File Download

There are no files associated with this item.

  • Find it @ UNIST can give you direct access to the published full text of this article. (UNISTARs only)
Related Researcher

기정민

Kee, Jung-Min
Bioorganic and Chembio Lab.
Read More

Views & Downloads

Detailed Information

Cited time in webofscience Cited time in scopus
Metadata Downloads

Distinct phosphorylation and dephosphorylation dynamics of protein arginine kinases revealed by fluorescent activity probes

Author(s)
Jung, HoyoungChoi, YigunLee, DongheeSeo, Jeong KonKee, Jung-Min
Issued Date
2019-07
DOI
10.1039/C9CC03285A
URI
https://scholarworks.unist.ac.kr/handle/201301/26707
Fulltext
https://pubs.rsc.org/en/Content/ArticleLanding/2019/CC/C9CC03285A#!divAbstract
Citation
CHEMICAL COMMUNICATIONS, v.55, no.52, pp.7482 - 7485
Abstract
Protein arginine (Arg) phosphorylation regulates stress responses and virulence in bacteria. With fluorescent activity probes, we show that McsB, a protein Arg kinase, can dephosphorylate phophoarginine (pArg) residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without the phosphatase.
Publisher
Royal Society of Chemistry
ISSN
1359-7345
Keyword
PHOSPHOARGININEASSAYREAL-TIME

qrcode

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