The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin.

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Article

The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin.

The Journal of biological chemistry - 15 Mar 1990

Lazarovits J, Shia S P, Ktistakis N, Lee M S, Bird C, Roth M G

Abstract excerpt

Eleven chimeric proteins were created in which the transmembrane, the cytoplasmic, or both topological domains of the influenza virus hemagglutinin (HA) were replaced with those from five other glycoproteins. All of the chimeric HAs reached the cell surface but appeared to differ in the degree to which they were stably folded. Comparisons of the rates of folding, passage into the Golgi, and arrival at the plasma...

Topics

Amino Acid Sequence
Biological Transport
Cell Membrane
Cloning, Molecular
Endoplasmic Reticulum
Exocytosis
Golgi Apparatus
Hemagglutinin Glycoproteins, Influenza Virus
Hemagglutinins, Viral
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Macromolecular Substances

Molecular Sequence Data

Mutation

Protein Conformation

Recombinant Proteins

Structure-Activity Relationship

Trypsin

Source

Open in PubMed

Identifiers

PMID: 2307684

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2307684-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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