Results 31 to 40 of about 73,344 (342)
Summary: Exocytosis of synaptic vesicles and dense-core vesicles requires both the Munc13 and CAPS (Ca2+-dependent activator proteins for secretion) proteins.
Hao Zhou +5 more
doaj +1 more source
Mechanistic insights into the SNARE complex disassembly. [PDF]
Near-atomic resolution structure of the 20S complex reveals the mechanism of α-SNAP mediated disassembly of the SNARE complex.
Huang X +10 more
europepmc +4 more sources
ATP-independent Control of Vac8 Palmitoylation by a SNARE Subcomplex on Yeast Vacuoles [PDF]
Yeast vacuole fusion requires palmitoylated Vac8. We previously showed that Vac8 acylation occurs early in the fusion reaction, is blocked by antibodies against Sec18 (yeast N-ethylmaleimide-sensitive fusion protein (NSF)), and is mediated by the R-SNARE
Cristodero, Marina +5 more
core +1 more source
Amyloid-β Oligomers May Impair SNARE-Mediated Exocytosis by Direct Binding to Syntaxin 1a
Alzheimer’s disease (AD) is closely associated with synaptic dysfunction, and thus current treatments often aim to stimulate neurotransmission to improve cognitive impairment.
Yoosoo Yang +7 more
doaj +1 more source
SNARE complex in axonal guidance and neuroregeneration. [PDF]
Through complex mechanisms that guide axons to the appropriate routes towards their targets, axonal growth and guidance lead to neuronal system formation. These mechanisms establish the synaptic circuitry necessary for the optimal performance of the nervous system in all organisms. Damage to these networks can be repaired by neuroregenerative processes
Ulloa F +4 more
europepmc +4 more sources
Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana [PDF]
The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic vesicle tether at the plasma membrane before soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex formation.
De Rycke, Riet +7 more
core +2 more sources
α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle
Intracellular membrane fusion is mediated by dynamic assembly and disassembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). α-SNAP guides NSF to disassemble SNARE complexes after membrane fusion.
Lu Ma +7 more
doaj +1 more source
Munc18-1 induces conformational changes of syntaxin-1 in multiple intermediates for SNARE assembly
In neuronal exocytosis, SNARE assembly into a stable four-helix bundle drives membrane fusion. Previous studies have revealed that the SM protein Munc18-1 plays a critical role for precise SNARE assembly with the help of Munc13-1, but the underlying ...
Sanghwa Lee +7 more
doaj +1 more source
Stability, folding dynamics, and long-range conformational transition of the synaptic t-SNARE complex [PDF]
Synaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) couple their stepwise folding to fusion of synaptic vesicles with plasma membranes.
Jiao, J +8 more
core +1 more source
Traumatic brain injury (TBI) and the activation of secondary injury mechanisms have been linked to impaired cognitive function, which, as observed in TBI patients and animal models, can persist for months and years following the initial injury ...
Shaun W. Carlson +5 more
doaj +1 more source

