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Relationship between cytochrome P450 polymorphisms and prescribed medication in elderly haemodialysis patients.

SpringerPlus

Parker K, Aasebø W, Haslemo T, Stavem K.
PMID: 27066364
Springerplus. 2016 Mar 22;5:350. doi: 10.1186/s40064-016-1986-y. eCollection 2016.

BACKGROUND: Elderly patients on haemodialysis have a high prevalence of polypharmacy and are at risk of drug-related complications. More than 80 % of all prescribed drugs are metabolized by the cytochrome P450 (CYP) enzyme system. The aims of this...

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Parker K, Aasebø W, Haslemo T, et al. Relationship between cytochrome P450 polymorphisms and prescribed medication in elderly haemodialysis patients. Springerplus. 2016;5:350doi: 10.1186/s40064-016-1986-y.
Parker, K., Aasebø, W., Haslemo, T., & Stavem, K. (2016). Relationship between cytochrome P450 polymorphisms and prescribed medication in elderly haemodialysis patients. SpringerPlus, 5350. https://doi.org/10.1186/s40064-016-1986-y
Parker, Krystina, et al. "Relationship between cytochrome P450 polymorphisms and prescribed medication in elderly haemodialysis patients." SpringerPlus vol. 5 (2016): 350. doi: https://doi.org/10.1186/s40064-016-1986-y
Parker K, Aasebø W, Haslemo T, Stavem K. Relationship between cytochrome P450 polymorphisms and prescribed medication in elderly haemodialysis patients. Springerplus. 2016 Mar 22;5:350. doi: 10.1186/s40064-016-1986-y. eCollection 2016. PMID: 27066364; PMCID: PMC4801827.
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Developmental changes in the isoenzymes controlling glycolysis in the acridine grasshopper,Caledia captiva.

Roux's archives of developmental biology : the official organ of the EDBO

Colgan DJ.
PMID: 28305256
Rouxs Arch Dev Biol. 1986 Apr;195(3):197-201. doi: 10.1007/BF02439439.

In this paper is reported an example of extensive developmental changes in the isoenzymes controlling a biochemical pathway: more than half of the glycolytic enzymes of the grasshopper,Caledia captiva differ in electrophoretic phenotype between embryonic and adult stages. A...

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Colgan DJ. Developmental changes in the isoenzymes controlling glycolysis in the acridine grasshopper,Caledia captiva. Rouxs Arch Dev Biol. 1986;195(3):197-201doi: 10.1007/BF02439439.
Colgan, D. J. (1986). Developmental changes in the isoenzymes controlling glycolysis in the acridine grasshopper,Caledia captiva. Roux's archives of developmental biology : the official organ of the EDBO, 195(3), 197-201. https://doi.org/10.1007/BF02439439
Colgan, D J. "Developmental changes in the isoenzymes controlling glycolysis in the acridine grasshopper,Caledia captiva." Roux's archives of developmental biology : the official organ of the EDBO vol. 195,3 (1986): 197-201. doi: https://doi.org/10.1007/BF02439439
Colgan DJ. Developmental changes in the isoenzymes controlling glycolysis in the acridine grasshopper,Caledia captiva. Rouxs Arch Dev Biol. 1986 Apr;195(3):197-201. doi: 10.1007/BF02439439. PMID: 28305256.
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Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria.

Planta

Nauen W, Hartmann T.
PMID: 24311259
Planta. 1980 Feb;148(1):7-16. doi: 10.1007/BF00385435.

A 2-8-fold increase in the activity of glutamate dehydrogenase (GDH), accompanied by an alteration of the GDH isoenzyme pattern, was observed in detached pea shoots floated on tap water (preincubated shoots). Sugars supressed the process, whereas NH + (4)...

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Nauen W, Hartmann T. Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria. Planta. 1980;148(1):7-16doi: 10.1007/BF00385435.
Nauen, W., & Hartmann, T. (1980). Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria. Planta, 148(1), 7-16. https://doi.org/10.1007/BF00385435
Nauen, W, and Hartmann, T. "Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria." Planta vol. 148,1 (1980): 7-16. doi: https://doi.org/10.1007/BF00385435
Nauen W, Hartmann T. Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria. Planta. 1980 Feb;148(1):7-16. doi: 10.1007/BF00385435. PMID: 24311259.
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Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

van den Berg BM, Bianchi F, Wijsman HJ.
PMID: 24263194
Theor Appl Genet. 1983 Apr;65(1):1-8. doi: 10.1007/BF00276254.

