Sharpin, a novel postsynaptic density protein that directly interacts with the shank family of proteins
about
Transcriptional and functional complexity of Shank3 provides a molecular framework to understand the phenotypic heterogeneity of SHANK3 causing autism and Shank3 mutant miceSHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complexSHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosisCharacterization of Staufen 1 ribonucleoprotein complexesDGKι regulates presynaptic release during mGluR-dependent LTDSHARPIN is an endogenous inhibitor of β1-integrin activationThe ankyrin repeat as molecular architecture for protein recognitionCrystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerizationCrystallographic and Biochemical Analysis of the Ran-binding Zinc Finger DomainStructural Analysis of SHARPIN, a Subunit of a Large Multi-protein E3 Ubiquitin Ligase, Reveals a Novel Dimerization Function for the Pleckstrin Homology SuperfoldActin-Dependent Alterations of Dendritic Spine Morphology in ShankopathiesThe Shank family of postsynaptic density proteins interacts with and promotes synaptic accumulation of the beta PIX guanine nucleotide exchange factor for Rac1 and Cdc42Sipl1 and Rbck1 are novel Eya1-binding proteins with a role in craniofacial developmentThe adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to promote inhibitory synapse developmentSHANK proteins: roles at the synapse and in autism spectrum disorder.Altered Striatal Synaptic Function and Abnormal Behaviour in Shank3 Exon4-9 Deletion Mouse Model of AutismSHANK3 mutations identified in autism lead to modification of dendritic spine morphology via an actin-dependent mechanism.Shank-interacting protein-like 1 promotes tumorigenesis via PTEN inhibition in human tumor cells.Shank3-mutant mice lacking exon 9 show altered excitation/inhibition balance, enhanced rearing, and spatial memory deficit.Sharpin contributes to TNFα dependent NFκB activation and anti-apoptotic signalling in hepatocytesSHARPIN is essential for cytokine production, NF-κB signaling, and induction of Th1 differentiation by dendritic cells.Constructing and decoding unconventional ubiquitin chains.Inhibition of NF-κB signaling retards eosinophilic dermatitis in SHARPIN-deficient mice.Chronic Proliferative Dermatitis in Mice: NFκB Activation Autoinflammatory DiseaseSystems analysis identifies an essential role for SHANK-associated RH domain-interacting protein (SHARPIN) in macrophage Toll-like receptor 2 (TLR2) responses.SHARPIN regulates mitochondria-dependent apoptosis in keratinocytes.Elevation of SIPL1 (SHARPIN) Increases Breast Cancer RiskMutually Exclusive Roles of SHARPIN in Integrin Inactivation and NF-κB Signaling.Crystallization of SHARPIN using an automated two-dimensional grid screen for optimization.SHARPIN is a key regulator of immune and inflammatory responsesIdentification and functional characterization of rare SHANK2 variants in schizophrenia.SHARPIN controls regulatory T cells by negatively modulating the T cell antigen receptor complexSharpin promotes hepatocellular carcinoma progression via transactivation of Versican expression.SHARPIN Facilitates p53 Degradation in Breast Cancer Cells.The emerging role of linear ubiquitination in cell signaling.Linear ubiquitination-mediated NF-κB regulation and its related disorders.The multifaceted role of the E3 ubiquitin ligase HOIL-1: beyond linear ubiquitination.The Sharpin interactome reveals a role for Sharpin in lamellipodium formation via the Arp2/3 complex.SHANK proteins limit integrin activation by directly interacting with Rap1 and R-Ras.SHARPIN overexpression induces tumorigenesis in human prostate cancer LNCaP, DU145 and PC-3 cells via NF-κB/ERK/Akt signaling pathway.
P2860
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P2860
Sharpin, a novel postsynaptic density protein that directly interacts with the shank family of proteins
description
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2001
@ast
im Februar 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2001/02/01)
@sk
vědecký článek publikovaný v roce 2001
@cs
wetenschappelijk artikel (gepubliceerd op 2001/02/01)
@nl
наукова стаття, опублікована в лютому 2001
@uk
مقالة علمية (نشرت في فبراير 2001)
@ar
name
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@ast
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@en
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@nl
type
label
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@ast
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@en
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@nl
prefLabel
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@ast
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@en
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@nl
P2093
P3181
P356
P1476
Sharpin, a novel postsynaptic ...... h the shank family of proteins
@en
P2093
P304
P3181
P356
10.1006/MCNE.2000.0940
P50
P577
2001-02-01T00:00:00Z