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-Mouse (Murine) Gephyrin Anticorps:
anti-Rat (Rattus) Gephyrin Anticorps:
anti-Human Gephyrin Anticorps:
Vous arrivez à notre recherche pré-filtrée.
Study unravels the critical role for cellular signal transduction pathways in determining gephyrin SUMOylation, phosphorylation and acetylation at identified residues to regulate its scaffolding properties at specific postsynaptic sites and in turn regulating GABAergic function and plasticity.
Ablation of gephyrin result in the forebrain-specific loss of postsynaptic gamma2-GABAA receptors, reduces LTP and network excitability in the dentate gyrus.
adult mice lacking interleukin-1 receptor 1 (IL-1R1) exhibit increased expression of both the excitatory scaffolding protein postsynaptic density-95 (PSD-95) and inhibitory scaffolding proteingephyrin, respectively, in the hippocampus.
The results demonstrate that formation of GABAergic synapses containing a postsynaptic gephyrin scaffold is crucial for morphological differentiation, synaptic integration, and long-term survival of adult-born granule cells/
Data suggest that KIF5 regulates gephyrin sorting by a mechanism that involves GSK3 activity.
Pin1-dependent signaling represents a mechanism to modulate GABAergic transmission by regulating NL2/gephyrin interaction.
These results reveal a homeostatic mechanism through which activity regulates the dynamics and function of perisomatic inhibitory synapses, and they identify a CaMKII-dependent phosphorylation site on gephyrin.
study reveals that palmitoylation of gephyrin by DHHC-12 contributes to dynamic and functional modulation of GABAergic synapses
Within this network, collybistin can adopt open/active and closed/inactive conformations to act as a switchable adaptor that links gephyrin to plasma membrane phosphoinositides.
these findings suggest that gephyrin may be a key factor in BDNF-dependent GABAAR regulation in the amygdala.
Data suggest that the loss of neurotransmitter receptor clustering at inhibitory synapses causes the early lethality of gephyrin deficient mice.
Gephyrin is critical for glycine receptor clustering in hippocampal neurons.
gephyrin is required for the membrane insertion/stabilization of the GABAAR gamma2 subunit as well as for its subsequent localization in the postsynaptic membrane
Endogenous gephyrin undergoes proline-directed phosphorylation, which is followed by the recruitment of the peptidyl-prolyl isomerase Pin1.
gephyrin has splice-specific functions in molybdenum cofactor biosynthesis
Immunoelectron and confocal microscopy reveal that postsynaptic membrane specializations can be formed in the absence of gephyrin.
Using quantitative photoactivated localisation microscopy the authors found that alpha-1 and alpha-3 containing glycine receptors display the same alpha3:beta2 stoichiometry and gephyrin binding.
This study shown that the SNPs located in the rs723432 (Pallele=0.007; uncorrected) in the GPHN gene showed associated with Japanese individuals affected with schizophrenia.
these data reveal that IQSEC3 acts together with gephyrin to regulate inhibitory synapse development.
A missense mutation of gephyrin that was unable to synthesize MoCo and activate MoCo-dependent enzymes was identified.
A yin-yang haplotype pattern encompassing gephyrin consists of 284 divergent nucleotide states and both variants vary drastically from their mutual ancestral haplotype, suggesting rapid evolution.
The N-terminal region of GABRA3 and the GlyR beta subunit occupies the same binding site of gephyrin.
Results show that PKC-dependent phosphorylation of GAP43 plays a critical role in regulating postsynaptic gephyrin aggregation in developing GABAergic synapses.
Structural exonic microdeletions affecting the GPHN gene constitute a rare genetic risk factor for IGE and other neuropsychiatric disorders by an impairment of the GABAergic inhibitory synaptic transmission.
The enhancement of Cb-induced gephyrin clustering by GTP-TC10 does not depend on the guanine nucleotide exchange activity of Cb but involves an interaction that resembles reported interactions of other small GTPases with their effectors
abnormal accumulations of gephyrin are highly correlated with the neuropathologic diagnosis of Alzheimer disease in 17 AD versus 14 control cases. Furthermore, gephyrin accumulations were specific for AD.
Rare exonic deletions implicate the synaptic organizer Gephyrin (GPHN) in risk for autism, schizophrenia and seizures.
Extracellular signal-regulated kinase and glycogen synthase kinase 3beta regulate gephyrin postsynaptic aggregation and GABAergic synaptic function in a calpain-dependent mechanism
A reduction in the number of gephyrin clusters in primary neurons reduces GABA signaling.
Phosphorylation of gephyrin in hippocampal neurons by cyclin-dependent kinase CDK5 at Ser-270 is dependent on collybistin.
The gephyrin's presence in a cytosolic 600 kDa protein complex suggests that its metabolic and/or other non-neuronal functions are exerted in the cytoplasm and are not confined to a particular subcellular compartment.
Gephyrin expression is significantly lower in the temporal neocortex of temporal lobe epilepsy (TLE) patients and may be involved in the development of TLE.
The authors have identified a protein kinase C (PKC) phosphorylation site within the cytoplasmic domain of the beta-subunit of the GlyR (residue S403) that causes a reduction of the binding affinity between the receptor and gephyrin.
Data demonstrate the direct interaction between DYNLL1 and peptides derived from ASFV p54 and gephyrin interacting sequences.
we did not obtain evidence for gephyrin gene mutations in patients with temporal lobe epilepsy
Data are consistent with the postsynaptic gephyrin scaffold acting as a platform for protein phosphatase 1 (PP1), which regulates gephyrin cluster size by dephosphorylation of gephyrin- or cytoskeleton-associated proteins.
duplicated gephyrin genes mediate Moco biosynthesis and control postsynaptic clustering of glycine receptor
This gene encodes a neuronal assembly protein that anchors inhibitory neurotransmitter receptors to the postsynaptic cytoskeleton via high affinity binding to a receptor subunit domain and tubulin dimers. In nonneuronal tissues, the encoded protein is also required for molybdenum cofactor biosynthesis. Mutations in this gene may be associated with the neurological condition hyperplexia and also lead to molybdenum cofactor deficiency. Numerous alternatively spliced transcript variants encoding different isoforms have been described\; however, the full-length nature of all transcript variants is not currently known.
, putative glycine receptor-tubulin linker protein
, LOW QUALITY PROTEIN: gephyrin