In P. hybrida and the putative progenitor species P. axillaris s. l. and P. integrifolia s. l. five mobility alleles of the structural gene prxA were found. The five alleles show differential expression during development of tissue and plant,...

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van den Berg BM, Bianchi F, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles. Theor Appl Genet. 1983;65(1):1-8doi: 10.1007/BF00276254.
van den Berg, B. M., Bianchi, F., & Wijsman, H. J. (1983). Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 65(1), 1-8. https://doi.org/10.1007/BF00276254
van den Berg, B M, et al. "Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 65,1 (1983): 1-8. doi: https://doi.org/10.1007/BF00276254
van den Berg BM, Bianchi F, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles. Theor Appl Genet. 1983 Apr;65(1):1-8. doi: 10.1007/BF00276254. PMID: 24263194.
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Genetics of the peroxidase isoenzymes in Petunia : Part 4. Location and developmental expression of the structural gene prxcC.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

van den Berg BM, Hendriks T, Wijsman HJ.
PMID: 24264828
Theor Appl Genet. 1982 Mar;64(1):75-81. doi: 10.1007/BF00303655.

By starch gel electrophoresis three mobility variants of a cathodic moving doublet of bands, encoded by the structural gene prxC, were detected in all organs of flowering petunias. In root tissue two of the variants showed a lower electrophoretic...

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van den Berg BM, Hendriks T, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : Part 4. Location and developmental expression of the structural gene prxcC. Theor Appl Genet. 1982;64(1):75-81doi: 10.1007/BF00303655.
van den Berg, B. M., Hendriks, T., & Wijsman, H. J. (1982). Genetics of the peroxidase isoenzymes in Petunia : Part 4. Location and developmental expression of the structural gene prxcC. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 64(1), 75-81. https://doi.org/10.1007/BF00303655
van den Berg, B M, et al. "Genetics of the peroxidase isoenzymes in Petunia : Part 4. Location and developmental expression of the structural gene prxcC." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 64,1 (1982): 75-81. doi: https://doi.org/10.1007/BF00303655
van den Berg BM, Hendriks T, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : Part 4. Location and developmental expression of the structural gene prxcC. Theor Appl Genet. 1982 Mar;64(1):75-81. doi: 10.1007/BF00303655. PMID: 24264828.
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Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

van den Berg BM, Bianchi F, Wijsman HJ.
PMID: 24258939
Theor Appl Genet. 1984 May;68(1):25-8. doi: 10.1007/BF00252306.

Two alleles of the structural gene prxA from Petunia, prxA6 and prxA7, could be identified by their differential temporal expression. The alleles prxA6 and prxA7 code for peroxidases with a similar electrophoretic mobility as the products of the previously...

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van den Berg BM, Bianchi F, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7. Theor Appl Genet. 1984;68(1):25-8doi: 10.1007/BF00252306.
van den Berg, B. M., Bianchi, F., & Wijsman, H. J. (1984). Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 68(1), 25-8. https://doi.org/10.1007/BF00252306
van den Berg, B M, et al. "Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 68,1 (1984): 25-8. doi: https://doi.org/10.1007/BF00252306
van den Berg BM, Bianchi F, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7. Theor Appl Genet. 1984 May;68(1):25-8. doi: 10.1007/BF00252306. PMID: 24258939.
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Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Suseelan KN, Bhatia CR, Eapen S.
PMID: 24270533
Theor Appl Genet. 1982 Mar;62(1):45-8. doi: 10.1007/BF00276281.

Two NAD-dependent alcohol dehydrogenases ADH-1 and ADH-2, under independent genetic control of genes designated as Adh-1 and Adh-2 located on chromosomes 4A, 4B and 4D, have been reported in aestivum wheat (Hart 1980). Only ADH-1 is expressed in developing...

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Suseelan KN, Bhatia CR, Eapen S. Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale. Theor Appl Genet. 1982;62(1):45-8doi: 10.1007/BF00276281.
Suseelan, K. N., Bhatia, C. R., & Eapen, S. (1982). Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 62(1), 45-8. https://doi.org/10.1007/BF00276281
Suseelan, K N, et al. "Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 62,1 (1982): 45-8. doi: https://doi.org/10.1007/BF00276281
Suseelan KN, Bhatia CR, Eapen S. Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale. Theor Appl Genet. 1982 Mar;62(1):45-8. doi: 10.1007/BF00276281. PMID: 24270533.
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Does cytochrome P450 liver isoenzyme induction increase the risk of liver toxicity after paracetamol overdose?.

