WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation.
about
The WASP and WAVE family proteinsWIP remodeling actin behind the scenes: how WIP reshapes immune and other functionsTuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeletonWIP provides an essential link between Nck and N-WASP during Arp2/3-dependent actin polymerization.Binding of the WASP/N-WASP-interacting protein WIP to actin regulates focal adhesion assembly and adhesionPodosomes in adhesion, migration, mechanosensing and matrix remodeling.The Wiskott-Aldrich syndrome protein: forging the link between actin and cell activation.WASP-interacting protein is important for actin filament elongation and prompt pseudopod formation in response to a dynamic chemoattractant gradient.WIP is a chaperone for Wiskott-Aldrich syndrome protein (WASP).Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex.Requirement for a complex of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein in podosome formation in macrophagesWIP and WICH/WIRE co-ordinately control invadopodium formation and maturation in human breast cancer cell invasionThe verprolin family of proteins: regulators of cell morphogenesis and endocytosis.Diversity of polyproline recognition by EVH1 domains.Dynamic shaping of cellular membranes by phospholipids and membrane-deforming proteins.Spatially distinct binding of Cdc42 to PAK1 and N-WASP in breast carcinoma cellsThe NF2 tumor suppressor Merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function.Enterohaemorrhagic and enteropathogenic Escherichia coli use different mechanisms for actin pedestal formation that converge on N-WASP.The enteropathogenic E. coli effector EspH promotes actin pedestal formation and elongation via WASP-interacting protein (WIP).EspF Interacts with nucleation-promoting factors to recruit junctional proteins into pedestals for pedestal maturation and disruption of paracellular permeability.Inhibiting Wipf2 downregulation by transgenic expression of its 3' mRNA-untranslated region improves cytotoxicity and vaccination response.Activation of WASP/N-WASP by WIP family and SH3 domain proteinsN-WASP regulates the epithelial junctional actin cytoskeleton through a non-canonical post-nucleation pathway.
P2860
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P2860
WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation.
description
2002 nî lūn-bûn
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2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
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2002年の論文
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2002年論文
@yue
2002年論文
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2002年論文
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2002年論文
@zh-mo
2002年論文
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2002年论文
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name
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@ast
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@en
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@nl
type
label
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@ast
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@en
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@nl
prefLabel
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@ast
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@en
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@nl
P2093
P356
P1476
WICH, a novel verprolin homolo ...... in actin-microspike formation.
@en
P2093
Hiroaki Miki
Hiroyuki Nakagawa
Masayoshi Kato
Shigeaki Miyamoto
Souichi Kurita
Tadaomi Takenawa
Takeshi Endo
P356
10.1006/BBRC.2002.6406
P407
P577
2002-02-01T00:00:00Z