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

Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites.

Journal of neurochemistry - 1 Jun 1998

Ramjaun A R, McPherson P S

Abstract excerpt

Amphiphysin I and II are nerve terminal-enriched proteins that display src homology 3 domain-mediated interactions with dynamin and synaptojanin. It has been demonstrated that the amphiphysins also bind to clathrin, and we have proposed that this interaction may help to target synaptojanin and dy...

Read the complete abstract on PubMed

Topics

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

Share to Alternative Splicing
Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Nerve Tissue Proteins

Share to Polymerase Chain Reaction

Share to Sequence Deletion

Source

Identifiers

PMID: 9603201
DOI: 10.1046/j.1471-4159.1998.70062369.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-9603201-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites.PMID 9603201Read ↗

The vesicular acetylcholine transporter interacts with clathrin-associated adaptor complexes AP-1 and AP-2.Semantic proximity Read ↗

Nerve growth factor-induced phosphorylation of amphiphysin-1 by casein kinase 2 regulates clathrin-amphiphysin interactions.Semantic proximity Read ↗

Regulation of amphiphysin1 by mitogen-activated protein kinase: its significance in nerve growth factor receptor-mediated endocytosis.Semantic proximity Read ↗

Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila.Semantic proximity Read ↗

Dual interaction of synaptotagmin with mu2- and alpha-adaptin facilitates clathrin-coated pit nucleation.Semantic proximity Read ↗

Localized expression of amphiphysin Ir, a retina-specific variant of amphiphysin I, in the ribbon synapse and its functional implication.Semantic proximity Read ↗

A distributed set of interactions controls mu2 functionality in the role of AP-2 as a sorting adaptor in synaptic vesicle endocytosis.Semantic proximity Read ↗

A phosphatidylinositol (4,5)-bisphosphate binding site within mu2-adaptin regulates clathrin-mediated endocytosis.Semantic proximity Read ↗

The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein ModuleSemantic proximity Read ↗

Expression and protein-binding studies of the EEN gene family, new interacting partners for dynamin, synaptojanin and huntingtin proteins.Semantic proximity Read ↗

A Novel Sequence in AP180 and CALM Promotes Efficient Clathrin Binding and Assembly.Semantic proximity Read ↗

Endocytosis of synaptotagmin 1 is mediated by a novel, tryptophan-containing motif.Semantic proximity Read ↗

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