S-nitrosylation: An emerging redox-based post-translational modification in plants

Yiqin Wang; Byung Wook Yun; Eun Jung Kwon; Jeum Kyu Hong; Joonseon Yoon; Gary J. Loake

doi:10.1093/jxb/erj211

S-nitrosylation: An emerging redox-based post-translational modification in plants

Yiqin Wang
, Byung Wook Yun
, Eun Jung Kwon
, Jeum Kyu Hong
, Joonseon Yoon
, Gary J. Loake

University of Edinburgh

Research output: Contribution to journal › Article › peer-review

111 Scopus citations

Abstract

S-nitrosylation, the covalent attachment of a nitric oxide moiety to a cysteine thiol, is now established as a key post-translational modification in animals. This process has been shown to regulate the function of a wide variety of regulatory, structural, and metabolic proteins. The emerging evidence now suggests that S-nitrosylation may also have a central function in plant biology.

Original language	English
Pages (from-to)	1777-1784
Number of pages	8
Journal	Journal of Experimental Botany
Volume	57
Issue number	8
DOIs	https://doi.org/10.1093/jxb/erj211
State	Published - May 2006

Keywords

Nitric oxide
Plant disease resistance
Redox signalling
S-nitrosothiols
S-nitrosylation

Access to Document

10.1093/jxb/erj211

Cite this

@article{ba0de0ecb22c4a6f93823e99ab09f7cb,

title = "S-nitrosylation: An emerging redox-based post-translational modification in plants",

abstract = "S-nitrosylation, the covalent attachment of a nitric oxide moiety to a cysteine thiol, is now established as a key post-translational modification in animals. This process has been shown to regulate the function of a wide variety of regulatory, structural, and metabolic proteins. The emerging evidence now suggests that S-nitrosylation may also have a central function in plant biology.",

keywords = "Nitric oxide, Plant disease resistance, Redox signalling, S-nitrosothiols, S-nitrosylation",

author = "Yiqin Wang and Yun, \{Byung Wook\} and Kwon, \{Eun Jung\} and Hong, \{Jeum Kyu\} and Joonseon Yoon and Loake, \{Gary J.\}",

year = "2006",

month = may,

doi = "10.1093/jxb/erj211",

language = "English",

volume = "57",

pages = "1777--1784",

journal = "Journal of Experimental Botany",

issn = "0022-0957",

publisher = "Oxford University Press",

number = "8",

}

TY - JOUR

T1 - S-nitrosylation

T2 - An emerging redox-based post-translational modification in plants

AU - Wang, Yiqin

AU - Yun, Byung Wook

AU - Kwon, Eun Jung

AU - Hong, Jeum Kyu

AU - Yoon, Joonseon

AU - Loake, Gary J.

PY - 2006/5

Y1 - 2006/5

N2 - S-nitrosylation, the covalent attachment of a nitric oxide moiety to a cysteine thiol, is now established as a key post-translational modification in animals. This process has been shown to regulate the function of a wide variety of regulatory, structural, and metabolic proteins. The emerging evidence now suggests that S-nitrosylation may also have a central function in plant biology.

AB - S-nitrosylation, the covalent attachment of a nitric oxide moiety to a cysteine thiol, is now established as a key post-translational modification in animals. This process has been shown to regulate the function of a wide variety of regulatory, structural, and metabolic proteins. The emerging evidence now suggests that S-nitrosylation may also have a central function in plant biology.

KW - Nitric oxide

KW - Plant disease resistance

KW - Redox signalling

KW - S-nitrosothiols

KW - S-nitrosylation

UR - https://www.scopus.com/pages/publications/33745601651

U2 - 10.1093/jxb/erj211

DO - 10.1093/jxb/erj211

M3 - Article

C2 - 16714306

AN - SCOPUS:33745601651

SN - 0022-0957

VL - 57

SP - 1777

EP - 1784

JO - Journal of Experimental Botany

JF - Journal of Experimental Botany

IS - 8

ER -

S-nitrosylation: An emerging redox-based post-translational modification in plants

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this