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

Identification of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer.

Molecular biology of the cell - 1 May 2005

Graf Carmen T, Riedel Dietmar, Schmitt Hans Dieter, Jahn Reinhard

Abstract excerpt

Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes form bundles of four parallel alpha-helices. The central '0' layer of interacting amino acid side chains is highly conserved and contains one arginine and three glutamines, leading to the classification of SNAREs into R, Qa, Qb, and Qc-SNAREs. Replacing one of the glutamines with arginine in the yeast exocytotic SNARE complex...

Read the complete abstract on PubMed

Topics

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

Share to Conserved Sequence
Share to DNA, Fungal
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genes, Fungal

Share to Golgi Apparatus

Share to SNARE Proteins

Share to Temperature

Share to Vesicular Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 15728725
DOI: 10.1091/mbc.e04-09-0830
PMCID: PMC1087233

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer.PMID 15728725Read ↗

Exocytosis requires asymmetry in the central layer of the SNARE complex.Semantic proximity Read ↗

Testing the 3Q:1R “Rule”: Mutational Analysis of the Ionic “Zero” Layer in the Yeast Exocytic SNARE Complex Reveals No Requirement for ArginineSemantic proximity Read ↗

Yeast Golgi SNARE interactions are promiscuous.Semantic proximity Read ↗

Binding interactions control SNARE specificity in vivo.Semantic proximity Read ↗

Ykt6 functionally overlaps with vacuolar and exocytic R-SNAREs in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Structural bases of signal generation and transduction by the SPS amino acid sensor of Saccharomyces cerevisiae.Semantic proximity Read ↗

Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification.Semantic proximity Read ↗

A database of recombinant wild-type and mutant serpins.Semantic proximity Read ↗

Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda.Semantic proximity Read ↗

Structure-function study of the N-terminal domain of exocyst subunit Sec3.Semantic proximity Read ↗

The conserved C-terminus of Sss1p is required to maintain the endoplasmic reticulum permeability barrier.Semantic proximity Read ↗

Functional analysis of phosphorylation on Saccharomyces cerevisiae syntaxin 1 homologues Sso1p and Sso2p.Semantic proximity Read ↗

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