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词条 UGT2B7
释义

  1. Function

  2. Structure

  3. Genetic polymorphism

  4. References

  5. Further reading

  6. External links

{{Infobox_gene}}UGT2B7 (UDP-Glucuronosyltransferase-2B7) is a phase II metabolism isoenzyme found to be active in the liver, kidneys, epithelial cells of the lower gastrointestinal tract and also has been reported in the brain. In humans, UDP-Glucuronosyltransferase-2B7 is encoded by the UGT2B7 gene.[1][2]

Function

The UGTs serve a major role in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. UGT2B7 has unique specificity for 3,4-catechol estrogens and estriol, suggesting that it may play an important role in regulating the level and activity of these potent estrogen metabolites.

This enzyme is located on the endoplasmic reticulum and nuclear membranes of cells. Its function is to catalyse the conjugation of a wide variety of lipophilic aglycon substrates with glucuronic acid, using uridine diphosphate glucuronic acid.

Together with UGT2B4, UGT2B7 is capable of glucosidation of hyodesoxycholic acid in the liver, but, unlike the 2B4 isoform, 2B7 is also able to glucuronidate various steroid hormones (androsterone, epitestosterone) and fatty acids.[3][4] It is also able to conjugate major classes of drugs such as analgesics (morphine), carboxylic nonsteroidal anti-inflammatory drugs (ketoprofen), and anticarcinogens (all-trans retinoic acid).[4] UGT2B7 is the major enzyme isoform for the metabolism of morphine to the main metabolites, morphine-3-glucuronide (M3G) which has no analgesic effect and morphine-6-glucuronide (M6G),[5] which has analgesic effects more potent than morphine.[6] As a consequence, altered UGT2B7 activity can significantly affect both the effectiveness and side-effects of morphine, as well as some related opiate drugs.[7][8][9][10][11]

Structure

No structure of a full human UGT enzyme has been determined yet, however Miley et al. resolved a partial UGT2B7 structure of the C-terminal portion showing two dimeric domains with Rossman-like folds in complex.[12][13] The Rossman fold typically binds nucleotide substrates, in this case the UDP-glucuronic acid cofactor involved in glucuronidation by UGT2B7. Generally, the C-terminus of UGT enzymes is highly conserved and binds the UDP-glucuronic acid cofactor, while the N-terminus (not resolved in this structure) is responsible for substrate binding.[14] This first resolved structure indicated that the C-terminus of one of the two dimers projected into the UDP-glucuronic acid binding site of the second dimer, thus rendering the second dimer ineffective.

Further studies have investigated dimerization of UGT enzyme polymorphisms and found both homodimer and heterodimer (with genetic polymorphisms of UGT2B7 or other UGT enzymes such as UGT1A1) formation are possible, with some combinations having an effect on enzyme activity.[15]

Genetic polymorphism

UGT2B7 is considered to be a highly polymorphic gene.[15] Various research efforts have investigated the potential effect of these polymorphic variants on glucuronidation activity of UGT2B7 and especially its clearance of administered drugs, including anticancer therapies. Decreased glucuronidation activity by genetically variant UGT2B7 could lead to increased toxicity due to elevated levels of the drug remaining or accumulating in a patient's organs especially liver, while increased activity could mean lower efficacy of the administered therapy due to lower than expected levels in the body.

One study found that Han Chinese dye-industry workers exposed to benzidine were at higher risk for developing bladder cancer if they had the UGT2B7 single nucleotide polymorphism (SNP) C802T encoding His268Tyr.[16] The histidine to tyrosine mutation at residue 268 is located in the N-terminal portion of UGT2B7, which binds the xenobiotic substrate as opposed to the C-terminus which binds UDP-glucuronic acid. The speculated mechanism for this increased cancer risk involved increased glucuronidation of benzidine by the mutant UGT2B7 followed by cleavage of the glucuronidated benzidine at urine pH levels, releasing higher concentrations of benzidine in the bladder. Another study looked for a similar association of variant UGT2B7 G900A with the risk of colorectal cancer but found no significant association.[17]

