eps15, a novel tyrosine kinase substrate, exhibits transforming activity. - Wikidata - wikimedia - TriplyDB

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

http://www.wikidata.org/entity/Q36701817

about

Genomic and epigenomic responses to chronic stress involve miRNA-mediated programming The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15.Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin Nucleocytoplasmic shuttling of endocytic proteins The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia Shared as well as distinct roles of EHD proteins revealed by biochemical and functional comparisons in mammalian cells and C. elegans Binding to DPF-motif by the POB1 EH domain is responsible for POB1-Eps15 interaction Eps15 homology domain-NPF motif interactions regulate clathrin coat assembly during synaptic vesicle recycling HIP1 and HIP1r stabilize receptor tyrosine kinases and bind 3-phosphoinositides via epsin N-terminal homology domains Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module Leucine-zipper dimerization motif encoded by the AF17 gene fused to ALL-1 (MLL) in acute leukemia Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15 BRCA1 is secreted and exhibits properties of a granin A protein-binding domain, EH, identified in the receptor tyrosine kinase substrate Eps15 and conserved in evolution Induction of S-phase entry by E2F transcription factors depends on their nuclear localization Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains Constitutive phosphorylation of eps8 in tumor cell lines: relevance to malignant transformation The eps15 homology (EH) domain-based interaction between eps15 and hrb connects the molecular machinery of endocytosis to that of nucleocytosolic transport Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery Numb is an endocytic protein AP-2/Eps15 interaction is required for receptor-mediated endocytosis Association and colocalization of Eps15 with adaptor protein-2 and clathrin Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1 Mechanism for the Selective Interaction of C-terminal Eps15 Homology Domain Proteins with Specific Asn-Pro-Phe-containing Partners Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1)A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15.EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae.The conserved Pkh-Ypk kinase cascade is required for endocytosis in yeast.The EH-domain-containing protein Pan1 is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae.EHD3 regulates early-endosome-to-Golgi transport and preserves Golgi morphology Hrs-2 regulates receptor-mediated endocytosis via interactions with Eps15 Calmodulin binds RalA and RalB and is required for the thrombin-induced activation of Ral in human platelets The ENTH domain An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1 The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R Eps15R is a tyrosine kinase substrate with characteristics of a docking protein possibly involved in coated pits-mediated internalization Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2

P2860

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P2860

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

http://www.wikidata.org/entity/Q36701817

description

1993 nî lūn-bûn

@nan

1993年の論文

@ja

1993年論文

@yue

1993年論文

@zh-hant

1993年論文

@zh-hk

1993年論文

@zh-mo

1993年論文

@zh-tw

1993年论文

@wuu

1993年论文

@zh

1993年论文

@zh-cn

name

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

@ast

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

@en

type

label

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

@ast

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

@en

prefLabel

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

@ast

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

@en

P1433

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P2860

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P1433

Molecular and Cellular Biology

P1476

eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

@en

P2093

Di Fiore PP

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

Fazioli F

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

Matoskova B

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

Minichiello L

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

Wong WT

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

P2860

Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62

Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases

Molecular cloning of cDNAs encoding the GAP-associated protein p190: implications for a signaling pathway from ras to the nucleus

Binding of GAP to activated PDGF receptors

Tyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction

A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction

The scanning model for translation: an update

Basic local alignment search tool

A simple method for displaying the hydropathic character of a protein

Signal transduction by receptors with tyrosine kinase activity

P304

5814-5828

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scholarly article

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10.1128/MCB.13.9.5814

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9

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13

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1993-09-01T00:00:00Z

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7689153

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360326

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