Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein
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Actin-based motility of intracellular microbial pathogensThe Wiskott-Aldrich syndromeWIP remodeling actin behind the scenes: how WIP reshapes immune and other functionsActin cytoskeletal defects in immunodeficiencyStoichiometry of Nck-dependent actin polymerization in living cellsUbiquitylation-dependent negative regulation of WASp is essential for actin cytoskeleton dynamicsDisease-associated missense mutations in the EVH1 domain disrupt intrinsic WASp function causing dysregulated actin dynamics and impaired dendritic cell migration.Tyrosine phosphorylation of WIP releases bound WASP and impairs podosome assembly in macrophagesDirect binding of a fragment of the Wiskott-Aldrich syndrome protein to the C-terminal end of the anaphylatoxin C5a receptor.Platelet-associated IgAs and impaired GPVI responses in platelets lacking WIP.A peptide derived from the Wiskott-Aldrich syndrome (WAS) protein-interacting protein (WIP) restores WAS protein level and actin cytoskeleton reorganization in lymphocytes from patients with WAS mutations that disrupt WIP bindingX-linked thrombocytopenia causing mutations in WASP (L46P and A47D) impair T cell chemotaxis.WASP-interacting protein is important for actin filament elongation and prompt pseudopod formation in response to a dynamic chemoattractant gradient.Competition between Blown fuse and WASP for WIP binding regulates the dynamics of WASP-dependent actin polymerization in vivo.WIP is a chaperone for Wiskott-Aldrich syndrome protein (WASP).Requirement for a complex of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein in podosome formation in macrophagesStructure-function analysis of the WIP role in T cell receptor-stimulated NFAT activation: evidence that WIP-WASP dissociation is not required and that the WIP NH2 terminus is inhibitory.WIP regulates signaling via the high affinity receptor for immunoglobulin E in mast cells.Wiskott-Aldrich Syndrome Interacting Protein Deficiency Uncovers the Role of the Co-receptor CD19 as a Generic Hub for PI3 Kinase Signaling in B Cells.WIP regulates the stability and localization of WASP to podosomes in migrating dendritic cells.
P2860
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P2860
Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein
description
1999 nî lūn-bûn
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1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Mutations that cause the Wisko ...... with WASP interacting protein
@ast
Mutations that cause the Wisko ...... with WASP interacting protein
@en
Mutations that cause the Wisko ...... with WASP interacting protein
@en-gb
Mutations that cause the Wisko ...... with WASP interacting protein
@nl
type
label
Mutations that cause the Wisko ...... with WASP interacting protein
@ast
Mutations that cause the Wisko ...... with WASP interacting protein
@en
Mutations that cause the Wisko ...... with WASP interacting protein
@en-gb
Mutations that cause the Wisko ...... with WASP interacting protein
@nl
prefLabel
Mutations that cause the Wisko ...... with WASP interacting protein
@ast
Mutations that cause the Wisko ...... with WASP interacting protein
@en
Mutations that cause the Wisko ...... with WASP interacting protein
@en-gb
Mutations that cause the Wisko ...... with WASP interacting protein
@nl
P2093
P1476
Mutations that cause the Wisko ...... with WASP interacting protein
@en
P2093
P304
P407
P577
1999-04-15T00:00:00Z