A study of erlotinib clearance in non-small cell lung cancer patients showed no statistical significance for SNPs of UGT2B7, which potentially metabolizes erlotinib as indicated by erlotinib inhibition of UGT2B7.[18] An investigation into the clearance of diclofenac, a nonsteroidal anti-inflammatory drug (NSAID) that can cause serious drug-induced liver injury, showed that mutant UGT2B7 with the C802T SNP had a 6-fold lower clearance of diclofenac than wild-type UGT27B, possibly contributing to increased liver toxicity in patients with this mutation.[19] Analysis of genetic polymorphisms of UGT2B7 in anti-tuberculosis drug-induced liver injury (ATLI) found no association between mutations of UGT2B7 and ATLI in the studied population.[20]

UGT2B7 is also known to be involved in the metabolism of opioids via glucuronidation, and a study investigating the effect of polymorphisms on the analgesic efficacy of buprenorphine found that the mutation C802T significantly worsened the analgesic response to buprenorphine after thoracic surgery, particularly at longer time-points (48 hours) where this long-lasting opioid is meant to remain effective.[21] This same variant was found separately to have significant effects on the blood plasma concentration of valproic acid administered to epilepsy patients, which may account for some of the individual variability seen with this narrow-therapeutic window treatment.[22] Both of these cases indicate decreased concentrations of drug compound probably due to increased glucuronidation activity of UGT2B7 with the C802T polymorphism.

Since UGT2B7 is involved in glucuronidation of many xenobiotic compounds, and polymorphisms of UGT2B7 are prevalent, investigation into potential effects of polymorphisms of UGT2B7 on clearance of pharmacologically relevant compounds is often of interest, as shown by the variety of studies undertaken. The UGT2B7 C802T polymorphism, for example, has been noted at 73% prevalence in Asians and 46% prevalence in Caucasians; therefore, effects of this polymorphism could impact a large portion of the population.[23] However, not all studies find significant changes in clearance due to these genetic polymorphisms. It is not always clear if this is due to the particular polymorphism not affecting enzyme activity of UGT2B7, or because the compound of interest is metabolized by various routes that can mask any differences due to changes in UGT2B7 activity.

