Uncoupling histone modification crosstalk by engineering lysine demethylase LSD1-Reference-Cited by-同舟云学术

Uncoupling histone modification crosstalk by engineering lysine demethylase LSD1

Published:2024-07-04 Issue: Volume: Page:
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Lee Kwangwoon^ORCID,Barone Marco^ORCID,Waterbury Amanda L.^ORCID,Jiang Hanjie^ORCID,Nam Eunju^ORCID,DuBois-Coyne Sarah E.,Whedon Samuel D.^ORCID,Wang Zhipeng A.^ORCID,Caroli Jonatan,Neal Katherine^ORCID,Ibeabuchi Brian,Dhoondia Zuzer^ORCID,Kuroda Mitzi I.^ORCID,Liau Brian B.^ORCID,Beck Samuel^ORCID,Mattevi Andrea^ORCID,Cole Philip A.^ORCID

Publisher

Springer Science and Business Media LLC

Link

https://www.nature.com/articles/s41589-024-01671-9.pdf

Reference116 articles.

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3. Wang, Z. A. & Cole, P. A. The chemical biology of reversible lysine post-translational modifications. Cell Chem. Biol. 27, 953–969 (2020).

4. Valencia-Sánchez, M. I. et al. Structural basis of Dot1L stimulation by histone H2B lysine 120 ubiquitination. Mol. Cell 74, 1010–1019 (2019).

5. Worden, E. J., Hoffmann, N. A., Hicks, C. W. & Wolberger, C. Mechanism of cross-talk between H2B ubiquitination and H3 methylation by Dot1L. Cell 176, 1490–1501 (2019).

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