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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1950 1
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1962 3
1963 1
1964 2
1965 3
1966 2
1967 1
1968 2
1969 4
1970 7
1971 10
1972 9
1973 18
1974 23
1975 118
1976 123
1977 126
1978 112
1979 141
1980 144
1981 140
1982 172
1983 186
1984 179
1985 170
1986 168
1987 147
1988 117
1989 140
1990 142
1991 106
1992 131
1993 114
1994 126
1995 139
1996 155
1997 115
1998 95
1999 92
2000 107
2001 109
2002 83
2003 95
2004 92
2005 92
2006 90
2007 98
2008 91
2009 92
2010 89
2011 118
2012 94
2013 76
2014 87
2015 49
2016 56
2017 58
2018 49
2019 50
2020 45
2021 38
2022 29
2023 21
2024 6

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5,098 results

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Page 1
Molecular Cloning and Identification of NADPH Cytochrome P450 Reductase from Panax ginseng.
Zou X, Zhang Y, Zeng X, Liu T, Li G, Dai Y, Xie Y, Luo Z. Zou X, et al. Molecules. 2021 Nov 3;26(21):6654. doi: 10.3390/molecules26216654. Molecules. 2021. PMID: 34771064 Free PMC article.
Cytochrome P450 enzymes (CYP450) and their primary redox molecular companion NADPH cytochrome P450 reductase (CPR) play a key role in ginsenoside biosynthesis pathway. ...Numerous studies on ginsenoside synthesis biology still use Arabidopsis CPR (AtCPR1) as a reductase …
Cytochrome P450 enzymes (CYP450) and their primary redox molecular companion NADPH cytochrome P450 reductase (CPR) play a key role in …
NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.
Iyanagi T, Xia C, Kim JJ. Iyanagi T, et al. Arch Biochem Biophys. 2012 Dec 1;528(1):72-89. doi: 10.1016/j.abb.2012.09.002. Epub 2012 Sep 11. Arch Biochem Biophys. 2012. PMID: 22982532 Free PMC article. Review.
NOS isoforms contain additional regulatory elements within the reductase domain that control electron transfer through Ca(2+)-dependent calmodulin (CaM) binding. ...This review summarizes recent advances in our understanding of the dynamics of domain movements during CYPOR …
NOS isoforms contain additional regulatory elements within the reductase domain that control electron transfer through Ca(2+)-depende …
NADPH-cytochrome c reductase from human neutrophil membranes: purification, characterization and localization.
Nisimoto Y, Otsuka-Murakami H, Iwata S. Nisimoto Y, et al. Biochem J. 1994 Feb 1;297 ( Pt 3)(Pt 3):585-93. doi: 10.1042/bj2970585. Biochem J. 1994. PMID: 8110198 Free PMC article.
Neutrophil-membrane-associated NADPH-cytochrome c reductase and cytochrome b558 were separately eluted and highly purified by a combination of ion-exchange Sepharose, N-amino-octylagarose, 2',5'-ADP-Sepharose and heparin-Sepharose column chromatographi …
Neutrophil-membrane-associated NADPH-cytochrome c reductase and cytochrome b558 were separately eluted and highl …
A Novel, Highly Potent NADPH-Dependent Cytochrome P450 Reductase from Waste Liza klunzingeri Liver.
Bahramian Nasab S, Homaei A, Fernandez-Lafuente R, Del Arco J, Fernández-Lucas J. Bahramian Nasab S, et al. Mar Drugs. 2023 Jan 29;21(2):99. doi: 10.3390/md21020099. Mar Drugs. 2023. PMID: 36827140 Free PMC article.
The present work describes the isolation, purification and biochemical characterization of a liver NADPH-dependent cytochrome P450 reductase (CPR) from the marine fish Liza klunzingeri (LkCPR). Experimental results revealed that LkCPR is a monomer of approximately 75 kDa t …
The present work describes the isolation, purification and biochemical characterization of a liver NADPH-dependent cytochrome P450 reduct …
Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes.
Backes WL, Kelley RW. Backes WL, et al. Pharmacol Ther. 2003 May;98(2):221-33. doi: 10.1016/s0163-7258(03)00031-7. Pharmacol Ther. 2003. PMID: 12725870 Review.
Although reductase and P450 are known to form a 1:1 functional complex, there exists a 10- to 20-fold excess of P450 over the reductase. ...This review summarizes evidence supporting the potential for enzymes involved in the P450 system to interact, focusing on the …
Although reductase and P450 are known to form a 1:1 functional complex, there exists a 10- to 20-fold excess of P450 over the redu …
NADPH-cytochrome c reductase from rabbit peritoneal neutrophils. Purification, properties and function in the respiratory burst.
Laporte F, Doussiere J, Mechin V, Vignais PV. Laporte F, et al. Eur J Biochem. 1991 Feb 26;196(1):59-66. doi: 10.1111/j.1432-1033.1991.tb15785.x. Eur J Biochem. 1991. PMID: 1848186 Free article.
When NADPH was the variable substrate, a KM value of 1.9 microM for NADPH was found, but a significant deviation from Michaelis-Menten kinetics was observed at high concentrations of NADPH. Mersalyl strongly inhibited the reductase activity when added to the enzyme prior t …
When NADPH was the variable substrate, a KM value of 1.9 microM for NADPH was found, but a significant deviation from Michaelis-Menten kinet …
Preparation of homogenous NADPH cytochrome c (P-450) reductase from house flies using affinity chromatography techniques.
Mayer RT, Durrant JL. Mayer RT, et al. J Biol Chem. 1979 Feb 10;254(3):756-61. J Biol Chem. 1979. PMID: 104996 Free article.
NADPH-cytochrome c (P-450) reductase (EC 1.6.2.4) was purified to apparent homogeneity from microsomes of house flies, Musca domestica L. ...NADP+ and 2'-AMP both inhibited the reductases with apparent Ki values of 6.9 and 187 muM, respectively. These preparations of NA …
NADPH-cytochrome c (P-450) reductase (EC 1.6.2.4) was purified to apparent homogeneity from microsomes of house flies, Musca domestic …
Solution structure of the cytochrome P450 reductase-cytochrome c complex determined by neutron scattering.
Freeman SL, Martel A, Devos JM, Basran J, Raven EL, Roberts GCK. Freeman SL, et al. J Biol Chem. 2018 Apr 6;293(14):5210-5219. doi: 10.1074/jbc.RA118.001941. Epub 2018 Feb 23. J Biol Chem. 2018. PMID: 29475945 Free PMC article.
Here, using small-angle neutron scattering with contrast matching with deuterated protein, we report the solution structure of the electron transfer complex between cytochrome P450 reductase (CPR) and its electron transfer partner cytochrome c This is the first reported so …
Here, using small-angle neutron scattering with contrast matching with deuterated protein, we report the solution structure of the electron …
Purification and partial characterization of NADPH-cytochrome c reductase from Petunia hybrida flowers.
Menting JG, Cornish E, Scopes RK. Menting JG, et al. Plant Physiol. 1994 Oct;106(2):643-50. doi: 10.1104/pp.106.2.643. Plant Physiol. 1994. PMID: 7991686 Free PMC article.
NADPH-cytochrome c reductase was solubilized from the microsomal fraction of Petunia hybrida flowers by 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate detergent and purified by adenosine 2',5'-bisphosphate-Sepharose chromatography, followed …
NADPH-cytochrome c reductase was solubilized from the microsomal fraction of Petunia hybrida flowers by 3-[(3-ch …
5,098 results