SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils.
Open Access
- 1 November 1994
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (44), 27427-27432
- https://doi.org/10.1016/s0021-9258(18)47003-2
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Implications of the SNARE hypothesis for intracellular membrane topology and dynamicsCurrent Biology, 1994
- Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxinNature, 1993
- Botulinum neurotoxins serotypes A and E cleave SNAP‐25 at distinct COOH‐terminal peptide bondsFEBS Letters, 1993
- Structure of the Chicken Gene for SNAP-25 Reveals Duplicated Exons Encoding Distinct Isoforms of the ProteinJournal of Molecular Biology, 1993
- Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion proteinNature, 1993
- A spring-loaded mechanism for the conformational change of influenza hemagglutininCell, 1993
- Epimorphin is related to a new class of neuronal and yeast vesicle targeting proteinsTrends in Biochemical Sciences, 1993
- SNAP receptors implicated in vesicle targeting and fusionNature, 1993
- Predicting Coiled Coils from Protein SequencesScience, 1991
- Continuous cultures of fused cells secreting antibody of predefined specificityNature, 1975