Results 21 to 30 of about 11,278 (212)

Action of Complexin on SNARE Complex [PDF]

open access: yesJournal of Biological Chemistry, 2002
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

Complexin/Synaptotagmin Interplay Controls Acrosomal Exocytosis [PDF]

open access: yesJournal of Biological Chemistry, 2007
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]

open access: yesBiophysical Journal, 2010
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

CaMKIIalpha interacts with multi-PDZ domain protein MUPP1 in spermatozoa and prevents spontaneous acrosomal exocytosis [PDF]

open access: yes, 2009
The success of acrosomal exocytosis, a complex process with a variety of inter-related steps, relies on the coordinated interaction of participating signaling molecules.
Ackermann, Frauke   +5 more
core   +1 more source

The rab3A-22A chimera prevents sperm exocytosis by stabilizing open fusion pores [PDF]

open access: yes, 2016
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 induces a conformational change at the membrane-proximal C-terminal end of the SNARE complex

open access: yeseLife, 2016
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

Analysis of tripartite Synaptotagmin‐1‐SNARE‐complexin‐1 complexes in solution

open access: yesFEBS Open Bio, 2023
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

Pseudemys alabamensis [PDF]

open access: yes, 1985
Number of Pages: 2Integrative BiologyGeological ...
McCoy, C. J., Vogt, Richard C.
core   +1 more source

Regulation of Syntaxin3B-Mediated Membrane Fusion by T14, Munc18, and Complexin

open access: yesBiomolecules, 2023
Retinal neurons that form ribbon-style synapses operate over a wide dynamic range, continuously relaying visual information to their downstream targets.
Rajkishor Nishad   +4 more
doaj   +1 more source

Synergistic roles of Synaptotagmin-1 and complexin in calcium-regulated neuronal exocytosis

open access: yeseLife, 2020
Calcium (Ca2+)-evoked release of neurotransmitters from synaptic vesicles requires mechanisms both to prevent un-initiated fusion of vesicles (clamping) and to trigger fusion following Ca2+-influx. The principal components involved in these processes are
Sathish Ramakrishnan   +4 more
doaj   +1 more source

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