Open access emergency medicine : OAEM

Kalsi SS, Wood DM, Waring WS, Dargan PI.
PMID: 27147854
Open Access Emerg Med. 2011 Oct 13;3:69-76. doi: 10.2147/OAEM.S24962. eCollection 2011.

Paracetamol (acetaminophen, N-acetyl-p-aminophenol, 4-hydroxyacetanilide) is the most common cause of acute liver failure in developed countries. There are a number of factors which potentially impact on the risk of an individual developing hepatotoxicity following an acute paracetamol overdose. These...

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Kalsi SS, Wood DM, Waring WS, et al. Does cytochrome P450 liver isoenzyme induction increase the risk of liver toxicity after paracetamol overdose?. Open Access Emerg Med. 2011;3:69-76doi: 10.2147/OAEM.S24962.
Kalsi, S. S., Wood, D. M., Waring, W. S., & Dargan, P. I. (2011). Does cytochrome P450 liver isoenzyme induction increase the risk of liver toxicity after paracetamol overdose?. Open access emergency medicine : OAEM, 369-76. https://doi.org/10.2147/OAEM.S24962
Kalsi, Sarbjeet S, et al. "Does cytochrome P450 liver isoenzyme induction increase the risk of liver toxicity after paracetamol overdose?." Open access emergency medicine : OAEM vol. 3 (2011): 69-76. doi: https://doi.org/10.2147/OAEM.S24962
Kalsi SS, Wood DM, Waring WS, Dargan PI. Does cytochrome P450 liver isoenzyme induction increase the risk of liver toxicity after paracetamol overdose?. Open Access Emerg Med. 2011 Oct 13;3:69-76. doi: 10.2147/OAEM.S24962. eCollection 2011. PMID: 27147854; PMCID: PMC4753969.
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A review of the evidence concerning hepatic glutathione depletion and susceptibility to hepatotoxicity after paracetamol overdose.

Open access emergency medicine : OAEM

Kalsi SS, Dargan PI, Waring WS, Wood DM.
PMID: 27147856
Open Access Emerg Med. 2011 Dec 23;3:87-96. doi: 10.2147/OAEM.S24963. eCollection 2011.

Paracetamol (acetaminophen) poisoning is common throughout the world. The management of nonstaggered (acute) paracetamol overdose is based on the plasma paracetamol concentration plotted on a treatment nomogram. In the UK there are two treatment lines on this nomogram, with...

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Kalsi SS, Dargan PI, Waring WS, et al. A review of the evidence concerning hepatic glutathione depletion and susceptibility to hepatotoxicity after paracetamol overdose. Open Access Emerg Med. 2011;3:87-96doi: 10.2147/OAEM.S24963.
Kalsi, S. S., Dargan, P. I., Waring, W. S., & Wood, D. M. (2011). A review of the evidence concerning hepatic glutathione depletion and susceptibility to hepatotoxicity after paracetamol overdose. Open access emergency medicine : OAEM, 387-96. https://doi.org/10.2147/OAEM.S24963
Kalsi, Sarbjeet S, et al. "A review of the evidence concerning hepatic glutathione depletion and susceptibility to hepatotoxicity after paracetamol overdose." Open access emergency medicine : OAEM vol. 3 (2011): 87-96. doi: https://doi.org/10.2147/OAEM.S24963
Kalsi SS, Dargan PI, Waring WS, Wood DM. A review of the evidence concerning hepatic glutathione depletion and susceptibility to hepatotoxicity after paracetamol overdose. Open Access Emerg Med. 2011 Dec 23;3:87-96. doi: 10.2147/OAEM.S24963. eCollection 2011. PMID: 27147856; PMCID: PMC4753970.
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Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism.

Enzyme and microbial technology

Aymard C, Belarbi A.
PMID: 11024525
Enzyme Microb Technol. 2000 Nov 01;27(8):612-618. doi: 10.1016/s0141-0229(00)00258-1.

Heat induced enzyme inactivation or protein denaturation is now well documented, due to progresses in methods, instruments and computation resources. Complex mechanisms, rather than the classic simple "one step - two states" model (still in use) are recognized in...

