Zobrazeno 1 - 10
of 327
pro vyhledávání: '"Paul R. Ortiz de Montellano"'
Publikováno v:
Biosensors, Vol 3, Iss 3, Pp 259-282 (2013)
DosS/DosR is a two-component regulatory system in which DosS, a heme-containing sensor also known as DevS, under certain conditions undergoes autophosphorylation and then transfers the phosphate to DosR, a DNA-binding protein that controls the entry
Externí odkaz:
https://doaj.org/article/1a222810d5e449dc948136c7c86eff93
Autor:
Paul R. Ortiz de Montellano
Publikováno v:
Journal of Inorganic Biochemistry. 180:235-245
The Mycobacterium tuberculosis genome encodes twenty cytochrome P450 enzymes, most or all of which appear to have specific physiological functions rather than being devoted to the removal of xenobiotics. However, in many cases their specific function
Publikováno v:
Archives of Biochemistry and Biophysics. 612:1-8
DosS is a sensor in Mycobacterium tuberculosis that differentially responds to O2, NO, and CO, as well as to changes in the redox state of the prosthetic heme iron atom. The ferrous protein and its Fe(II)-NO and Fe(II)-CO complexes undergo autophosph
Autor:
Paul R. Ortiz de Montellano
Publikováno v:
Drug Metab Rev
The oxidation of carbon-carbon triple bonds by cytochrome P450 produces ketene metabolites that are hydrolyzed to acetic acid derivatives or are trapped by nucleophiles. In the special case of 17α-ethynyl sterols, D-ring expansion and de-ethynylatio
Autor:
Paul R. Ortiz de Montellano
Publikováno v:
Handbook of Drug Metabolism ISBN: 9780429190315
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::edfd63adab723afb1e11d86fe373004a
https://doi.org/10.1201/9780429190315-3
https://doi.org/10.1201/9780429190315-3
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
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals, vol 44, iss 5
CYP2W1 is a recently discovered human cytochrome P450 enzyme with a distinctive tumor-specific expression pattern. We show here that CYP2W1 exhibits tight binding affinities for retinoids, which have low nanomolar binding constants, and much poorer b
Publikováno v:
Biochemistry
Biochemistry, vol 54, iss 46
Biochemistry, vol 54, iss 46
Mycobacterium tuberculosis (Mtb) and Mycobacterium smegmatis (Msmeg) can grow on cholesterol as the sole carbon source. In Mtb the utilization of cholesterol can be initiated by CYP125A1 or CYP142A1 and in Msmeg by the orthologous CYP125A3 and CYP142
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals, vol 46, iss 8
Ethionamide (ETH) plays a central role in the treatment of tuberculosis in patients resistant to the first-line drugs. The ETH, thioamide, and thiourea class of antituberculosis agents are prodrugs that are oxidatively converted to their active S-oxi
Autor:
Paul R, Ortiz de Montellano
Publikováno v:
Biochemistry. 57(5)