Contribution of Electrostatic CH<sub>3</sub>–π Interactions to Recognition of Histone Asymmetric Dimethylarginine by the SPIN1 Triple Tudor Domain-Reference-Cited by-同舟云学术

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Contribution of Electrostatic CH₃–π Interactions to Recognition of Histone Asymmetric Dimethylarginine by the SPIN1 Triple Tudor Domain

Published:2024-07-18 Issue:30 Volume:146 Page:20678-20684
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Travis Christopher R.¹^ORCID,Dumais Ryan G.¹,Treacy Joseph W.²^ORCID,Kean Kelsey M.³^ORCID,Houk K. N.²^ORCID,Waters Marcey L.¹^ORCID

Affiliation:

1. Department of Chemistry, CB 3290, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States

2. Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, California 90095-1569, United States

3. Department of Chemistry, High Point University, High Point, North Carolina 27268, United States

Funder

National Science Foundation Graduate Research Fellowship Program

National Institute of Allergy and Infectious Diseases

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.4c03463

Reference60 articles.

1. Histone arginine methylation

2. Protein Arginine Methylation in Mammals: Who, What, and Why

3. The language of covalent histone modifications

4. Writers, Readers, and Erasers of Epigenetic Marks

5. Role of Protein Methylation in Regulation of Transcription

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