Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Nancy Counts Gerber"'
Autor:
Carmen R. Domingo, Diane Harris, R. David Rebanal, Sally G. Pasion, Nancy Counts Gerber, Sue V. Rosser, Laura Mamo
Publikováno v:
Journal of Diversity in Higher Education. 15:365-379
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::362a9dfad43a78bdeb49fe8a79074704
https://doi.org/10.1037/dhe0000292
https://doi.org/10.1037/dhe0000292
Publikováno v:
Analytical Biochemistry. 348:57-63
We describe the development of a rapid colorimetric assay for soluble guanylate cyclase (sGC) activity adapted for a 96-well microplate. The assay greatly decreases the analysis time and cost over traditional methodologies based on radio- and immunoa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b4c053e7f4ae774d393154213e20f18
https://doi.org/10.1016/j.ab.2005.10.008
https://doi.org/10.1016/j.ab.2005.10.008
Publikováno v:
Journal of Inorganic Biochemistry. 87:267-276
Soluble guanylate cyclase (sGC) is a receptor for endogenous and exogenous nitric oxide (NO) and is activated many fold upon its binding, making it a core enzyme in the nitric oxide signal transduction pathway. Much effort has been made to understand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1838e2db74b8efc5ef0e25da56cd9a2c
https://doi.org/10.1016/s0162-0134(01)00387-7
https://doi.org/10.1016/s0162-0134(01)00387-7
Publikováno v:
Archives of Biochemistry and Biophysics. 343:249-253
We have cloned the human liver inducible isoform of nitric oxide synthase (NOS) into an Escherichia coli expression vector and have expressed and purified the enzyme. The protein has been expressed with and without a polyhistidine tail. In both cases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfacf95c8b1056d8afabc9de6e0c5580
https://doi.org/10.1006/abbi.1997.0187
https://doi.org/10.1006/abbi.1997.0187
Autor:
Clinton R. Nishida, Ignacio Rodríguez-Crespo, Nancy Counts Gerber, Paul R. Ortiz de Montellano
Publikováno v:
Journal of Biological Chemistry. 272:6285-6290
The active site topologies of neuronal (nNOS), endothelial (eNOS), and inducible (iNOS) nitric-oxide synthases heterologously expressed in Escherichia coli have been examined using three aryldiazene (Ar-N=NH) probes. The topological information deriv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a6101450fe6412b0b858a053bae1dfe
https://doi.org/10.1074/jbc.272.10.6285
https://doi.org/10.1074/jbc.272.10.6285
Publikováno v:
Journal of Biological Chemistry. 271:11462-11467
Bovine endothelial nitric-oxide synthase (eNOS) expressed in Escherichia coli does not have the post-translational modifications found in the native enzyme and is free of tetrahydrobiopterin (BH4). In the presence of BH4, eNOS has an absorption maxim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0ff967643cfe163c358b76be580316dd
https://doi.org/10.1074/jbc.271.19.11462
https://doi.org/10.1074/jbc.271.19.11462
Publikováno v:
Chemical Research in Toxicology. 9:484-491
The Ca(2+)-dependent binding of calmodulin (CaM) to neuronal nitric oxide synthase (nNOS) stimulates the catalytic oxidation of L-arginine to nitric oxide. The CaM-dependent increase in catalytic activity is associated with an increase in the flow of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03729d3eece20a8361d8c6c46960f1c0
https://doi.org/10.1021/tx950152l
https://doi.org/10.1021/tx950152l
Publikováno v:
Journal of Biological Chemistry. 270:17791-17796
A gene coding for rat neuronal nitric oxide synthase (nNOS) has been cloned into pCWori and the vector has been expressed in Escherichia coli. The expressed enzyme has been purified with a final yield of purified protein of approximately 1 mg/g of we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2642decd4897be96357b2f4270597c3
https://doi.org/10.1074/jbc.270.30.17791
https://doi.org/10.1074/jbc.270.30.17791
Publikováno v:
The FASEB Journal. 24
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b0f0a082ac0d4ace6cfb4a42037c6262
https://doi.org/10.1096/fasebj.24.1_supplement.871.4
https://doi.org/10.1096/fasebj.24.1_supplement.871.4
Publikováno v:
Biophysical Journal. 96(3)
Nitric Oxide (NO) is an important signaling molecule that is involved in many physiological processes. In cells, NO is produced by Nitric Oxide Synthases (NOs) then bind to its principal receptor Soluble Guanylate Cyclase (sGC). Upon NO binding, sGC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d5771cfeaed0e68a851627d7f730c0c