PuSH - Publikationsserver des Helmholtz Zentrums München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
Sell, S. ; Lindermayr, C. ; Durner, J.

Identification of S-nitrosylated proteins in plants.

Methods Enzymol. 440, 283-293 (2008)
DOI
Posttranslational protein modifications affect the function or the activity of proteins and exhibit important mechanisms in regulating cellular events. A broad spectrum of modifications is known, including redox-dependent alterations. During the last decade, covalent binding of nitric oxide (NO) to protein cysteines, termed S-nitrosylation, seems especially an evident process for redox-related signaling. To reveal potential target proteins for S-nitrosylation, the biotin switch method gains more and more in importance. This technique is a tool used for analyzing the nitrosylome as well as the examination of single candidates. It is based on substitution of the NO group by a biotin linker that simplifies the detection and the purification of recently S-nitrosylated proteins in a three-step procedure.
Impact Factor
Scopus SNIP
Scopus
Cited By
Altmetric
2.122
0.000
15
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Sprache englisch
Veröffentlichungsjahr 2008
HGF-Berichtsjahr 2008
ISSN (print) / ISBN 0076-6879
e-ISSN 0076-6879
Zeitschrift Methods in Enzymology
Quellenangaben Band: 440, Heft: , Seiten: 283-293 Artikelnummer: , Supplement: ,
Verlag Elsevier
Begutachtungsstatus Peer reviewed
Institut(e) Research Unit Environmental Simulation (EUS)
POF Topic(s) 30202 - Environmental Health
Forschungsfeld(er) Environmental Sciences
PSP-Element(e) G-504900-002
DOI 10.1016/S0076-6879(07)00818-X
Scopus ID 44849085497
Erfassungsdatum 2008-07-10
[➜Korrektur melden]