References

1. ^{{cite journal | vauthors = Ritter JK, Sheen YY, Owens IS | title = Cloning and expression of human liver UDP-glucuronosyltransferase in COS-1 cells. 3,4-catechol estrogens and estriol as primary substrates | journal = The Journal of Biological Chemistry | volume = 265 | issue = 14 | pages = 7900–6 | date = May 1990 | pmid = 2159463 | doi = | url = http://www.jbc.org/cgi/pmidlookup?view=long&pmid=2159463 }}
2. ^{{cite journal | vauthors = Monaghan G, Clarke DJ, Povey S, See CG, Boxer M, Burchell B | title = Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13 | journal = Genomics | volume = 23 | issue = 2 | pages = 496–9 | date = September 1994 | pmid = 7835904 | doi = 10.1006/geno.1994.1531 }}
3. ^{{cite journal | vauthors = Mackenzie P, Little JM, Radominska-Pandya A | title = Glucosidation of hyodeoxycholic acid by UDP-glucuronosyltransferase 2B7 | journal = Biochemical Pharmacology | volume = 65 | issue = 3 | pages = 417–21 | date = February 2003 | pmid = 12527334 | doi = 10.1016/S0006-2952(02)01522-8 }}
4. ^1 {{cite journal | vauthors = Barre L, Fournel-Gigleux S, Finel M, Netter P, Magdalou J, Ouzzine M | title = Substrate specificity of the human UDP-glucuronosyltransferase UGT2B4 and UGT2B7. Identification of a critical aromatic amino acid residue at position 33 | journal = The FEBS Journal | volume = 274 | issue = 5 | pages = 1256–64 | date = March 2007 | pmid = 17263731 | doi = 10.1111/j.1742-4658.2007.05670.x }}
5. ^{{cite journal | vauthors = Coffman BL, Rios GR, King CD, Tephly TR | title = Human UGT2B7 catalyzes morphine glucuronidation | journal = Drug Metabolism and Disposition | volume = 25 | issue = 1 | pages = 1–4 | date = January 1997 | pmid = 9010622 | url = http://dmd.aspetjournals.org/cgi/content/abstract/25/1/1 }}
6. ^{{cite journal | vauthors = van Dorp EL, Romberg R, Sarton E, Bovill JG, Dahan A | title = Morphine-6-glucuronide: morphine's successor for postoperative pain relief? | journal = Anesthesia and Analgesia | volume = 102 | issue = 6 | pages = 1789–97 | date = June 2006 | pmid = 16717327 | doi = 10.1213/01.ane.0000217197.96784.c3 | url = http://www.anesthesia-analgesia.org/cgi/content/full/102/6/1789 }}
7. ^{{cite journal | vauthors = Coller JK, Christrup LL, Somogyi AA | title = Role of active metabolites in the use of opioids | journal = European Journal of Clinical Pharmacology | volume = 65 | issue = 2 | pages = 121–39 | date = February 2009 | pmid = 18958460 | doi = 10.1007/s00228-008-0570-y }}
8. ^{{cite journal | vauthors = Fujita K, Ando Y, Yamamoto W, Miya T, Endo H, Sunakawa Y, Araki K, Kodama K, Nagashima F, Ichikawa W, Narabayashi M, Akiyama Y, Kawara K, Shiomi M, Ogata H, Iwasa H, Okazaki Y, Hirose T, Sasaki Y | title = Association of UGT2B7 and ABCB1 genotypes with morphine-induced adverse drug reactions in Japanese patients with cancer | journal = Cancer Chemotherapy and Pharmacology | volume = 65 | issue = 2 | pages = 251–8 | date = January 2010 | pmid = 19466410 | doi = 10.1007/s00280-009-1029-2 }}
