Results 181 to 190 of about 11,073 (199)

Ca²⁺/calmodulin and protein kinase C (PKC) reverse the vesicle fusion arrest by unmasking PIP₂. [PDF]

Sci Adv
Moussa HYA, Shin KC, Park Y.
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Eight decades of follow-up link life course exposures to proteomic organ ageing and longevity

Groves JW, Bot VA, Ding DY, Nicholas J, Farinas A, See-Oh H, James S, Wong A, Williams DM, King-Robson J, Chaturvedi N, Richards M, Wyss-Coray T, Schott JM.   +13 more
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Regulation of complexin 1 and complexin 2 in the developing human prefrontal cortex

Synapse, 2008
AbstractComplexin 1 (CX1) and complexin 2 (CX2) are presynaptic proteins that modulate neurotransmitter release and are used as markers of inhibitory and excitatory synapses, respectively. The aim of this study was to gain insight into the development of inhibitory and excitatory synapses in human prefrontal cortex (PFC) by examining the expression of ...
Kayvon, Salimi, Leisa A, Glantz, Robert M, Hamer, Thomas T, German, John H, Gilmore, L Fredrik, Jarskog   +5 more
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CLINICAL SYMPTOM COMPLEXIN VERTEBROGENIC LUMBOSACRAL RADICULOPATHY

Oriental Journal of Medicine and Pharmacology, 2022
Vertebrogenic lumbosacral radiculopathy, being a global problem of modern healthcare, occupies one of the leading places among the reasons for visiting doctors of various specialties and disability of people of different age categories. According to modern scientific medical research by a number of authors, an episode of back pain, at least once in a ...
M.B. Urinov, M.M. Usmonov
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Cloning and expression of a leech complexin

Gene Expression Patterns, 2004
Release of neurotransmitter from presynaptic nerve terminals is mediated by SNARE proteins, which are located on the vesicle and plasma membranes. These proteins form a SNARE complex thought to mediate membrane fusion. Complexin is a soluble protein essential for transmitter release, which has been postulated to bind to and stabilise the SNARE complex.
Dykes, Iain M, Davies, Jane A
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The absence of Complexin 3 and Complexin 4 differentially impacts the ON and OFF pathways in mouse retina

European Journal of Neuroscience, 2012
AbstractComplexins (Cplxs) regulate the speed and Ca2+‐sensitivity of synaptic vesicle fusion. It has been shown that all four known Cplxs are present at mouse retinal synapses – at conventional amacrine cell synapses (Cplx 1 to Cplx 3) and at photoreceptor and bipolar cell ribbon synapses (Cplx 3 and Cplx 4) [K. Reim et al. (2005)J.
Landgraf, I., Mühlhans, J., Dedek, K., Reim, K., Brandstätter, J., Ammermüller, J.   +5 more
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Complexin arrests a neighbor

Nature Structural & Molecular Biology, 2011
Mechanistic details about complexin's contradictory double life as both a facilitator and an inhibitor of SNARE-mediated synaptic vesicle fusion have been challenging to uncover. A series of studies in this issue addresses the problem by revealing a switchable complexin conformation in which fusion arrest occurs when complexin clamps neighboring SNAREs.
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Complexin Membrane Interactions: Implications for Synapse Evolution and Function

Journal of Molecular Biology, 2023
The molecules and mechanisms behind chemical synaptic transmission have been explored for decades. For several of the core proteins involved in synaptic vesicle fusion, we now have a reasonably detailed grasp of their biochemical, structural, and functional properties.
Justine A, Lottermoser, Jeremy S, Dittman   +1 more
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Characterization of the Complexin Membrane Interaction

2021
In neuronal exocytosis, neurotransmitters are released via membrane fusion between synaptic vesicle and presynaptic plasma membrane. Assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) drive this membrane fusion in a millisecond within the Ca2+ trigger.
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ComPLEXIN new targets for CIITA

Nature Immunology, 2003
Growing evidence indicates immune and nervous systems use common mechanisms to mediate intercellular communication. Adding to this list is the discovery that dendritic cells modulate T cell interactions through expression of the neuronal receptor plexin-A1, which is regulated by the transcriptional activator CIITA.
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