Results 21 to 30 of about 11,073 (199)
A Conceptual Review of Naturally Occurring Toxins and Venoms as Peptide Blockers to Combat Chronic Low Back Pain. [PDF]
This review explores the therapeutic potential of naturally occurring venom‐derived peptides, particularly from reptiles and insects, as novel calcium channel blockers for managing chronic low back pain caused by intervertebral disc degeneration.
Melrose J +4 more
europepmc +2 more sources
Action of Complexin on SNARE Complex [PDF]
Calcium-dependent synaptic vesicle exocytosis requires three SNARE (soluble N-ethylmaleimide-sensitive-factor attachment protein receptor) proteins: synaptobrevin/vesicle-associated membrane protein in the vesicular membrane and syntaxin and SNAP-25 in the presynaptic membrane.
Kuang, Hu +3 more
openaire +2 more sources
Expression of Concern: Complexin in ivermectin resistance in body lice [PDF]
PLOS Genetics Editors.
doaj +2 more sources
Complexin/Synaptotagmin Interplay Controls Acrosomal Exocytosis [PDF]
La secreción regulada es un proceso fundamental que subyace a la función de muchos tipos de células. En particular, la exocitosis acrosómica en espermatozoides de mamíferos es esencial para la fertilización de óvulos. La secreción regulada requiere proteínas SNARE y, en las neuronas, también sinaptotagmina I y complexina.
Carlos M. Roggero +5 more
openaire +2 more sources
Accessory Alpha-Helix of Complexin I Can Displace VAMP2 Locally in the Complexin-Snare Quaternary Complex [PDF]
The calcium-triggered neurotransmitter release requires three SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins: synaptobrevin 2 (or vesicle-associated membrane protein 2) on the synaptic vesicle and syntaxin 1 and SNAP-25 (synaptosome-associated protein of 25 kDa) at the presynaptic plasma membrane.
Lu, Bin, Song, Shuang, Shin, Yeon-Kyun
openaire +3 more sources
The rab3A-22A chimera prevents sperm exocytosis by stabilizing open fusion pores [PDF]
At the final stage of exocytotis, a fusion pore opens between the plasma and a secretory vesicle membranes; typically, when the pore dilates the vesicle releases its cargo.
Bustos, Matias Alberto +5 more
core +1 more source
Complexin regulates spontaneous and activates Ca2+-triggered neurotransmitter release, yet the molecular mechanisms are still unclear. Here we performed single molecule fluorescence resonance energy transfer experiments and uncovered two conformations of
Ucheor B Choi +4 more
doaj +1 more source
Three-dimensional structure of the complexin/snare complex [PDF]
During neurotransmitter release, the neuronal SNARE proteins synaptobrevin/VAMP, syntaxin, and SNAP-25 form a four-helix bundle, the SNARE complex, that pulls the synaptic vesicle and plasma membranes together possibly causing membrane fusion. Complexin binds tightly to the SNARE complex and is essential for efficient Ca(2+)-evoked neurotransmitter ...
Chen, Xiaocheng +6 more
openaire +3 more sources
Analysis of tripartite Synaptotagmin‐1‐SNARE‐complexin‐1 complexes in solution
Characterizing interactions of Synaptotagmin‐1 with the SNARE complex is crucial to understand the mechanism of neurotransmitter release. X‐ray crystallography revealed how the Synaptotagmin‐1 C2B domain binds to the SNARE complex through a so‐called ...
Klaudia Jaczynska +8 more
doaj +1 more source
Complexin is a small soluble presynaptic protein that interacts with neuronal SNARE proteins in order to regulate synaptic vesicle exocytosis. While the SNARE-binding central helix of complexin is required for both the inhibition of spontaneous fusion ...
David Snead +7 more
doaj +1 more source

