Results 141 to 150 of about 15,774 (176)

S-nitrosylation in health and disease

Trends in Molecular Medicine, 2003
S-nitrosylation is a ubiquitous redox-related modification of cysteine thiol by nitric oxide (NO), which transduces NO bioactivity. Accumulating evidence suggests that the products of S-nitrosylation, S-nitrosothiols (SNOs), play key roles in human health and disease.
Matthew W, Foster, Timothy J, McMahon, Jonathan S, Stamler   +2 more
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Expression, S-Nitrosylation, and Measurement of S-Nitrosylation Ratio of Recombinant Galectin-2

2020
S-nitrosylation, which involves the coupling of an NO group to the reactive thiol of Cys residue(s) in a polypeptide, is an important posttranslational modification detected in a variety of proteins. Here, we present the S-nitrosylation of recombinant galectin-2 (Gal-2) using S-nitrosocysteine and the measurement of the molecular ratio of S ...
Mayumi, Tamura, Yoichiro, Arata
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Protein S-nitrosylation and cancer

Cancer Letters, 2012
Protein S-nitrosylation is a covalent post-translational modification through coupling of a nitric oxide (NO) moiety with the reactive thiol group of a protein cysteine residue to form an S-nitrosothiol (SNO). S-nitrosylation is a key mechanism in the transmission of NO-based cellular signals in the vital cellular processes, including transcription ...
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Protein S-Nitrosylation Measurement

2013
G protein-coupled receptors (GPCRs) are the most abundant and diverse type of cell surface receptors. GPCR signal duration and amplitude are both controlled by posttranslational modifications, principally phosphorylation. Emerging evidence demonstrates that the GCPRs and their effectors are also subject to S-nitrosylation modification.
Yu, Qin, Anindya, Dey, Yehia, Daaka
openaire   +2 more sources

S-nitrosylation in the regulation of gene transcription [PDF]

Biochimica Et Biophysica Acta - General Subjects, 2012
Post-translational modification of proteins by S-nitrosylation serves as a major mode of signaling in mammalian cells and a growing body of evidence has shown that transcription factors and their activating pathways are primary targets. S-nitrosylation directly modifies a number of transcription factors, including NF-κB, HIF-1, and AP-1. In addition, S-
Yonggang, Sha, Harvey E, Marshall
exaly   +3 more sources

An Insight of S‐Nitrosylation of Human GIF

Chinese Journal of Chemistry, 2005
AbstractNeural growth inhibitory factor (GIF), a member of metallothionein family (metallothionein‐3, MT3), was well known by its distinct neural growth inhibitory activity, which is not shown by other MT isoforms. However, till now, people still did not know clearly how GIF exerts its biological functions.
Sun, HZ, Zhang, MJ, Huang, ZX, Teng, XC, Zheng, Q, Cai, B, Ni, FY, Xie, Y   +7 more
openaire   +3 more sources

Products of S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase: Relation between S-nitrosylation and oxidation

Biochimica et Biophysica Acta (BBA) - General Subjects, 2022
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is one of the major targets of NO in cells, especially in neurodegenerative diseases. S-Nitrosylation of GAPDH is accompanied by its translocation into the nucleus with subsequent apoptosis. The product of GAPDH modification by NO is considered to be S-nitrosylated GAPDH (GAPDH-SNO).
E V, Schmalhausen, M V, Medvedeva, M V, Serebryakova, V V, Chagovets, V I, Muronetz   +4 more
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Regulation of S-Nitrosylation in Aging and Senescence

Rejuvenation Research, 2019
Nitric oxide signals through several distinct mechanisms, including interaction with the heme group of guanylyl cyclase enzymes resulting in modulation of cyclic guanosine monophosphate levels in the vascular endothelium. Alternatively, reactive nitrogen oxide species can bind cysteine residues in target proteins forming S-nitrosothiols.
James W, Larrick, Andrew R, Mendelsohn
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Quantitative Analysis of S-Nitrosylated Proteins

2012
Protein S-nitrosylation is the covalent binding of nitric oxide to specific cysteine residues in proteins. This modification influences a large number of cellular events and signaling processes. As this process is finely regulated in vivo, the level of nitrosylation changes in response to different stimuli.
Torta, F., Bachi, A.
openaire   +2 more sources

Myosin is reversibly inhibited by S-nitrosylation

Biochemical Journal, 2009
Nitric oxide (NO•) is synthesized in skeletal muscle and its production increases during contractile activity. Although myosin is the most abundant protein in muscle, it is not known whether myosin is a target of NO• or NO• derivatives. In the present study, we have shown that exercise increases protein S-nitrosylation in muscle, and, among contractile
Leonardo, Nogueira, Cicero, Figueiredo-Freitas, Gustavo, Casimiro-Lopes, Margaret H, Magdesian, Jamil, Assreuy, Martha M, Sorenson   +5 more
openaire   +2 more sources