molecules that were either partially or fully retained in the endoplasmic reticulum (ER). Pulse-chase an...

Topics

Amino Acid Sequence
Base Sequence
Biological Transport
CD4 Antigens
Cell Membrane
Endoplasmic Reticulum
Gene Products, env
Giant Cells
HIV Envelope Protein gp120
HIV Envelope Protein gp160
HIV Envelope Protein gp41

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

HIV-1

HeLa Cells

Humans

Molecular Sequence Data

Mutation

Protein Precursors

Viral Fusion Proteins

Source

Open in PubMed

Identifiers

PMID: 8409933
DOI: 10.1099/0022-1317-74-10-2085

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8409933-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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