SNObase, a database for S-nitrosation modification
نویسندگان
چکیده
منابع مشابه
S-nitrosation of proteins
Nitric oxide (NO) is a key factor in inflammation as it regulates microvascular permeability, leukocyte adhesion and wound healing. This mini-review addresses mainly spatial and temporal requirements of NO regulatory mechanisms, with special emphasis on S-nitrosation. Endothelial nitric oxide synthase (eNOS)-derived NO induces S-nitrosation of p120 and β-catenin, particularly in response to pla...
متن کاملNitric oxide and posttranslational modification of the vascular proteome: S-nitrosation of reactive thiols.
Nitric oxide (NO*) is known to exert its effects via guanylyl cyclase and cyclic GMP-dependent pathways and by cyclic GMP-independent pathways, including the posttranslational modification of proteins. Much ongoing research is focused on defining the mechanisms of NO*-mediated protein modification, the identity and function of the modified proteins, and the significance of these changes in heal...
متن کاملS-nitrosation: current concepts and new developments.
The S-nitrosation (also referred to as S-nitrosylation) of cysteine residues is an important post-translational protein modification that regulates protein function and cell signaling. The original research articles and reviews in this Forum cover important concepts in protein S-nitrosation and identify key developments and opportunities for progress in this area. Defining the mechanisms by whi...
متن کاملESNOQ, Proteomic Quantification of Endogenous S-Nitrosation
S-nitrosation is a post-translational protein modification and is one of the most important mechanisms of NO signaling. Endogenous S-nitrosothiol (SNO) quantification is a challenge for detailed functional studies. Here we developed an ESNOQ (Endogenous SNO Quantification) method which combines the stable isotope labeling by amino acids in cell culture (SILAC) technique with the detergent-free ...
متن کاملFurther study on S-nitrosation by nitrite.
At neutral pH, S-nitrosoglutathione was formed by the reaction of reduced glutathione and sodium nitrite. The degradation of S-nitrosoglutathione, presumably by transnitrosation/denitrosation, was catalyzed by L-cysteine, or CoA-SH. Additionally, from the crude extract of rat brain, one protein with a large molecular mass was nitrosolated with nitrite, and was split into duplet peptides noted i...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Protein & Cell
سال: 2012
ISSN: 1674-800X,1674-8018
DOI: 10.1007/s13238-012-2094-6