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

Synaptotagmin perturbs the structure of phospholipid bilayers.

Biochemistry - 19 Feb 2008

Shahin Victor, Datta Debajyoti, Hui Enfu, Henderson Robert M, Chapman Edwin R, Edwardson J Michael

Abstract excerpt

Synaptotagmin I (syt), an integral protein of the synaptic vesicle membrane, is believed to act as a Ca2+ sensor for neuronal exocytosis. Syt's cytoplasmic domain consists largely of two C2 domains, C2A and C2B. In response to Ca2+ binding, the C2 domains interact with membranes, becoming partial...

Read the complete abstract on PubMed

Topics

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

Share to DNA, Complementary
Share to AFM gene
Share to Lipid Bilayers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Atomic Force

Share to Molecular Structure

Share to Mutation

Share to Synaptotagmin I

Source

Open in PubMed Open full text

Identifiers

PMID: 18205405
DOI: 10.1021/bi701879g
PMCID: PMC3095487

Genes

AFM

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18205405-2026-09-02.2. 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

Synaptotagmin perturbs the structure of phospholipid bilayers.PMID 18205405Read ↗

Interaction of synaptotagmin with lipid bilayers, analyzed by single-molecule force spectroscopy.Semantic proximity Read ↗

Synaptotagmin oligomerization is essential for calcium control of regulated exocytosis.Semantic proximity Read ↗

Synaptotagmin-mediated bending of the target membrane is a critical step in Ca(2+)-regulated fusion.Semantic proximity Read ↗

Conformational dynamics of calcium-triggered activation of fusion by synaptotagmin.Semantic proximity Read ↗

The C2 domains of synaptotagmin--partners in exocytosis.Semantic proximity Read ↗

Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs.Semantic proximity Read ↗

Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.Semantic proximity Read ↗

The AD3 locus of synaptotagmin-1 C2 domains modulates domain stability.Semantic proximity Read ↗

synaptotagmin mutants reveal essential functions for the C2B domain in Ca2+-triggered fusion and recycling of synaptic vesicles in vivo.Semantic proximity Read ↗

Synaptotagmin-Ca2+ triggers two sequential steps in regulated exocytosis in rat PC12 cells: fusion pore opening and fusion pore dilation.Semantic proximity Read ↗

Functional and biochemical analysis of the C2 domains of synaptotagmin IV.Semantic proximity Read ↗

Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion.Semantic proximity Read ↗

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