Protein S-nitrosylation: a physiological signal for neuronal nitric oxide
- S. Jaffrey, H. Erdjument-Bromage, C. D. Ferris, P. Tempst, S. Snyder
- BiologyNature Cell Biology
- 1 February 2001
Protein S-nitrosylation is established as a physiological signalling mechanism for neuronally generated NO in mice harbouring a genomic deletion of neuronal NO synthase (nNOS).
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
- Makoto R. Hara, N. Agrawal, A. Sawa
- BiologyNature Cell Biology
- 1 July 2005
A signalling pathway in which nitric oxide generation that follows apoptotic stimulation elicits S-nitrosylation of GAPDH, which triggers binding to Siah1 (an E3 ubiquitin ligase), nuclear translocation and apoptosis, which is prevented by NO deletion is reported.
Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme.
It is shown that nitric oxide synthetase activity requires calmodulin, and the native enzyme appears to be a monomer.
H2S as a Physiologic Vasorelaxant: Hypertension in Mice with Deletion of Cystathionine γ-Lyase
- Guangdong Yang, Lingyun Wu, Rui Wang
- Biology, ChemistryScience
- 24 October 2008
It is shown that H2S is physiologically generated by cystathionine γ-lyase (CSE) and that genetic deletion of this enzyme in mice markedly reduces H 2S levels in the serum, heart, aorta, and other tissues.
D-serine, an endogenous synaptic modulator: localization to astrocytes and glutamate-stimulated release.
- M. Schell, M. Molliver, S. Snyder
- BiologyProceedings of the National Academy of Sciences…
- 25 April 1995
D-Serine appears to be the endogenous ligand for the glycine site of NMDA receptors, suggesting a mechanism by which astrocyte-derived D-serine could modulate neurotransmission.
H2S Signals Through Protein S-Sulfhydration
- A. Mustafa, Moataz M. Gadalla, S. Snyder
- BiologyScience Signaling
- 10 November 2009
Ex vivo endogenous H2S physiologically modifies cysteine residues in many proteins, including glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and actin, converting Cysteine -SH groups to -SSH groups in a process the authors call S-sulfhydration.
RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1.
- P. Burnett, R. Barrow, N. Cohen, S. Snyder, D. Sabatini
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 17 February 1998
It is shown that RAFT1 directly phosphorylates p70(S6k), 4E-BP1, and 4e-BP2 and that serum stimulates RAFT 1 kinase activity with kinetics similar to those of p70 (S6K) and 4E -BP1 phosphorylation.
Nitric oxide synthase and neuronal NADPH diaphorase are identical in brain and peripheral tissues.
- T. Dawson, D. Bredt, M. Fotuhi, P. Hwang, S. Snyder
- BiologyProceedings of the National Academy of Sciences…
- 1 September 1991
The identity of neuronal NO synthase and NADPH diaphorase suggests a role for NO in modulating neurotoxicity, and is in line with previous work on neuronal messenger molecules.
Localization of nitric oxide synthase indicating a neural role for nitric oxide
It is demonstrated that NO synthase in the brain to be exclusively associated with discrete neuronal populations, and prominent neural localizations provided the first conclusive evidence for a strong association of NO with neurons.
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