Results 51 to 60 of about 11,073 (199)
Neurotransmitter release depends on the SNARE complex formed by syntaxin-1, synaptobrevin and SNAP-25, as well as on complexins, which bind to the SNARE complex and play active and inhibitory roles. A crystal structure of a Complexin-I fragment bearing a
Eric A Prinslow +2 more
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Binary polypeptide system for permanent and oriented protein immobilization. [PDF]
RIGHTS : This article is licensed under the BioMed Central licence at http://www.biomedcentral.com/about/license which is similar to the 'Creative Commons Attribution Licence'.
Bailes, Julian +6 more
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Complexin and Ca2+ stimulate SNARE-mediated membrane fusion [PDF]
Ca(2+)-triggered, synchronized synaptic vesicle fusion underlies interneuronal communication. Complexin is a major binding partner of the SNARE complex, the core fusion machinery at the presynapse. The physiological data on complexin, however, have been at odds with each other, making delineation of its molecular function difficult.
Yoon, TY Yoon, Tae-Young +5 more
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Background In sensory systems with broad bandwidths, polarized receptor cells utilize highly specialized organelles in their apical and basolateral compartments to transduce and ultimately transmit signals to the rest of the nervous system.
Zanazzi George, Matthews Gary
doaj +1 more source
Cholesterol-loaded nanoparticles ameliorate synaptic and cognitive function in Huntington's disease mice [PDF]
Brain cholesterol biosynthesis and cholesterol levels are reduced in mouse models of Huntington's disease (HD), suggesting that locally synthesized, newly formed cholesterol is less available to neurons.
Alessandro Vercelli +22 more
core +4 more sources
Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension
The SNARE complex enables the fusion of synaptic vesicles with presynaptic membrane via a zippering process that is modulated by the protein complexin, though the precise mechanism remains unclear.
Min Ju Shon, Haesoo Kim, Tae-Young Yoon
doaj +1 more source
Multiple factors maintain assembled trans-SNARE complexes in the presence of NSF and αSNAP
Neurotransmitter release requires formation of trans-SNARE complexes between the synaptic vesicle and plasma membranes, which likely underlies synaptic vesicle priming to a release-ready state.
Eric A Prinslow +4 more
doaj +1 more source
The use of single-molecule optical tweezers shows that complexin-1 shapes the assembly of the Synaptic-soluble N-ethylmaleimide-sensitive factor Attachment Receptor by multiple domains’ coordination.
Tongrui Hao +5 more
doaj +1 more source
The actin binding proteins cortactin and HS1 are dispensable for platelet actin nodule and megakaryocyte podosome formation [PDF]
A dynamic, properly organised actin cytoskeleton is critical for the production and haemostatic function of platelets. The Wiskott Aldrich Syndrome protein (WASp) and Actin-Related Proteins 2 & 3 Complex (Arp2/3 complex) are critical mediators of ...
Bem, Danai +5 more
core +4 more sources
Distinct domains of complexin I differentially regulate neurotransmitter release [PDF]
Complexins constitute a family of four synaptic high-affinity SNARE complex-binding proteins. They positively regulate a late, post-priming step in Ca2+-triggered synchronous neurotransmitter release, but the underlying molecular mechanisms are unclear.
Xue, M. +7 more
openaire +4 more sources