9. ^{{cite journal | vauthors = Abildskov K, Weldy P, Garland M | title = Molecular cloning of the baboon UDP-glucuronosyltransferase 2B gene family and their activity in conjugating morphine | journal = Drug Metabolism and Disposition | volume = 38 | issue = 4 | pages = 545–53 | date = April 2010 | pmid = 20071451 | pmc = 2845934 | doi = 10.1124/dmd.109.030635 }}
10. ^{{cite journal | vauthors = Pergolizzi JV, Raffa RB, Gould E | title = Considerations on the use of oxymorphone in geriatric patients | journal = Expert Opinion on Drug Safety | volume = 8 | issue = 5 | pages = 603–13 | date = September 2009 | pmid = 19614559 | doi = 10.1517/14740330903153854 }}
11. ^{{cite journal | vauthors = Rouguieg K, Picard N, Sauvage FL, Gaulier JM, Marquet P | title = Contribution of the different UDP-glucuronosyltransferase (UGT) isoforms to buprenorphine and norbuprenorphine metabolism and relationship with the main UGT polymorphisms in a bank of human liver microsomes | journal = Drug Metabolism and Disposition | volume = 38 | issue = 1 | pages = 40–5 | date = January 2010 | pmid = 19841060 | doi = 10.1124/dmd.109.029546 }}
12. ^{{cite journal | vauthors = Lampe JN | title = Advances in the Understanding of Protein-Protein Interactions in Drug Metabolizing Enzymes through the Use of Biophysical Techniques | journal = Frontiers in Pharmacology | volume = 8 | pages = 521 | date = 2017 | pmid = 28848438 | pmc = 5550701 | doi = 10.3389/fphar.2017.00521 }}
13. ^{{cite journal | vauthors = Miley MJ, Zielinska AK, Keenan JE, Bratton SM, Radominska-Pandya A, Redinbo MR | title = Crystal structure of the cofactor-binding domain of the human phase II drug-metabolism enzyme UDP-glucuronosyltransferase 2B7 | journal = Journal of Molecular Biology | volume = 369 | issue = 2 | pages = 498–511 | date = June 2007 | pmid = 17442341 | pmc = 1976284 | doi = 10.1016/j.jmb.2007.03.066 }}
14. ^{{cite journal | vauthors = Yuan L, Qian S, Xiao Y, Sun H, Zeng S | title = Homo- and hetero-dimerization of human UDP-glucuronosyltransferase 2B7 (UGT2B7) wild type and its allelic variants affect zidovudine glucuronidation activity | journal = Biochemical Pharmacology | volume = 95 | issue = 1 | pages = 58–70 | date = May 2015 | pmid = 25770680 | doi = 10.1016/j.bcp.2015.03.002 }}
15. ^1 {{cite journal | vauthors = Yuan LM, Gao ZZ, Sun HY, Qian SN, Xiao YS, Sun LL, Zeng S | title = Inter-isoform Hetero-dimerization of Human UDP-Glucuronosyltransferases (UGTs) 1A1, 1A9, and 2B7 and Impacts on Glucuronidation Activity | journal = Scientific Reports | volume = 6 | pages = 34450 | date = November 2016 | pmid = 27857056 | pmc = 5114717 | doi = 10.1038/srep34450 }}
16. ^{{cite journal | vauthors = Lin GF, Guo WC, Chen JG, Qin YQ, Golka K, Xiang CQ, Ma QW, Lu DR, Shen JH | title = An association of UDP-glucuronosyltransferase 2B7 C802T (His268Tyr) polymorphism with bladder cancer in benzidine-exposed workers in China | journal = Toxicological Sciences | volume = 85 | issue = 1 | pages = 502–6 | date = May 2005 | pmid = 15615884 | doi = 10.1093/toxsci/kfi068 | url = http://academic.oup.com/toxsci/article/85/1/502/1674327/An-Association-of-UDPGlucuronosyltransferase-2B7 }}
