Solution Structure of the N-Terminal Domain of Mediator Subunit MED26 and Molecular Characterization of Its Interaction with EAF1 and TAF7-Reference-Cited by-同舟云学术

Solution Structure of the N-Terminal Domain of Mediator Subunit MED26 and Molecular Characterization of Its Interaction with EAF1 and TAF7

Published:2017-10 Issue:20 Volume:429 Page:3043-3055
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Lens Zoé,Cantrelle François-Xavier,Peruzzini Riccardo,Hanoulle Xavier,Dewitte Frédérique,Ferreira Elisabeth,Baert Jean-Luc,Monté Didier,Aumercier Marc,Villeret Vincent,Verger Alexis,Landrieu Isabelle

Funder

TGE RMN THC

FRABio

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference39 articles.

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3. The metazoan Mediator co-activator complex as an integrative hub for transcriptional regulation;Malik;Nat. Rev. Genet.,2010

4. The Mediator complex and transcription regulation;Poss;Crit. Rev. Biochem. Mol. Biol.,2013

5. A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology;Sato;Mol. Cell,2004

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1. MED26-enriched condensates drive erythropoiesis through modulating transcription pausing;2024-08-26

2. MED26‐containing Mediator may orchestrate multiple transcription processes through organization of nuclear bodies;BioEssays;2023-02-28

3. The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder;Biochemical Society Transactions;2023-01-18

4. The Mediator complex as a master regulator of transcription by RNA polymerase II;Nature Reviews Molecular Cell Biology;2022-06-20

5. Transcription Pause and Escape in Neurodevelopmental Disorders;Frontiers in Neuroscience;2022-05-09