Structures of the neuronal and endothelial nitric oxide synthase heme domain with D-nitroarginine-containing dipeptide inhibitors bound
No abstract prepared.
- Research Organization:
- SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
- Sponsoring Organization:
- USDOE Office of Science (US)
- DOE Contract Number:
- AC03-76SF00515
- OSTI ID:
- 831834
- Report Number(s):
- SLAC-REPRINT-2004-071; TRN: US0406297
- Journal Information:
- Biochemistry, Vol. 43; Other Information: PBD: 1 Jan 2004
- Country of Publication:
- United States
- Language:
- English
Similar Records
Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase - implications for dimer stability and comparison with endothelial nitric-oxide synthase
Implications for Isoform selective Inhibitor Design Derived from the Binding Mode of Bulky Isothioureas to the Heme Domain of Endothelial Nitric Oxide Synthase
Structural basis for dipeptide amide isoform-selective inhibition of neuronal nitric oxide synthase
Journal Article
·
Fri Jul 23 00:00:00 EDT 1999
· Journal of Biological Chemistry
·
OSTI ID:831834
+5 more
Implications for Isoform selective Inhibitor Design Derived from the Binding Mode of Bulky Isothioureas to the Heme Domain of Endothelial Nitric Oxide Synthase
Journal Article
·
Mon Jan 01 00:00:00 EST 2001
· J.Biol.Chem.276:26486,2001
·
OSTI ID:831834
Structural basis for dipeptide amide isoform-selective inhibition of neuronal nitric oxide synthase
Journal Article
·
Thu Jan 01 00:00:00 EST 2004
· Nature Structural Biology
·
OSTI ID:831834