Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Colin T, Stomberski"'
Autor:
Nicholas M. Venetos, Colin T. Stomberski, Zhaoxia Qian, Richard T. Premont, Jonathan S. Stamler
Publikováno v:
Journal of Lipid Research, Vol 65, Iss 5, Pp 100542- (2024)
Nitric oxide (NO), produced primarily by nitric oxide synthase enzymes, is known to influence energy metabolism by stimulating fat uptake and oxidation. The effects of NO on de novo lipogenesis (DNL), however, are less clear. Here we demonstrate that
Externí odkaz:
https://doaj.org/article/3cc03f53e51e45339f1a1a0980076d37
Autor:
Hua-Lin Zhou, Alfred Hausladen, Puneet Anand, Malligarjunan Rajavel, Colin T. Stomberski, Rongli Zhang, Richard T. Premont, William J. Greenlee, Focco van den Akker, Jonathan S. Stamler
Publikováno v:
Journal of Medicinal Chemistry. 66:5657-5668
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3d8a4cb7b1dbbe05bf149528ba3752d7
https://doi.org/10.1021/acs.jmedchem.2c02089
https://doi.org/10.1021/acs.jmedchem.2c02089
Autor:
Divya Seth, Colin T. Stomberski, Precious J. McLaughlin, Richard T Premont, Kathleen Lundberg, Jonathan S Stamler
Publikováno v:
Antioxidants & Redox Signaling.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da92914494399f38134a5c8490f8bbfd
https://doi.org/10.1089/ars.2022.0199
https://doi.org/10.1089/ars.2022.0199
Autor:
Colin T. Stomberski, Nicholas M. Venetos, Hua-Lin Zhou, Zhaoxia Qian, Bryce R. Collison, Seth J. Field, Richard T. Premont, Jonathan S. Stamler
Publikováno v:
Cell reports. 41(4)
Accumulating evidence suggests that protein S-nitrosylation is enzymatically regulated and that specificity in S-nitrosylation derives from dedicated S-nitrosylases and denitrosylases that conjugate and remove S-nitrosothiols, respectively. Here, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e19a52eb37517d4cc7cb1ea8a0d1f298
https://pubmed.ncbi.nlm.nih.gov/36288700
https://pubmed.ncbi.nlm.nih.gov/36288700
Publikováno v:
Antioxidants & Redox Signaling. 30:1331-1351
Significance: Protein S-nitrosylation, the oxidative modification of cysteine by nitric oxide (NO) to form protein S-nitrosothiols (SNOs), mediates redox-based signaling that conveys, in large part, the ubiquitous influence of NO on cellular function
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5a64c223d833d386768525a09707d40
https://doi.org/10.1089/ars.2017.7403
https://doi.org/10.1089/ars.2017.7403
Publikováno v:
Journal of Biological Chemistry. 294:1568-1578
Protein S-nitrosylation mediates a large part of nitric oxide's influence on cellular function by providing a fundamental mechanism to control protein function across different species and cell types. At steady state, cellular S-nitrosylation reflect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e7a1263d7deb86c990583d6c275e501
https://doi.org/10.1074/jbc.ra118.004947
https://doi.org/10.1074/jbc.ra118.004947
Autor:
Colin T. Stomberski, Zhaoxia Qian, Jonathan S. Stamler, Puneet Anand, Eugene P. Rhee, Samir M. Parikh, Rongli Zhang, Alfred Hausladen, Hua-Lin Zhou, Liwen Wang, S. Ananth Karumanchi
Publikováno v:
Nature
Endothelial nitric oxide synthase (eNOS) is protective against kidney injury, but the molecular mechanisms of this protection are poorly understood1,2. Nitric oxide-based cellular signalling is generally mediated by protein S-nitrosylation, the oxida
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::156a450fd734bfe9d35716a1cfac7ced
http://europepmc.org/articles/PMC6318002
http://europepmc.org/articles/PMC6318002
Publikováno v:
Circulation Research. 122:1485-1487
GSK3 (glycogen synthase kinase-3)—one of the busiest kinases in cells—phosphorylates >100 known substrates. Typical substrates of GSK3 contain a phosphorylated priming sequence, S/T-X-X-X-S/T(P), where the GSK3-targeted serine/threonine lies 4 re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::134659c083644c08216ff1d6ec6fa707
https://doi.org/10.1161/circresaha.118.313109
https://doi.org/10.1161/circresaha.118.313109
Autor:
Colin T, Stomberski, Puneet, Anand, Nicholas M, Venetos, Alfred, Hausladen, Hua-Lin, Zhou, Richard T, Premont, Jonathan S, Stamler
Publikováno v:
J Biol Chem
Oxidative modification of Cys residues by NO results in S-nitrosylation, a ubiquitous post-translational modification and a primary mediator of redox-based cellular signaling. Steady-state levels of S-nitrosylated proteins are largely determined by d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6ef3995c9a4ece1f7bb6115ca2be5b38
https://pubmed.ncbi.nlm.nih.gov/31649033
https://pubmed.ncbi.nlm.nih.gov/31649033
Publikováno v:
The Journal of biological chemistry. 294(5)
Protein S-nitrosylation mediates a large part of nitric oxide's influence on cellular function by providing a fundamental mechanism to control protein function across different species and cell types. At steady state, cellular S-nitrosylation reflect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::04eb23009c913fc595ac4d0f4d79e341
https://pubmed.ncbi.nlm.nih.gov/30538128
https://pubmed.ncbi.nlm.nih.gov/30538128