A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. - Test2 - elhamkhani - TriplyDB

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

http://www.wikidata.org/entity/Q37235659

about

Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X Structure of cellular ESCRT-III spirals and their relationship to HIV budding ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding ESCRT requirements for EIAV budding The ESCRT complexes Molecular mechanism of multivesicular body biogenesis by ESCRT complexes Membrane budding and scission by the ESCRT machinery: it's all in the neck Assembly and disassembly of the ESCRT-III membrane scission complex Virus budding and the ESCRT pathway The ESCRT machinery: from the plasma membrane to endosomes and back again Wrapping up the bad news: HIV assembly and release Atypical regulation of G protein-coupled receptor intracellular trafficking by ubiquitination ALIX is recruited temporarily into HIV-1 budding sites at the end of gag assembly ALG-2 interacting protein-X (Alix) is essential for clathrin-independent endocytosis and signaling Identification and Structural Characterization of the ALIX-Binding Late Domains of Simian Immunodeficiency Virus SIVmac239 and SIVagmTan-1 Structural Basis for ESCRT-III CHMP3 Recruitment of AMSH The Phe105 Loop of Alix Bro1 Domain Plays a Key Role in HIV-1 Release Structure of the Bro1 Domain Protein BROX and Functional Analyses of the ALIX Bro1 Domain in HIV-1 Budding CC2D1A Is a Regulator of ESCRT-III CHMP4B The Yeast Alix Homolog Bro1 Functions as a Ubiquitin Receptor for Protein Sorting into Multivesicular Endosomes Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments Crenarchaeal CdvA forms double-helical filaments containing DNA and interacts with ESCRT-III-like CdvB Arabidopsis ALIX is required for the endosomal localization of the deubiquitinating enzyme AMSH3.Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggests that spiraling filaments are involved in membrane scission.Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly.Computational model of membrane fission catalyzed by ESCRT-III.Rescue of HIV-1 release by targeting widely divergent NEDD4-type ubiquitin ligases and isolated catalytic HECT domains to Gag.Membrane fission reactions of the mammalian ESCRT pathway.Old world arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport Viral infection controlled by a calcium-dependent lipid-binding module in ALIX.Interaction of HIV-1 Nef protein with the host protein Alix promotes lysosomal targeting of CD4 receptor.Negative staining and cryo-negative staining of macromolecules and viruses for TEM.ALIX/AIP1 is required for NP incorporation into Mopeia virus Z-induced virus-like particles A combined global and local approach to elucidate spatial organization of the Mycobacterial ParB-parS partition assembly.ALIX and ESCRT-III coordinately control cytokinetic abscission during germline stem cell division in vivo.The role of cellular factors in promoting HIV budding.Proline-rich regions and motifs in trafficking: from ESCRT interaction to viral exploitation.Super-resolution imaging of ESCRT-proteins at HIV-1 assembly sites.Budding of retroviruses utilizing divergent L domains requires nucleocapsid.Alix protein is substrate of Ozz-E3 ligase and modulates actin remodeling in skeletal muscle.

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A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

http://www.wikidata.org/entity/Q37235659

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on June 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

@en

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

@nl

type

label

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

@en

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

@nl

prefLabel

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

@en

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

@nl

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J.STR.2009.04.007

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P1476

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments

@en

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Andreas Hinz

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

Bettina Hartlieb

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

Eric Forest

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

Heinrich G Göttlinger

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

Luca Signor

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

Manfred Roessle

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

Marc Jamin

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

Remy Sadoul

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

Ricardo Pires

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

Sergei Popov

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

P2860

Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding

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

The protein network of HIV budding

Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins

Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding

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

The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting

The penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1

Structural basis for autoinhibition of ESCRT-III CHMP3

Helical structures of ESCRT-III are disassembled by VPS4

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843-856

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scholarly article

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10.1016/J.STR.2009.04.007

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6

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17

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

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Christine Moriscot

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2009-06-01T00:00:00Z

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26289701

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

P698

19523902

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identical protein binding

Charged multivesicular body protein 4B

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2699623

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