Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Clinton R. Nishida"'
Autor:
Debashree Basudhar, Clinton R. Nishida, Yarrow Madrona, Pierre Moënne-Loccoz, Erik T. Yukl, Santhosh Sivaramakrishnan, Paul R. Ortiz de Montellano
Publikováno v:
The Journal of biological chemistry, vol 291, iss 31
Mycobacterium tuberculosis DosS is critical for the induction of M. tuberculosis dormancy genes in response to nitric oxide (NO), carbon monoxide (CO), or hypoxia. These environmental stimuli, which are sensed by the DosS heme group, result in autoph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3da63315f85b8b9a3d94469627086eba
https://doi.org/10.1074/jbc.m116.724815
https://doi.org/10.1074/jbc.m116.724815
Autor:
Asvi A. Francois, Ian Phillips, Paul R. Ortiz de Montellano, Clinton R. Nishida, Elizabeth A. Shephard
Publikováno v:
Drug Metabolism and Disposition. 37:178-186
The second-line antitubercular drugs thiacetazone (TAZ) and ethionamide (ETA) are bioactivated by the mycobacterial enzyme EtaA. We report here that human flavin-containing monooxygenase 2.1 (FMO2.1), which is expressed predominantly in the lung, cat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71d371de1f656c46796c8c519794d243
https://doi.org/10.1124/dmd.108.024158
https://doi.org/10.1124/dmd.108.024158
Publikováno v:
Biochemistry. 47:2071-2079
The crystal structure of a cytochrome P450 from the thermoacidophile Picrophilus torridus, CYP231A2 (PTO1399), has been solved. This structure reveals a wide open substrate access channel. To better understand ligand-induced structural transitions in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5563e7dd6b769bfb170b56f43f63c7df
https://doi.org/10.1021/bi702240k
https://doi.org/10.1021/bi702240k
Autor:
Paul R. Ortiz de Montellano, Huiying Li, Thomas L. Poulos, Shingo Nagano, Hideaki Shimizu, Clinton R. Nishida, Hiroshi Ogura
Publikováno v:
Journal of Biological Chemistry. 278:44886-44893
Epothilones are potential anticancer drugs that stabilize microtubules by binding to tubulin in a manner similar to paclitaxel. Cytochrome P450epoK (P450epoK), a heme containing monooxygenase involved in epothilone biosynthesis in the myxobacterium S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd2dc7f56472eb61aff99016c82034a9
https://doi.org/10.1074/jbc.m308115200
https://doi.org/10.1074/jbc.m308115200
Publikováno v:
Journal of Biological Chemistry. 278:31814-31824
Inducible (iNOS) and constitutive (eNOS, nNOS) nitric-oxide synthases differ in their Ca2+-calmodulin (CaM) dependence. iNOS binds CaM irreversibly but eNOS and nNOS, which bind CaM reversibly, have inserts in their reductase domains that regulate el
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcefd42f31a94ee6487d9df5dc42d7e4
https://doi.org/10.1074/jbc.m303267200
https://doi.org/10.1074/jbc.m303267200
Autor:
Paul R. Ortiz de Montellano, Clinton R. Nishida, Snezana Djordjevic, Patrick J. Hillas, Christine M. Nunn
Publikováno v:
Journal of Biological Chemistry. 277:20033-20040
The resistance of Mycobacterium tuberculosis to isoniazid is commonly linked to inactivation of a catalase-peroxidase, KatG, that converts isoniazid to its biologically active form. Loss of KatG is associated with elevated expression of the alkylhydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4977e5437468bf4380946b64b03c6fe
https://doi.org/10.1074/jbc.m200864200
https://doi.org/10.1074/jbc.m200864200
Autor:
Debashree Basudhar, Clinton R. Nishida, Jed N. Lampe, Sylvie E. Kandel, Paul R. Ortiz de Montellano, Yarrow Madrona
Publikováno v:
The Journal of biological chemistry, vol 290, iss 16
Defining the conformational states of cytochrome P450 active sites is critical for the design of agents that minimize drug-drug interactions, the development of isoform-specific P450 inhibitors, and the engineering of novel oxidative catalysts. We us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c88517b76685ac84d8cf033c9787f5ec
https://pubmed.ncbi.nlm.nih.gov/25670859
https://pubmed.ncbi.nlm.nih.gov/25670859
Publikováno v:
Journal of Biological Chemistry. 276:20116-20124
To clarify the role of the autoinhibitory insert in the endothelial (eNOS) and neuronal (nNOS) nitric-oxide synthases, the insert was excised from nNOS and chimeras with its reductase domain; the eNOS and nNOS inserts were swapped and put into the no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::220c45d534848ba17670458562c7326c
https://doi.org/10.1074/jbc.m101548200
https://doi.org/10.1074/jbc.m101548200
Autor:
Clinton R. Nishida, Giselle M. Knudsen, Ignacio Rodríguez-Crespo, Paul R. Ortiz de Montellano
Publikováno v:
Journal of Biological Chemistry. 274:21617-21624
Five conserved histidine residues are found in the human endothelial nitric-oxide synthase (NOS) heme domain: His-420, His-421, and His-461 are close to the heme, whereas His-146 and His-214 are some distance away. To investigate whether the histidin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fb79956eda662090eee9926fe26f434d
https://doi.org/10.1074/jbc.274.31.21617
https://doi.org/10.1074/jbc.274.31.21617
Publikováno v:
Journal of Biological Chemistry. 274:14692-14698
The primary sequences of the three mammalian nitric- oxide synthase (NOS) isoforms differ by the insertion of a 52–55-amino acid loop into the reductase domains of the endothelial (eNOS) and neuronal (nNOS), but not inducible (iNOS). On the basis o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bd79ccd34543c7a77b68a152b97fb31
https://doi.org/10.1074/jbc.274.21.14692
https://doi.org/10.1074/jbc.274.21.14692