Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Douglas T. Hess"'
Autor:
Michael T. Forrester, Douglas T. Hess, J. Will Thompson, Rainbo Hultman, M. Arthur Moseley, Jonathan S. Stamler, Patrick J. Casey
Publikováno v:
Journal of Lipid Research, Vol 52, Iss 2, Pp 393-398 (2011)
Protein S-acylation is a major posttranslational modification whereby a cysteine thiol is converted to a thioester. A prototype is S-palmitoylation (fatty acylation), in which a protein undergoes acylation with a hydrophobic 16 carbon lipid chain. Al
Externí odkaz:
https://doaj.org/article/2f7b93eb409b49f38595ffb502bbfe7a
Autor:
Fabio V. Fonseca, Thomas M. Raffay, Kunhong Xiao, Precious J. McLaughlin, Zhaoxia Qian, Zachary W. Grimmett, Naoko Adachi, Benlian Wang, Alfred Hausladen, Brian A. Cobb, Rongli Zhang, Douglas T. Hess, Benjamin Gaston, Nevin A. Lambert, James D. Reynolds, Richard T. Premont, Jonathan S. Stamler
Publikováno v:
Molecular Cell. 82:3089-3102.e7
Autor:
Fabio V, Fonseca, Thomas M, Raffay, Kunhong, Xiao, Precious J, McLaughlin, Zhaoxia, Qian, Zachary W, Grimmett, Naoko, Adachi, Benlian, Wang, Alfred, Hausladen, Brian A, Cobb, Rongli, Zhang, Douglas T, Hess, Benjamin, Gaston, Nevin A, Lambert, James D, Reynolds, Richard T, Premont, Jonathan S, Stamler
Publikováno v:
Molecular cell. 82(16)
The β
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
Publikováno v:
Journal of Biological Chemistry. 294(7):2569-2578
With few reported exceptions, G protein–coupled receptors (GPCRs) are modified by Cys palmitoylation (S-palmitoylation). In multiple GPCRs, S-palmitoylation targets a canonical site within the C-terminal cytoplasmic tail adjacent to the C terminus
Publikováno v:
Journal of Clinical Investigation. 126:4654-4658
Homeostatic control of tissue oxygenation is achieved largely through changes in blood flow that are regulated by the classic physiological response of hypoxic vasodilation. The role of nitric oxide (NO) in the control of blood flow is a central tene
Publikováno v:
Journal of Biological Chemistry. 291:20232-20246
We report here that a population of human β2-adrenergic receptors (β2AR), a canonical G protein-coupled receptor, traffics along a previously undescribed intracellular itinerary via the Golgi complex that is associated with the sequential S-palmito
Publikováno v:
Proceedings for Annual Meeting of The Japanese Pharmacological Society. 94:3-O
Autor:
Richard E. Moon, Ryan Nazemian, Douglas T. Hess, Obada Farhan, Jonathan S. Stamler, Faisal Matto, Trevor Jenkins, John M. Longphre, Nathan Morris, Claude A. Piantadosi, James D. Reynolds
Disruption of microvascular blood flow is a common cause of tissue hypoxia in disease, yet no therapies are available that directly target the microvasculature to improve tissue oxygenation. Red blood cells (RBCs) autoregulate blood flow through S-ni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56ba3aff933fd805e4b55447d6976fa1
https://europepmc.org/articles/PMC6590078/
https://europepmc.org/articles/PMC6590078/
Autor:
Guo-Fang Zhang, Puneet Anand, Colin T. Stomberski, Yajuan Wang, Douglas T. Hess, Jonathan S. Stamler, Henri Brunengraber, Alfred Hausladen
Publikováno v:
Proceedings of the National Academy of Sciences. 111:18572-18577
Coenzyme A (CoA) mediates thiol-based acyl-group transfer (acetylation and palmitoylation). However, a role for CoA in the thiol-based transfer of NO groups (S-nitrosylation) has not been considered. Here we describe protein S-nitrosylation in yeast