Protein Arginine Methyltransferase 1‐Dependent Labeling and Isolation of Histone H4 through N ‐Mustard Analogues of S ‐Adenosyl‐ l ‐methionine-Reference-Cited by-同舟云学术

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Protein Arginine Methyltransferase 1‐Dependent Labeling and Isolation of Histone H4 through N ‐Mustard Analogues of S ‐Adenosyl‐ l ‐methionine

Published:2019-01-09 Issue:3 Volume:20 Page:379-384
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Hymbaugh Sarah J.¹,Pecor Lindsay M.¹,Tracy Christopher M.¹,Comstock Lindsay R.¹^ORCID

Affiliation:

1. Department of ChemistryWake Forest University 455 Vine Street Wake Downtown NC 27101-4135 USA

Funder

National Science Foundation

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.201800477

Reference29 articles.

1. AdoMet-dependent methylation, DNA methyltransferases and base flipping

2. Arginine Methylation

3. Epigenetic regulation of gene expression: how the genome integrates intrinsic and environmental signals

4. Role of Protein Methylation in Regulation of Transcription

5. Protein arginine methyltransferases (PRMTs): Role in chromatin organization

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Promiscuous Enzymes for Residue‐Specific Peptide and Protein Late‐Stage Functionalization;ChemBioChem;2023-07-19

2. Chemical probes and methods for the study of protein arginine methylation;RSC Chemical Biology;2023

3. Analogs of S-Adenosyl-L-Methionine in Studies of Methyltransferases;Molecular Biology;2022-04

4. Assaying epigenome functions of PRMTs and their substrates;Methods;2020-03

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