نتایج جستجو برای: cyp2d6

تعداد نتایج: 2395  

Journal: :Journal of the National Cancer Institute 2014
Matthew P Goetz James X Sun Vera J Suman Grace O Silva Charles M Perou Yusuke Nakamura Nancy J Cox Philip J Stephens Vincent A Miller Jeffrey S Ross David Chen Stephanie L Safgren Mary J Kuffel Matthew M Ames Krishna R Kalari Henry L Gomez Ana M Gonzalez-Angulo Octavio Burgues Hiltrud B Brauch James N Ingle Mark J Ratain Roman Yelensky

BACKGROUND Controversy exists regarding the impact of CYP2D6 genotype on tamoxifen responsiveness. We examined loss of heterozygosity (LOH) at the CYP2D6 locus and determined its impact on genotyping error when tumor tissue is used as a DNA source. METHODS Genomic tumor data from the adjuvant and metastatic settings (The Cancer Genome Atlas [TCGA] and Foundation Medicine [FM]) were analyzed t...

Journal: :Drug metabolism and disposition: the biological fate of chemicals 2002
Tomoko Shiraishi Masakiyo Hosokawa Kaoru Kobayashi Hitoshi Tainaka Yoshiyuki Yamaura Miwo Taguchi Kan Chiba

CYP2D6 is a polymorphic enzyme that catalyzes the oxidation of various drugs. At least 40-mutant alleles of CYP2D6 have been reported. CYP2D6*14, which is one of them found in Asian populations, causes deficient activity of CYP2D6. Four amino acid substitutions, P34S, G169R, R296C, and S486T, are present in the protein encoded by CYP2D6*14 (CYP2D6 14). Among them, G169R is thought to be a defin...

Journal: :British journal of pharmacology 2010
C F Samer Y Daali M Wagner G Hopfgartner C B Eap M C Rebsamen M F Rossier D Hochstrasser P Dayer J A Desmeules

BACKGROUND AND PURPOSE The major drug-metabolizing enzymes for the oxidation of oxycodone are CYP2D6 and CYP3A. A high interindividual variability in the activity of these enzymes because of genetic polymorphisms and/or drug-drug interactions is well established. The possible role of an active metabolite in the pharmacodynamics of oxycodone has been questioned and the importance of CYP3A-mediat...

Journal: :Drug metabolism and disposition: the biological fate of chemicals 2008
Masakatsu Kotsuma Hiroyuki Hanzawa Yoriko Iwata Kenji Takahashi Taro Tokui

Typical CYP2D6 substrates generally contain a basic nitrogen atom that interacts with Asp(301) and/or Glu(216) and an aromatic moiety adjacent to the site of metabolism. Recently, we found novel acidic substrates for CYP2D6, pactimibe, and its indole metabolite, R-125528, that are not protonated but are negatively charged at physiological pH. The K(m) value of R-125528 in CYP2D6-expressing micr...

Journal: :Drug metabolism and disposition: the biological fate of chemicals 2003
Lisa A McConnachie Brian Phillips Manoj Bajpai Danny D Shen Rodney J Y Ho

Genotyping of the highly polymorphic cytochrome p450 2D6 (CYP2D6) permits a gross classification of individual phenotype (viz. ultra-rapid, extensive, and poor metabolizers). It does not, however, provide a precise prediction of CYP2D6 activity, particularly in an individual possessing at least one functional CYP2D6 allele. It has been suggested that the level of mRNA expression or enzyme activ...

Journal: :Clinical cancer research : an official journal of the American Association for Cancer Research 2008
William G Newman Kristen D Hadfield Ayshe Latif Stephen A Roberts Andrew Shenton Christopher McHague Fiona Lalloo Sacha Howell D Gareth Evans

PURPOSE Tamoxifen has been the mainstay adjuvant hormonal treatment for breast cancer for many years. Conversion of tamoxifen to its active metabolite, endoxifen, is reduced by low activity of the cytochrome P450 enzyme, CYP2D6. We examined the effect of reduced CYP2D6 activity on the response to tamoxifen in patients with familial early-onset breast cancer. EXPERIMENTAL DESIGN We conducted a...

Journal: :Drug metabolism and pharmacokinetics 2014
Yuka Muroi Takahiro Saito Masamitsu Takahashi Kanako Sakuyama Yui Niinuma Miyabi Ito Chiharu Tsukada Kiminori Ohta Yasuyuki Endo Akifumi Oda Noriyasu Hirasawa Masahiro Hiratsuka

Genetic variations in cytochrome P450 2D6 (CYP2D6) contribute to interindividual variability in the metabolism of clinically used drugs, e.g., tamoxifen. CYP2D6 is genetically polymorphic and is associated with large interindividual variations in therapeutic efficacy and drug toxicity. In this study, we performed an in vitro analysis of 50 allelic variants of CYP2D6 proteins. Wild-type CYP2D6.1...

Journal: :Progress in neuro-psychopharmacology & biological psychiatry 2006
Margaret T Susce Elaina Murray-Carmichael Jose de Leon

Codeine is metabolized by the cytochrome P450 2D6 (CYP2D6) to morphine. Codeine is a much weaker agonist at mu opioid receptors than morphine. Therefore, codeine analgesia is highly dependent on CYP2D6 activity. Large prospective studies in the clinical environment do not exist, but it appears reasonable to avoid codeine use in CYP2D6 poor metabolizers (PMs). CYP2D6 metabolizes other opioid ana...

Journal: :Clinical pharmacology and therapeutics 2014
K R Crews A Gaedigk H M Dunnenberger J S Leeder T E Klein K E Caudle C E Haidar D D Shen J T Callaghan S Sadhasivam C A Prows E D Kharasch T C Skaar

Codeine is bioactivated to morphine, a strong opioid agonist, by the hepatic cytochrome P450 2D6 (CYP2D6); hence, the efficacy and safety of codeine are governed by CYP2D6 activity. Polymorphisms are a major cause of CYP2D6 variability. We summarize evidence from the literature supporting this association and provide therapeutic recommendations for codeine based on CYP2D6 genotype. This documen...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید