Structural Basis of Ist1 Function and Ist1-Did2 Interaction in the Multivesicular Body Pathway and Cytokinesis - Wikidata - wikimedia - TriplyDB

Structural Basis of Ist1 Function and Ist1-Did2 Interaction in the Multivesicular Body Pathway and Cytokinesis

Structural Basis of Ist1 Function and Ist1-Did2 Interaction in the Multivesicular Body Pathway and Cytokinesis

http://www.wikidata.org/entity/Q27655663

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SPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1 and participates in cytokinesis.Structure of cellular ESCRT-III spirals and their relationship to HIV budding Autolytic activity of human calpain 7 is enhanced by ESCRT-III-related protein IST1 through MIT-MIM interaction ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport The ESCRT complexes Regulation of Vps4 during MVB sorting and cytokinesis Membrane budding and scission by the ESCRT machinery: it's all in the neck Assembly and disassembly of the ESCRT-III membrane scission complex Wrapping up the bad news: HIV assembly and release CC2D1A Is a Regulator of ESCRT-III CHMP4B Two Distinct Binding Modes Define the Interaction of Brox with the C-Terminal Tails of CHMP5 and CHMP4B Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggests that spiraling filaments are involved in membrane scission.Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles Binding to any ESCRT can mediate ubiquitin-independent cargo sorting Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation Membrane fission reactions of the mammalian ESCRT pathway.Assembly of the AAA ATPase Vps4 on ESCRT-III.Coordination of substrate binding and ATP hydrolysis in Vps4-mediated ESCRT-III disassembly.Activation of human VPS4A by ESCRT-III proteins reveals ability of substrates to relieve enzyme autoinhibition.Vps4 stimulatory element of the cofactor Vta1 contacts the ATPase Vps4 α7 and α9 to stimulate ATP hydrolysis.Distinct mechanisms of recognizing endosomal sorting complex required for transport III (ESCRT-III) protein IST1 by different microtubule interacting and trafficking (MIT) domains Interactome of the plant-specific ESCRT-III component AtVPS2.2 in Arabidopsis thaliana Vps4 disassembles an ESCRT-III filament by global unfolding and processive translocation.Binding of Substrates to the Central Pore of the Vps4 ATPase Is Autoinhibited by the Microtubule Interacting and Trafficking (MIT) Domain and Activated by MIT Interacting Motifs (MIMs).The ESCRT regulator Did2 maintains the balance between long-distance endosomal transport and endocytic trafficking Structure and membrane remodeling activity of ESCRT-III helical polymers.Conformational Changes in the Endosomal Sorting Complex Required for the Transport III Subunit Ist1 Lead to Distinct Modes of ATPase Vps4 Regulation Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments.Relief of autoinhibition enhances Vta1 activation of Vps4 via the Vps4 stimulatory element The linker region plays a regulatory role in assembly and activity of the Vps4 AAA ATPase.Electrostatic Interactions between Elongated Monomers Drive Filamentation of Drosophila Shrub, a Metazoan ESCRT-III Protein.NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway.Reverse-topology membrane scission by the ESCRT proteins.Structure and function of the membrane deformation AAA ATPase Vps4.HIV-1 assembly, budding, and maturation.Activation of the retroviral budding factor ALIX.The Drosophila Chmp1 protein determines wing cell fate through regulation of epidermal growth factor receptor signaling.Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase.Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing.

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Structural Basis of Ist1 Function and Ist1-Did2 Interaction in the Multivesicular Body Pathway and Cytokinesis

http://www.wikidata.org/entity/Q27655663

description

2009 nî lūn-bûn

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2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2009 թվականի օգոստոսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Structural Basis of Ist1 Funct ...... r Body Pathway and Cytokinesis

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MBC.E09-05-0403

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Molecular Biology of the Cell

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Structural Basis of Ist1 Funct ...... r Body Pathway and Cytokinesis

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P2093

Alan R Saltiel

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

Brian A Davies

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

David J Katzmann

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

Junyu Xiao

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

Xiao-Wei Chen

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Zhaohui Xu

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

P2860

Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis.

ESCRT-III recognition by VPS4 ATPases

Plasma membrane deformation by circular arrays of ESCRT-III protein filaments

Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding

Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B

Biochemical analyses of human IST1 and its function in cytokinesis.

Essential role of hIST1 in cytokinesis.

Structural basis for autoinhibition of ESCRT-III CHMP3

Helical structures of ESCRT-III are disassembled by VPS4

Structural basis for budding by the ESCRT-III factor CHMP3

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3514-24

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scholarly article

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4474727

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10.1091/MBC.E09-05-0403

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15

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20

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2009-08-01T00:00:00Z

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19477918

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2719569

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