Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Internalization-competent influenza hemagglutinin mutants form complexes with clathrin-deficient multivalent AP-2 oligomers in live cells.

The Journal of biological chemistry - 27 Jul 2001

Keren T, Roth M G, Henis Y I

Abstract excerpt

Most membrane proteins are endocytosed through clathrin-coated pits via AP-2 adaptor complexes. However, little is known about the interaction of internalization signals with AP-2 in live cells in the absence of clathrin lattices. To investigate this issue, we employed cells cotransfected with pairs of antigenically distinct influenza hemagglutinin (HA) mutants containing different internalization signals of the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adaptor Proteins, Vesicular Transport
Share to Clathrin

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cytoplasm

Share to Dimerization

Share to Dopamine Antagonists

Share to Hemagglutinin Glycoproteins, Influenza Virus

Share to Microscopy, Fluorescence

Share to Precipitin Tests

Source

Identifiers

PMID: 11369772
DOI: 10.1074/jbc.M102235200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Internalization-competent influenza hemagglutinin mutants form complexes with clathrin-deficient multivalent AP-2 oligomers in live cells.PMID 11369772Read ↗

Dynamic or stable interactions of influenza hemagglutinin mutants with coated pits. Dependence on the internalization signal but not on aggregation.Semantic proximity Read ↗

Transmembrane Domain Length of Influenza a Virus M2 Does Not Determine Its Non-Lipid Raft Localization.Semantic proximity Read ↗

Mutation of a raft-targeting signal in the transmembrane region retards transport of influenza virus hemagglutinin through the Golgi.Semantic proximity Read ↗

Cholesterol binding to the transmembrane region of a group 2 HA of Influenza virus is essential for virus replication affecting both virus assembly and HA’s fusion activitySemantic proximity Read ↗

Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL.Semantic proximity Read ↗

Influenza-virus membrane fusion by cooperative fold-back of stochastically induced hemagglutinin intermediates.Semantic proximity Read ↗

Endocytosis of chimeric influenza virus hemagglutinin proteins that lack a cytoplasmic recognition feature for coated pits.Semantic proximity Read ↗

The heads of the measles virus attachment protein move to transmit the fusion-triggering signal.Semantic proximity Read ↗

A Defect in Influenza A Virus Particle Assembly Specific to Primary Human MacrophagesSemantic proximity Read ↗

Reversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusion.Semantic proximity Read ↗

Co-localization analysis of complex formation among membrane proteins by computerized fluorescence microscopy: application to immunofluorescence co-patching studies.Semantic proximity Read ↗

Evidence from lateral mobility studies for dynamic interactions of a mutant influenza hemagglutinin with coated pits.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.