Zobrazeno 1 - 10
of 14
pro vyhledávání: '"J. Patrick Connick"'
Publikováno v:
Biochem J
Previous studies showed that cytochrome P450 1A2 (CYP1A2) forms a homomeric complex that influences its metabolic characteristics. Specifically, CYP1A2 activity exhibits a sigmoidal response as a function of NADPH-cytochrome P450 reductase (POR) conc
Publikováno v:
Biochem J
P450 and heme oxygenase-1 (HO-1) receive their necessary electrons by interaction with the NADPH-cytochrome P450 reductase (POR). As the POR concentration is limiting when compared with P450 and HO-1, they must effectively compete for POR to function
Publikováno v:
Drug Metabolism and Disposition. 46:197-203
Cytochromes P450s (P450s) catalyze oxygenation reactions via interactions with their redox partners. However, other proteins, particularly other P450s, also have been shown to form complexes that modulate P450 function. Previous studies showed that C
Publikováno v:
The FASEB Journal. 33
Publikováno v:
The Journal of Biological Chemistry
Heme oxygenase 1 (HO-1) and the cytochromes P450 (P450s) are endoplasmic reticulum-bound enzymes that rely on the same protein, NADPH-cytochrome P450 reductase (POR), to provide the electrons necessary for substrate metabolism. Although the HO-1 and
Publikováno v:
The FASEB Journal. 34:1-1
Publikováno v:
Biochemical Journal. 446:489-497
Previous studies have shown that the presence of one P450 enzyme can affect the function of another. The goal of the present study was to determine if P450 enzymes are capable of forming homomeric complexes that affect P450 function. To address this
Autor:
Satya Prakash Panda, Wayne L. Backes, Karen McCammon, Warren J. Huber, Pavel Martásek, Bettie Sue Siler Masters, J. Patrick Connick, Christopher C. Marohnic, James R. Reed
Publikováno v:
Archives of Biochemistry and Biophysics. 513:42-50
Genetic variations in POR, encoding NADPH-cytochrome P450 oxidoreductase (CYPOR), can diminish the function of numerous cytochromes P450, and also have the potential to block degradation of heme by heme oxygenase-I (HO-1). Purified full-length human
Autor:
Lianhong Xu, Eric F. Johnson, Manoj C. Desai, D. Fernando Estrada, Emily E. Scott, James R. Reed, Jennifer S. Laurence, J. Patrick Connick, Wayne L. Backes
This report summarizes a symposium sponsored by the American Society for Pharmacology and Experimental Therapeutics at Experimental Biology held April 20-24 in Boston, MA. Presentations discussed the status of cytochrome P450 (P450) knowledge, emphas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::843806905fb198afa51ccd7ce9ad9b59
https://europepmc.org/articles/PMC3876788/
https://europepmc.org/articles/PMC3876788/
Ligation of polyubiquitin chains to proteins is a fundamental post-translational modification, often resulting in targeted degradation of conjugated proteins. Attachment of polyubiquitin chains requires the activities of an E1 activating enzyme, an E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89dcff0f3b29fa2b2be42c79e9f613d2
https://europepmc.org/articles/PMC3605639/
https://europepmc.org/articles/PMC3605639/