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Aymard C, Belarbi A. Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism. Enzyme Microb Technol. 2000;27(8):612-618doi: 10.1016/s0141-0229(00)00258-1.
Aymard, C., & Belarbi, A. (2000). Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism. Enzyme and microbial technology, 27(8), 612-618. https://doi.org/10.1016/s0141-0229(00)00258-1
Aymard, and Belarbi. "Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism." Enzyme and microbial technology vol. 27,8 (2000): 612-618. doi: https://doi.org/10.1016/s0141-0229(00)00258-1
Aymard C, Belarbi A. Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism. Enzyme Microb Technol. 2000 Nov 01;27(8):612-618. doi: 10.1016/s0141-0229(00)00258-1. PMID: 11024525.
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Inhibition of human lactate dehydrogenase isoenzymes by oestradiol-17-beta in vitro.

FEBS letters

Spellman CM, Fottrell PF.
PMID: 11946506
FEBS Lett. 1972 Mar 15;21(2):186-188. doi: 10.1016/0014-5793(72)80133-9.

No abstract available.

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Spellman CM, Fottrell PF. Inhibition of human lactate dehydrogenase isoenzymes by oestradiol-17-beta in vitro. FEBS Lett. 1972;21(2):186-188doi: 10.1016/0014-5793(72)80133-9.
Spellman, C. M., & Fottrell, P. F. (1972). Inhibition of human lactate dehydrogenase isoenzymes by oestradiol-17-beta in vitro. FEBS letters, 21(2), 186-188. https://doi.org/10.1016/0014-5793(72)80133-9
Spellman, C M., and Fottrell, P F.. "Inhibition of human lactate dehydrogenase isoenzymes by oestradiol-17-beta in vitro." FEBS letters vol. 21,2 (1972): 186-188. doi: https://doi.org/10.1016/0014-5793(72)80133-9
Spellman CM, Fottrell PF. Inhibition of human lactate dehydrogenase isoenzymes by oestradiol-17-beta in vitro. FEBS Lett. 1972 Mar 15;21(2):186-188. doi: 10.1016/0014-5793(72)80133-9. PMID: 11946506.
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Semiautomated analysis of alkaline phosphatase isoenzymes in serum of normal cynomolgus monkeys (Macaca fascicularis).

Veterinary clinical pathology

Wiedmeyer CE, Morton DG, Cusick PK, Wright T, Solter PF, Hoffmann WE.
PMID: 12075530
Vet Clin Pathol. 1999;28(1):2-7. doi: 10.1111/j.1939-165x.1999.tb01034.x.

Alkaline phosphatase (ALP) isoenzyme analysis, using a combination of wheat germ lectin (WGL) precipitation, levamisole inhibition and an automated p-nitrophenylphosphate assay was validated for use with serum from monkeys (Macaca fascicularis) and used to determine the activities of liver...

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Wiedmeyer CE, Morton DG, Cusick PK, et al. Semiautomated analysis of alkaline phosphatase isoenzymes in serum of normal cynomolgus monkeys (Macaca fascicularis). Vet Clin Pathol. 1999;28(1):2-7doi: 10.1111/j.1939-165x.1999.tb01034.x.
Wiedmeyer, C. E., Morton, D. G., Cusick, P. K., Wright, T., Solter, P. F., & Hoffmann, W. E. (1999). Semiautomated analysis of alkaline phosphatase isoenzymes in serum of normal cynomolgus monkeys (Macaca fascicularis). Veterinary clinical pathology, 28(1), 2-7. https://doi.org/10.1111/j.1939-165x.1999.tb01034.x
Wiedmeyer, Charles E., et al. "Semiautomated analysis of alkaline phosphatase isoenzymes in serum of normal cynomolgus monkeys (Macaca fascicularis)." Veterinary clinical pathology vol. 28,1 (1999): 2-7. doi: https://doi.org/10.1111/j.1939-165x.1999.tb01034.x
Wiedmeyer CE, Morton DG, Cusick PK, Wright T, Solter PF, Hoffmann WE. Semiautomated analysis of alkaline phosphatase isoenzymes in serum of normal cynomolgus monkeys (Macaca fascicularis). Vet Clin Pathol. 1999;28(1):2-7. doi: 10.1111/j.1939-165x.1999.tb01034.x. PMID: 12075530.
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