계명대학교 의학도서관 Repository

Versatility of ARD1/NAA10-mediated protein lysine acetylation

Metadata Downloads
Author(s)
Tam Thuy Lu VoChul-Ho JeongSooyeun LeeKyu-Won KimEunyoung HaJi Hae Seo
Keimyung Author(s)
Jung, Chul HoHa, Eun YoungSeo, Ji Hye
Department
Dept. of Psychiatry (정신건강의학)
Dept. of Biochemistry (생화학)
Journal Title
Experimental & Molecular Medicine
Issued Date
2018
Volume
50
Issue
7
Abstract
Post-translational modifications (PTMs) are chemical alterations that occur in proteins that play critical roles in various cellular functions. Lysine acetylation is an important PTM in eukaryotes, and it is catalyzed by lysine acetyltransferases (KATs). KATs transfer acetyl-coenzyme A to the internal lysine residue of substrate proteins. Arrest defective 1 (ARD1) is a member of the KAT family. Since the identification of its KAT activity 15 years ago, many studies have revealed that diverse cellular proteins are acetylated by ARD1. ARD1-mediated lysine acetylation is a key switch that regulates the enzymatic activities and biological functions of proteins and influences cell biology from development to pathology. In this review, we summarize protein lysine acetylation mediated by ARD1 and describe the biological meanings of this modification.
Keimyung Author(s)(Kor)
정철호
하은영
서지혜
Publisher
School of Medicine (의과대학)
Citation
Tam Thuy Lu Vo et al. (2018). Versatility of ARD1/NAA10-mediated protein lysine acetylation. Experimental & Molecular Medicine, 50(7), 86–86. doi: 10.1038/s12276-018-0100-7
Type
Article
ISSN
2092-6413
Source
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6063952/
DOI
10.1038/s12276-018-0100-7
URI
https://kumel.medlib.dsmc.or.kr/handle/2015.oak/41741
Appears in Collections:
1. School of Medicine (의과대학) > Dept. of Biochemistry (생화학)
1. School of Medicine (의과대학) > Dept. of Psychiatry (정신건강의학)
공개 및 라이선스
  • 공개 구분공개
파일 목록

Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.