17. ^{{cite journal | vauthors = Falkowski S, Woillard JB, Postil D, Tubiana-Mathieu N, Terrebonne E, Pariente A, Smith D, Guimbaud R, Thalamas C, Rouguieg-Malki K, Marquet P, Picard N | title = Common variants in glucuronidation enzymes and membrane transporters as potential risk factors for colorectal cancer: a case control study | journal = BMC Cancer | volume = 17 | issue = 1 | pages = 901 | date = December 2017 | pmid = 29282011 | pmc = 5745594 | doi = 10.1186/s12885-017-3728-0 }}
18. ^{{cite journal | vauthors = Endo-Tsukude C, Sasaki JI, Saeki S, Iwamoto N, Inaba M, Ushijima S, Kishi H, Fujii S, Semba H, Kashiwabara K, Tsubata Y, Hayashi M, Kai Y, Saito H, Isobe T, Kohrogi H, Hamada A | title = Population Pharmacokinetics and Adverse Events of Erlotinib in Japanese Patients with Non-small-cell Lung Cancer: Impact of Genetic Polymorphisms in Metabolizing Enzymes and Transporters | journal = Biological & Pharmaceutical Bulletin | volume = 41 | issue = 1 | pages = 47–56 | date = 2018-01-01 | pmid = 29311482 | doi = 10.1248/bpb.b17-00521 | url = https://www.jstage.jst.go.jp/article/bpb/41/1/41_b17-00521/_article }}
19. ^{{cite journal | vauthors = Lazarska KE, Dekker SJ, Vermeulen NP, Commandeur JN | title = Effect of UGT2B7*2 and CYP2C8*4 polymorphisms on diclofenac metabolism | journal = Toxicology Letters | volume = 284 | pages = 70–78 | date = March 2018 | pmid = 29203276 | doi = 10.1016/j.toxlet.2017.11.038 | url = http://linkinghub.elsevier.com/retrieve/pii/S0378427417314996 }}
20. ^{{cite journal | vauthors = Chen G, Wu SQ, Feng M, Wang Y, Wu JC, Ji GY, Zhang MM, Liu QQ, He JQ | title = Association of UGT2B7 polymorphisms with risk of induced liver injury by anti-tuberculosis drugs in Chinese Han | journal = International Journal of Immunopathology and Pharmacology | volume = 30 | issue = 4 | pages = 434–438 | date = December 2017 | pmid = 28934901 | pmc = 5806809 | doi = 10.1177/0394632017733638 }}
21. ^{{cite journal | vauthors = Sastre JA, Varela G, López M, Muriel C, González-Sarmiento R | title = Influence of uridine diphosphate-glucuronyltransferase 2B7 (UGT2B7) variants on postoperative buprenorphine analgesia | journal = Pain Practice | volume = 15 | issue = 1 | pages = 22–30 | date = January 2015 | pmid = 24256307 | doi = 10.1111/papr.12152 }}
22. ^{{cite journal | vauthors = Sun YX, Zhuo WY, Lin H, Peng ZK, Wang HM, Huang HW, Luo YH, Tang FQ | title = The influence of UGT2B7 genotype on valproic acid pharmacokinetics in Chinese epilepsy patients | journal = Epilepsy Research | volume = 114 | pages = 78–80 | date = August 2015 | pmid = 26088889 | doi = 10.1016/j.eplepsyres.2015.04.015 }}
23. ^{{cite journal | vauthors = Lampe JW, Bigler J, Bush AC, Potter JD | title = Prevalence of polymorphisms in the human UDP-glucuronosyltransferase 2B family: UGT2B4(D458E), UGT2B7(H268Y), and UGT2B15(D85Y) | journal = Cancer Epidemiology, Biomarkers & Prevention | volume = 9 | issue = 3 | pages = 329–33 | date = March 2000 | pmid = 10750673 }}

