Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch - Wikidata - wikimedia - TriplyDB

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

http://www.wikidata.org/entity/Q33947927

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pH sensing and regulation in cancer PAK1 regulates RUFY3-mediated gastric cancer cell migration and invasion Membrane insertion of the FYVE domain is modulated by pH Stabilized phosphatidylinositol-5-phosphate analogues as ligands for the nuclear protein ING2: chemistry, biology, and molecular modeling FYVE-dependent endosomal targeting of an arrestin-related protein in amoeba A high-resolution solution structure of a trypanosomatid FYVE domain Molecular Basis of Phosphatidylinositol 4-Phosphate and ARF1 GTPase Recognition by the FAPP1 Pleckstrin Homology (PH) Domain Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a β-propeller protein family Trio engagement via plasma membrane phospholipids and the myristoyl moiety governs HIV-1 matrix binding to bilayers Molecular mechanism of membrane docking by the Vam7p PX domain.Translation of the phosphoinositide code by PI effectors Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding Considering protonation as a posttranslational modification regulating protein structure and function.Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain Membrane-Induced Folding of the Plant Stress Dehydrin Lti30.Role of class III phosphatidylinositol 3-kinase during programmed nuclear death of Tetrahymena thermophila.Transcriptional profiling reveals the expression of novel genes in response to various stimuli in the human dermatophyte Trichophyton rubrum.Putting the pH into phosphatidic acid signaling The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues.Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi.The adipophilin C terminus is a self-folding membrane-binding domain that is important for milk lipid secretion Cellular and molecular interactions of phosphoinositides and peripheral proteins Receptor-mediated Endocytosis 8 Utilizes an N-terminal Phosphoinositide-binding Motif to Regulate Endosomal Clathrin Dynamics.pH-dependent binding of the Epsin ENTH domain and the AP180 ANTH domain to PI(4,5)P2-containing bilayers.Host targeting of virulence determinants and phosphoinositides in blood stage malaria parasites Phosphatidylinositol 3-phosphate recognition and membrane docking by the FYVE domain.Molecular mechanism of membrane targeting by the GRP1 PH domain Mechanistic similarities in docking of the FYVE and PX domains to phosphatidylinositol 3-phosphate containing membranes.Phosphoinositide, phosphopeptide and pyridone interactions of the Abl SH2 domain Lipid binding domains: more than simple lipid effectors.Molecular analysis of protein-phosphoinositide interactions.A Histidine Cluster in the Cytoplasmic Domain of the Na-H Exchanger NHE1 Confers pH-sensitive Phospholipid Binding and Regulates Transporter Activity.The endosomal Na(+)/H(+) exchanger contributes to multivesicular body formation by regulating the recruitment of ESCRT-0 Vps27p to the endosomal membrane.ZF21 protein regulates cell adhesion and motility.Tools for visualization of phosphoinositides in the cell nucleus.Endoplasmic reticulum PI(3)P lipid binding targets malaria proteins to the host cell.A FYVE zinc finger domain protein specifically links mRNA transport to endosome trafficking.TbFRP, a novel FYVE-domain containing phosphoinositide-binding Ras-like GTPase from trypanosomes.Time-resolved ultrastructural detection of phosphatidylinositol 3-phosphate Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species.

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P2860

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

http://www.wikidata.org/entity/Q33947927

description

2005 nî lūn-bûn

@nan

2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

@ast

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

@en

type

label

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

@ast

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

@en

prefLabel

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

@ast

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

@en

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PNAS.0503900102

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch

@en

P2093

Jinming Geng

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

Matthew L Cheever

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

Rosemary Eyeson

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

Stephanie A Lee

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

Vladislav V Verkhusha

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

P2860

SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor

Regulation of acidification and apoptosis by SHP-1 and Bcl-2

Multivalent endosome targeting by homodimeric EEA1

Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells

Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p

Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction

Structural mechanism of endosome docking by the FYVE domain

All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate.

Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains.

Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.

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13052-13057

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scholarly article

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10.1073/PNAS.0503900102

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P433

37

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P478

102

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P50

Christopher G Burd

Michael Overduin

Tatiana G Kutateladze

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2005-09-02T00:00:00Z

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7620637

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16141328

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1201587

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