Regulation of Bin1 SH3 domain binding by phosphoinositides - Wikidata - wikimedia - TriplyDB

Regulation of Bin1 SH3 domain binding by phosphoinositides

Regulation of Bin1 SH3 domain binding by phosphoinositides

http://www.wikidata.org/entity/Q24561373

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Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region Identification of a link between the SAMP repeats of adenomatous polyposis coli tumor suppressor and the Src homology 3 domain of DDEF The myotubularin-amphiphysin 2 complex in membrane tubulation and centronuclear myopathies Targeting AMAP1 and cortactin binding bearing an atypical src homology 3/proline interface for prevention of breast cancer invasion and metastasis Molecular and structural characterization of the SH3 domain of AHI-1 in regulation of cellular resistance of BCR-ABL(+) chronic myeloid leukemia cells to tyrosine kinase inhibitors The roles of lipid and glucose metabolism in modulation of β-amyloid, tau, and neurodegeneration in the pathogenesis of Alzheimer disease Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy Grb2 carboxyl-terminal SH3 domain can bivalently associate with two ligands, in an SH3 dependent manner.BIN1 membrane curvature sensing and generation show autoinhibition regulated by downstream ligands and PI(4,5)P2.Dual role of BAR domain-containing proteins in regulating vesicle release catalyzed by the GTPase, dynamin-2.The BAR Domain Superfamily Proteins from Subcellular Structures to Human Diseases Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction Bin1 SRC homology 3 domain acts as a scaffold for myofiber sarcomere assembly Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain.Bridging integrator 1 (Bin1) deficiency in zebrafish results in centronuclear myopathy.Comparison of Petunia inflata S-Locus F-box protein (Pi SLF) with Pi SLF like proteins reveals its unique function in S-RNase based self-incompatibility.Mild functional differences of dynamin 2 mutations associated to centronuclear myopathy and Charcot-Marie Tooth peripheral neuropathy.Altered splicing of the BIN1 muscle-specific exon in humans and dogs with highly progressive centronuclear myopathy T-tubule biogenesis and triad formation in skeletal muscle and implication in human diseases.Structural insights into the centronuclear myopathy-associated functions of BIN1 and dynamin 2.Dynamin 2 the rescue for centronuclear myopathy.Barfly: sculpting membranes at the Drosophila neuromuscular junction.Amphiphysin 2 (BIN1) in physiology and diseases.Phosphorylation of amphiphysin I by minibrain kinase/dual-specificity tyrosine phosphorylation-regulated kinase, a kinase implicated in Down syndrome.Amphiphysin (BIN1) negatively regulates dynamin 2 for normal muscle maturation.Defects in amphiphysin 2 (BIN1) and triads in several forms of centronuclear myopathies Centronuclear myopathies under attack: A plethora of therapeutic targets

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P2860

Regulation of Bin1 SH3 domain binding by phosphoinositides

http://www.wikidata.org/entity/Q24561373

description

2004 nî lūn-bûn

@nan

2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

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2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Regulation of Bin1 SH3 domain binding by phosphoinositides

@ast

Regulation of Bin1 SH3 domain binding by phosphoinositides

@en

Regulation of Bin1 SH3 domain binding by phosphoinositides

@nl

type

label

Regulation of Bin1 SH3 domain binding by phosphoinositides

@ast

Regulation of Bin1 SH3 domain binding by phosphoinositides

@en

Regulation of Bin1 SH3 domain binding by phosphoinositides

@nl

prefLabel

Regulation of Bin1 SH3 domain binding by phosphoinositides

@ast

Regulation of Bin1 SH3 domain binding by phosphoinositides

@en

Regulation of Bin1 SH3 domain binding by phosphoinositides

@nl

P1433

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SJ.EMBOJ.7600442

P1433

The EMBO Journal

P1476

Regulation of Bin1 SH3 domain binding by phosphoinositides

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P2093

Ari Hashimoto

http://www.w3.org/2001/XMLSchema#string

Chie Kojima

http://www.w3.org/2001/XMLSchema#string

Hideki Sumimoto

http://www.w3.org/2001/XMLSchema#string

Hisataka Sabe

http://www.w3.org/2001/XMLSchema#string

Izumi Yabuta

http://www.w3.org/2001/XMLSchema#string

Mayumi Hirose

http://www.w3.org/2001/XMLSchema#string

Shigeru Hashimoto

http://www.w3.org/2001/XMLSchema#string

Yasunori Kanaho

http://www.w3.org/2001/XMLSchema#string

P2860

SAP couples Fyn to SLAM immune receptors

Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family, is concentrated in the cortical cytomatrix of axon initial segments and nodes of ranvier in brain and around T tubules in skeletal muscle

PAK kinases are directly coupled to the PIX family of nucleotide exchange factors

A role for the putative tumor suppressor Bin1 in muscle cell differentiation

A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration

Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation

Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila

The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain

Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation

Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p.

P304

4413-22

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scholarly article

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4754429

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P356

10.1038/SJ.EMBOJ.7600442

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P433

22

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P478

23

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P50

Takahisa Ikegami

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2004-11-10T00:00:00Z

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P5875

8232309

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P698

15483625

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526460

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