Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher toutes les espèces
Afficher tous les synonymes
Sélectionnez vos espèces et l'application
anti-Human Complexin 1 Anticorps:
anti-Mouse (Murine) Complexin 1 Anticorps:
anti-Rat (Rattus) Complexin 1 Anticorps:
Vous arrivez à notre recherche pré-filtrée.
Findings do not support microRNA137 (MIR137) and complexin 1 (CPLX1) conferring susceptibility to schizophrenia in Han Chinese.
data define CPLX1 as a PD risk factor and provide functional insights into the role and regulation of blood SNCA levels. The new blood biomarkers of PARK4 in this Turkish family might become useful for PD prediction
Homozygous CPLX1 variants were identified in three patients with severe infantile myoclonic epilepsy and ID.
This study demonstrated that complexin-I influence cognitive function in early and late stages of Alzheimer's disease.
Study showed for the first time that neuro-Behcet's disease and Behcet's disease patients are inclined to display the GG genotype of the CPLX1 rs936551 polymorphism and to exhibit increased CPLX1 expression levels
Collectively these results demonstrate that CPX-1 is a secreted collagen-binding glycoprotein and provide a foundation for future studies investigating the function of CPX-1.
Studies indicate the role of the small regulatory factor complexin in Ca(2+)-dependent vesicle fusion and exocytosis.
Data support the the trans insertion model for complexin clamping.
Together with synaptotagmin 1, complexin synchronizes and stimulates rapid fusion of accumulated docked vesicles in response to physiological Ca(2+) concentrations.
The crystal structure of complexin bound to a prefusion SNAREpin mimetic shows that the accessory helix extends away from the SNAREpin in an 'open' conformation, binding another SNAREpin and inhibiting its assembly, to clamp fusion.
The 'central helix' of complexin is anchored to one SNARE complex, while its 'accessory helix' extends away at ~45 degrees and bridges to a second complex, occupying the vacant v-SNARE binding site to inhibit fusion.
role in synaptic vesicle exocytosis
altered immunoreactivity of this protein in prefrontal cortex in severe mental illness
description of what may represent a basic principle of the coupling mechanism in SNARE dependent exocytosis: a reversible clamping protein, complexin, that can freeze the SNAREpin, an assembled fusion-competent intermediate en route to fusion
CX1 level increased progressively across development
The response of CPLX1 and Foxp1 levels to SNCA deficiency supports the notion that these factors are regulated by altered physiological function of alpha-synuclein.
In the absence of Cplx1, synaptic vesicles remain unstable and prone to premature fusion.
Cplx 1 and 2 play a role in facilitating vesicle priming, and also lead to the new hypothesis that Cplxs may synchronize vesicle release by promoting coupling between secretory vesicles and calcium channels.
Complexin-1 carboxyl-terminal domain binds lipids through a novel protein motif by targeting complexin-1 to synaptic vesicles.
the ataxia in Cplx1(-/-) mice is likely to be due to pathological changes in both cerebellum and thalamus
These results suggest a complexin-dependent molecular mechanism for regulating AMPAR delivery to synapses
This study demonistrated that relatively large C-terminal complexin-1 sequence acts in priming and clamping synaptic exocytosis and demonstrate that the clamping function
The study uncovers an interaction between the complexin-1 N terminus and the SNARE complex C terminus, and shows that disrupting this interaction abolishes the facilitatory function of complexins in mouse neurons.
We studied the mRNA distribution of CPLXI and CPLXII in mouse brain. We show that while CPLXs are expressed in distinct cell populations they do not segregate with particular neurotransmitters or different classes of transmitter action
CPX I plays a critical role in beta-cells in the control of the stimulated-exocytosis of insulin.
Here we propose that complexin binding activates SNARE complexes into a metastable state and that Ca(2+) binding to synaptotagmin 1 triggers fast exocytosis by displacing complexin from metastable SNARE complexes.
Its co-localization and interaction with complexin I suggest that dynamin 2 may play a role during acrosome formation and/or acrosomal exocytosis.
early behavioural development of Cplx1(-/-) mice showed marked abnormalities
Complexin 1 knockout mice have pronounced deficits in social behaviours in addition to the severe motor and exploratory deficits.
complexin I functions in exocytosis in two related but morphologically distinct secretory processes.
Results indicate that distinct functional domains of copmplexin I differentially regulate synaptic exocytosis, and that CplxI carries out a crucial role in fine-tuning Ca2+-triggered fast neurotransmitter release.
Data show that Cplx1 in the locus Rgcs1 region is highly expressed in the ganglion cell layer and optic nerve head.
study shows in neuronal synapses, complexin simultaneously suppressed spontaneous membrane fusion & activated fast calcium ion-evoked fusion; complexin probably activates & clamps force transfer from assembled trans-SNARE complexes onto fusing membranes
Complexin 1 is required for faithful processing of sound onset and offset in the cochlear nucleus.
Proteins encoded by the complexin/synaphin gene family are cytosolic proteins that function in synaptic vesicle exocytosis. These proteins bind syntaxin, part of the SNAP receptor. The protein product of this gene binds to the SNAP receptor complex and disrupts it, allowing transmitter release.
, CPX I
, complexin I
, synaphin 2