A Versatile Approach for Site‐Specific Lysine Acylation in Proteins-Reference-Cited by-同舟云学术

A Versatile Approach for Site‐Specific Lysine Acylation in Proteins

Published:2017-02 Issue:6 Volume:56 Page:1643-1647
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Wang Zhipeng A.¹,Kurra Yadagiri¹,Wang Xin²,Zeng Yu¹,Lee Yan‐Jiun¹,Sharma Vangmayee¹,Lin Hening³,Dai Susie Y.²,Liu Wenshe R.¹^ORCID

Affiliation:

1. Department of ChemistryTexas A&M University College Station TX 77843 USA

2. Department of Plant Pathology and MicrobiologyInstitute for Plant GenomicsOffice of the Texas State ChemistDepartment of Veterinary Pathobiology College Station TX 77843 USA

3. Department of Chemistry and Chemical BiologyCornell University Ithaca NY 14853 USA

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201611415

Reference40 articles.

1. The growing landscape of lysine acetylation links metabolism and cell signalling

2. N ε -Formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function

3. Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark

4. Lysine Propionylation and Butyrylation Are Novel Post-translational Modifications in Histones

5. Identification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification

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