Further reading

{{refbegin | 2}}
  • {{cite journal | vauthors = Kwara A, Lartey M, Boamah I, Rezk NL, Oliver-Commey J, Kenu E, Kashuba AD, Court MH | title = Interindividual variability in pharmacokinetics of generic nucleoside reverse transcriptase inhibitors in TB/HIV-coinfected Ghanaian patients: UGT2B71c is associated with faster zidovudine clearance and glucuronidation | journal = Journal of Clinical Pharmacology | volume = 49 | issue = 9 | pages = 1079–90 | date = September 2009 | pmid = 19628728 | pmc = 2749505 | doi = 10.1177/0091270009338482 }}
  • {{cite journal | vauthors = Hwang MS, Lee SJ, Jeong HE, Lee S, Yoo MA, Shin JG | title = Genetic variations in UDP-glucuronosyltransferase 2B7 gene (UGT2B7) in a Korean population | journal = Drug Metabolism and Pharmacokinetics | volume = 25 | issue = 4 | pages = 398–402 | year = 2010 | pmid = 20814162 | doi = 10.2133/dmpk.DMPK-10-SC-021 }}
  • {{cite journal | vauthors = Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR | title = Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score | journal = Molecular Medicine | volume = 16 | issue = 7–8 | pages = 247–53 | year = 2010 | pmid = 20379614 | pmc = 2896464 | doi = 10.2119/molmed.2009.00159 }}
  • {{cite journal | vauthors = Holmes MV, Shah T, Vickery C, Smeeth L, Hingorani AD, Casas JP | title = Fulfilling the promise of personalized medicine? Systematic review and field synopsis of pharmacogenetic studies | journal = PLOS One | volume = 4 | issue = 12 | pages = e7960 | date = December 2009 | pmid = 19956635 | pmc = 2778625 | doi = 10.1371/journal.pone.0007960 }}
  • {{cite journal | vauthors = Kwara A, Lartey M, Sagoe KW, Kenu E, Court MH | title = CYP2B6, CYP2A6 and UGT2B7 genetic polymorphisms are predictors of efavirenz mid-dose concentration in HIV-infected patients | journal = AIDS | volume = 23 | issue = 16 | pages = 2101–6 | date = October 2009 | pmid = 19779319 | pmc = 2875867 | doi = 10.1097/QAD.0b013e3283319908 }}
  • {{cite journal | vauthors = Setlur SR, Chen CX, Hossain RR, Ha JS, Van Doren VE, Stenzel B, Steiner E, Oldridge D, Kitabayashi N, Banerjee S, Chen JY, Schäfer G, Horninger W, Lee C, Rubin MA, Klocker H, Demichelis F | title = Genetic variation of genes involved in dihydrotestosterone metabolism and the risk of prostate cancer | journal = Cancer Epidemiology, Biomarkers & Prevention | volume = 19 | issue = 1 | pages = 229–39 | date = January 2010 | pmid = 20056642 | doi = 10.1158/1055-9965.EPI-09-1018 }}
  • {{cite journal | vauthors = Sánchez MB, Herranz JL, Leno C, Arteaga R, Oterino A, Valdizán EM, Nicolás JM, Adín J, Armijo JA | title = Genetic factors associated with drug-resistance of epilepsy: relevance of stratification by patient age and aetiology of epilepsy | journal = Seizure | volume = 19 | issue = 2 | pages = 93–101 | date = March 2010 | pmid = 20064729 | doi = 10.1016/j.seizure.2009.12.004 }}
  • {{cite journal | vauthors = Chen M, LeDuc B, Kerr S, Howe D, Williams DA | title = Identification of human UGT2B7 as the major isoform involved in the O-glucuronidation of chloramphenicol | journal = Drug Metabolism and Disposition | volume = 38 | issue = 3 | pages = 368–75 | date = March 2010 | pmid = 20008037 | doi = 10.1124/dmd.109.029900 }}
  • {{cite journal | vauthors = Ross CJ, Katzov-Eckert H, Dubé MP, Brooks B, Rassekh SR, Barhdadi A, Feroz-Zada Y, Visscher H, Brown AM, Rieder MJ, Rogers PC, Phillips MS, Carleton BC, Hayden MR | title = Genetic variants in TPMT and COMT are associated with hearing loss in children receiving cisplatin chemotherapy | journal = Nature Genetics | volume = 41 | issue = 12 | pages = 1345–9 | date = December 2009 | pmid = 19898482 | doi = 10.1038/ng.478 }}
  • {{cite journal | vauthors = Tang L, Ye L, Singh R, Wu B, Lv C, Zhao J, Liu Z, Hu M | title = Use of glucuronidation fingerprinting to describe and predict mono- and dihydroxyflavone metabolism by recombinant UGT isoforms and human intestinal and liver microsomes | journal = Molecular Pharmaceutics | volume = 7 | issue = 3 | pages = 664–79 | date = June 2010 | pmid = 20297805 | pmc = 2941766 | doi = 10.1021/mp900223c }}
  • {{cite journal | vauthors = Woillard JB, Rerolle JP, Picard N, Rousseau A, Drouet M, Munteanu E, Essig M, Marquet P, Le Meur Y | title = Risk of diarrhoea in a long-term cohort of renal transplant patients given mycophenolate mofetil: the significant role of the UGT1A8 2 variant allele | journal = British Journal of Clinical Pharmacology | volume = 69 | issue = 6 | pages = 675–83 | date = June 2010 | pmid = 20565459 | pmc = 2883760 | doi = 10.1111/j.1365-2125.2010.03625.x }}
