Structural basis for binding diversity of acetyltransferase p300 to the nucleosome-Reference-Cited by-同舟云学术

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Structural basis for binding diversity of acetyltransferase p300 to the nucleosome

Published:2022-07 Issue:7 Volume:25 Page:104563
ISSN:2589-0042
Container-title:iScience
language:en
Short-container-title:iScience

Author:

Hatazawa Suguru,Liu Jiuyang,Takizawa Yoshimasa,Zandian Mohamad,Negishi Lumi,Kutateladze Tatiana G.^ORCID,Kurumizaka Hitoshi^ORCID

Publisher

Elsevier BV

Subject

Multidisciplinary

Reference48 articles.

1. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53;An;Cell,2004

2. Structural basis of a nucleosome containing histone H2A.B/H2A.Bbd that transiently associates with reorganized chromatin;Arimura;Sci. Rep.,2013

3. RNA binding to CBP stimulates histone acetylation and transcription;Bose;Cell,2017

4. ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps;Croll;Acta Crystallogr. D Struct. Biol.,2018

5. Protein lysine acetylation by p300/CBP;Dancy;Chem. Rev.,2015

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1. Molecular and structural basis of the chromatin remodeling activity by Arabidopsis DDM1;Nature Communications;2024-07-11

2. Stepwise Discriminant Analysis based Optimal Frequency Band Selection and Ensemble Learning for Same Limb MI Recognition;2024-04-24

3. p300 is an obligate integrator of combinatorial transcription factor inputs;Molecular Cell;2024-01

4. Histone acetylation and deacetylation – Mechanistic insights from structural biology;Gene;2024-01

5. Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II;Nucleic Acids Research;2023-09-18

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