Associated Papers
SNAP-25 disease variants affect synaptic transmission by destabilizing SNARE complexes within a multimeric SNARE ring.
Vold VA et al.
Cell Reports, 2026
Synaptobrevin-2 disease variants reveal spatial constraints within the presynaptic active zone.
Guzikowski NJ et al.
Proceedings of the National Academy of Sciences of the United States of America, 2025
41166419 (PubMed )
Supplement: pnas.2507347122.sapp.pdf
Intrinsic Disorder of the Neuronal SNARE Protein SNAP25a in its Pre-fusion Conformation.
Stief T et al.
Journal of Molecular Biology, 2023
Complexin-1 regulated assembly of single neuronal SNARE complex revealed by single-molecule optical tweezers.
Hao T et al.
Communications Biology, 2023
36750663 (PubMed )
Supplement: 42003_2023_4506_MOESM1_ESM.pdf
Stability profile of the neuronal SNARE complex reflects its potency to drive fast membrane fusion.
Wang S et al.
Biophysical Journal, 2022
SNARE assembly enlightened by cryo-EM structures of a synaptobrevin-Munc18-1-syntaxin-1 complex.
Stepien KP et al.
Science Advances, 2022
Re-examining how Munc13-1 facilitates opening of syntaxin-1.
Magdziarek M et al.
Protein Science : a Publication of the Protein Society, 2020
Multiple factors maintain assembled trans-SNARE complexes in the presence of NSF and αSNAP.
Prinslow EA et al.
Elife, 2019
Two Disease-Causing SNAP-25B Mutations Selectively Impair SNARE C-terminal Assembly.
Rebane AA et al.
Journal of Molecular Biology, 2018
Munc18a does not alter fusion rates mediated by neuronal SNAREs, synaptotagmin, and complexin.
Zhang Y et al.
The Journal of Biological Chemistry, 2015
Identification of SNAP-47, a novel Qbc-SNARE with ubiquitous expression.
Holt M et al.
The Journal of Biological Chemistry, 2006
Sequential N- to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles.
Sørensen JB et al.
The Embo Journal, 2006
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