  • {{cite journal | vauthors = Yu L, Qian M, Liu Y, Yao T, Zeng S | title = Stereoselective metabolism of propranolol glucuronidation by human UDP-glucuronosyltransferases 2B7 and 1A9 | journal = Chirality | volume = 22 | issue = 4 | pages = 456–61 | date = May 2010 | pmid = 19644937 | doi = 10.1002/chir.20765 }}
  • {{cite journal | vauthors = Yang JW, Lee PH, Hutchinson IV, Pravica V, Shah T, Min DI | title = Genetic polymorphisms of MRP2 and UGT2B7 and gastrointestinal symptoms in renal transplant recipients taking mycophenolic acid | journal = Therapeutic Drug Monitoring | volume = 31 | issue = 5 | pages = 542–8 | date = October 2009 | pmid = 19730281 | doi = 10.1097/FTD.0b013e3181b1dd5e }}
  • {{cite journal | vauthors = Ahn J, Schumacher FR, Berndt SI, Pfeiffer R, Albanes D, Andriole GL, Ardanaz E, Boeing H, Bueno-de-Mesquita B, Chanock SJ, Clavel-Chapelon F, Diver WR, Feigelson HS, Gaziano JM, Giovannucci E, Haiman CA, Henderson BE, Hoover RN, Kolonel LN, Kraft P, Ma J, Le Marchand L, Overvad K, Palli D, Stattin P, Stampfer M, Stram DO, Thomas G, Thun MJ, Travis RC, Trichopoulos D, Virtamo J, Weinstein SJ, Yeager M, Kaaks R, Hunter DJ, Hayes RB | title = Quantitative trait loci predicting circulating sex steroid hormones in men from the NCI-Breast and Prostate Cancer Cohort Consortium (BPC3) | journal = Human Molecular Genetics | volume = 18 | issue = 19 | pages = 3749–57 | date = October 2009 | pmid = 19574343 | pmc = 2742399 | doi = 10.1093/hmg/ddp302 }}
  • {{cite journal | vauthors = Hu M, Lui SS, Mak VW, Chu TT, Lee VW, Poon EW, Tsui TK, Ko GT, Baum L, Tam LS, Li EK, Tomlinson B | title = Pharmacogenetic analysis of lipid responses to rosuvastatin in Chinese patients | journal = Pharmacogenetics and Genomics | volume = 20 | issue = 10 | pages = 634–7 | date = October 2010 | pmid = 20679960 | doi = 10.1097/FPC.0b013e32833de489 }}
  • {{cite journal | vauthors = Zhao W, Fakhoury M, Deschênes G, Roussey G, Brochard K, Niaudet P, Tsimaratos M, André JL, Cloarec S, Cochat P, Bensman A, Azougagh S, Jacqz-Aigrain E | title = Population pharmacokinetics and pharmacogenetics of mycophenolic acid following administration of mycophenolate mofetil in de novo pediatric renal-transplant patients | journal = Journal of Clinical Pharmacology | volume = 50 | issue = 11 | pages = 1280–91 | date = November 2010 | pmid = 20147615 | doi = 10.1177/0091270009357429 }}
  • {{cite journal | vauthors = Blanca Sánchez M, Herranz JL, Leno C, Arteaga R, Oterino A, Valdizán EM, Nicolas JM, Adín J, Shushtarian M, Armijo JA | title = UGT2B7_-161C>T polymorphism is associated with lamotrigine concentration-to-dose ratio in a multivariate study | journal = Therapeutic Drug Monitoring | volume = 32 | issue = 2 | pages = 177–84 | date = April 2010 | pmid = 20216122 | doi = 10.1097/FTD.0b013e3181ceecc6 | hdl = 10261/49808 }}
  • {{cite journal | vauthors = Yong M, Schwartz SM, Atkinson C, Makar KW, Thomas SS, Newton KM, Aiello Bowles EJ, Holt VL, Leisenring WM, Lampe JW | title = Associations between polymorphisms in glucuronidation and sulfation enzymes and mammographic breast density in premenopausal women in the United States | journal = Cancer Epidemiology, Biomarkers & Prevention | volume = 19 | issue = 2 | pages = 537–46 | date = February 2010 | pmid = 20142249 | pmc = 2820123 | doi = 10.1158/1055-9965.EPI-09-0898 }}
  • {{cite journal | vauthors = Joy MS, Boyette T, Hu Y, Wang J, La M, Hogan SL, Stewart PW, Falk RJ, Dooley MA, Smith PC | title = Effects of uridine diphosphate glucuronosyltransferase 2B7 and 1A7 pharmacogenomics and patient clinical parameters on steady-state mycophenolic acid pharmacokinetics in glomerulonephritis | journal = European Journal of Clinical Pharmacology | volume = 66 | issue = 11 | pages = 1119–30 | date = November 2010 | pmid = 20567810 | pmc = 3739695 | doi = 10.1007/s00228-010-0846-x }}
{{refend}}

External links

  • {{MeshName|human+UGT2B7}}
  • {{MeshName|UGT2B7+protein,+human}}
  • {{cite web | url = http://www.pharmgkb.org/do/serve?objId=PA361 | title = GT2B7 | work = PharmGKB | publisher = PharmGKB | access-date = 2009-01-13}}
{{Glycosyltransferases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{DEFAULTSORT:Ugt2b7}}

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