Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions. - Wikidata - wikimedia - TriplyDB

Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.

Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.

http://www.wikidata.org/entity/Q37000704

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Chaperone-client interactions: Non-specificity engenders multifunctionality.

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Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.

http://www.wikidata.org/entity/Q37000704

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on June 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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Chaperonin TRiC/CCT Recognizes ...... Subunit-Specific Interactions.

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Chaperonin TRiC/CCT Recognizes ...... Subunit-Specific Interactions.

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Chaperonin TRiC/CCT Recognizes ...... Subunit-Specific Interactions.

@en

Chaperonin TRiC/CCT Recognizes ...... Subunit-Specific Interactions.

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Chaperonin TRiC/CCT Recognizes ...... Subunit-Specific Interactions.

@en

Chaperonin TRiC/CCT Recognizes ...... Subunit-Specific Interactions.

@nl

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J.BPJ.2016.04.045

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Biophysical Journal

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Chaperonin TRiC/CCT Recognizes ...... Subunit-Specific Interactions.

@en

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David J Tweardy

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

Jesús G Galaz-Montoya

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

Moses M Kasembeli

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Soung-Hun Roh

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P2860

Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro

The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity

Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis

DNA recognition by the RUNX1 transcription factor is mediated by an allosteric transition in the RUNT domain and by DNA bending

A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription

Structure of the AML1-ETO NHR3-PKA(RIIα) complex and its contribution to AML1-ETO activity

Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin

The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins

Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.

The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional Partitioning

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scholarly article

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10.1016/J.BPJ.2016.04.045

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11

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2016-06-01T00:00:00Z

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