Polymorphisms of genes related to phase II metabolism and resistance to clopidogrel

References

• 1. Jung JH, Tantry US, Gurbel PA, Jeong YH. Current antiplatelet treatment strategy in patients with diabetes mellitus. Diabet. Metab. J. 39(2), 95–113 (2015).
  MedlineGoogle Scholar
• 2. Bernlochner I, Sibbing D. Thienopyridines and other ADP-receptor antagonists. Handb. Exp. Pharmacol. 210, 165–198 (2012).
  CASGoogle Scholar
• 3. Frelinger AL, Bhatt DL, Lee RD et al. Clopidogrel pharmacokinetics and pharmacodynamics vary widely despite exclusion or control of polymorphisms (CYP2C19, ABCB1, PON1), noncompliance, diet, smoking, co-medications (including proton pump inhibitors), and pre-existent variability in platelet function. J. Am. Coll. Cardiol. 61(8), 872–879 (2013).
  Medline CASGoogle Scholar
• 4. Zhu Y, Zhou J. In vitro biotransformation studies of 2-oxo-clopidogrel: multiple thiolactone ring-opening pathways further attenuate prodrug activation. Chem. Res. Toxicol. 26(1), 179–190 (2013).
  Medline CASGoogle Scholar
• 5. Alkattan A, Alsalameen E. Polymorphisms of genes related to phase-I metabolic enzymes affecting the clinical efficacy and safety of clopidogrel treatment. Expert Opin. Drug Metab. Toxicol. 15, 1–1 (2021).
  Google Scholar
• 6. Simon T .French Registry of Acute ST-Elevation and Non-ST-Elevation Myocardial Infarction (FAST-MI) Investigators. Genetic determinants of response to clopidogrel and cardiovascular events. N. Engl. J. Med. 360(4), 363–375 (2009).
  Medline CASGoogle Scholar
• 7. Geisler T, Schaeffeler E, Dippon J et al. CYP2C19 and nongenetic factors predict poor responsiveness to clopidogrel loading dose after coronary stent implantation. Pharmacogenomics 9(9), 1251–1259 (2008).
  CASGoogle Scholar
• 8. Harmsze A, Van Werkum JW, Bouman HJ et al. Besides CYP2C19*2, the variant allele CYP2C9*3 is associated with higher on clopidogrel platelet reactivity in patients on dual antiplatelet therapy undergoing elective coronary stent implantation. Pharmacogenet. Genom. 20(1), 18–25 (2010).
  Medline CASGoogle Scholar
• 9. Alhazzani AA, Munisamy M, Karunakaran G. Pharmacogenetics of CYP2C19 genetic polymorphism on clopidogrel response in patients with ischemic stroke from Saudi Arabia. Neurosci. J. 22(1), 31–37 (2017).
  Google Scholar
• 10. Al-Azzam SI, Alzoubi KH, Khabour OF et al. Factors that contribute to clopidogrel resistance in cardiovascular disease patients: environmental and genetic approach. Int. J. Clin. Pharmacol. Ther. 51(3), 179–186 (2013).
  Medline CASGoogle Scholar
• 11. Ayesh BM, Al-Astal IR, Yassin MM. The clinical effects of CYP2C19*2 allele frequency on Palestinian patients receiving clopidogrel after percutaneous coronary intervention. Int. J. Clin. Pharmacol. Ther. 41(1), 96–103 (2019).
  CASGoogle Scholar
• 12. Khalil BM, Shahin MH, Solayman MH et al. Genetic and nongenetic factors affecting clopidogrel response in the Egyptian population. Clin. Trans. Sci. 9(1), 23–28 (2016).
  Medline CASGoogle Scholar
• 13. Mohammad AM, Al-Allawi NA. CYP2C19 genotype is an independent predictor of adverse cardiovascular outcome in Iraqi patients on clopidogrel after percutaneous coronary intervention. J. Cardiovasc. Pharmacol. 71(6), 347–351 (2018).
  Medline CASGoogle Scholar
• 14. Hagihara K, Kazui M, Kurihara A, Ikeda T, Izumi T. Glutaredoxin is involved in the formation of the pharmacologically active metabolite of clopidogrel from its GSH conjugate. Drug Metab. Dispos. 40(9), 1854–1859 (2012).
  Medline CASGoogle Scholar
• 15. Bubp J, Jen M, Matuszewski K. Caring for glucose-6-phosphate dehydrogenase (G6PD)-deficient patients: implications for pharmacy. Pharm. Ther. 40(9), 572 (2015).
  Google Scholar
• 16. Berkholz DS, Faber HR, Savvides SN, Karplus PA. Catalytic cycle of human glutathione reductase near 1 Å resolution. J. Mol. Biol. 382(2), 371–384 (2008).
  Medline CASGoogle Scholar
• 17. Paramasivan K, Mutturi S. Regeneration of NADPH coupled with HMG-CoA reductase activity increases squalene synthesis in Saccharomyces cerevisiae. J. Agricult. Food Chem. 65(37), 8162–8170 (2017).
  Medline CASGoogle Scholar
• 18. Alharbi KK, Khan IA, Abed AS, Syed R. Insertion/deletion polymorphisms do play any role in G6PD deficiency individuals in the Kingdom of the Saudi Arabia. Bioinformation 9(1), 49 (2013).
  MedlineGoogle Scholar
• 19. Gómez-Manzo S, Marcial-Quino J, Vanoye-Carlo A et al. Glucose-6-phosphate dehydrogenase: update and analysis of new mutations around the world. Int. J. Mol. Sci. 17(12), 2069 (2016).
  Google Scholar
• 20. McDonagh EM, Thorn CF, Bautista JM, Youngster I, Altman RB, Klein TE. PharmGKB summary: very important pharmacogene information for G6PD. Pharmacogenet. Genom. 22(3), 219 (2012).
  Medline CASGoogle Scholar
• 21. Kashmoola MA, Eissa AA, Al-Takay DT, Al-Allawi NA. Molecular characterization of G6PD deficient variants in Nineveh Province, Northwestern Iraq. Indian J. Hematol. Blood Transfus. 31(1), 133–136 (2015).
  MedlineGoogle Scholar
• 22. Sirdah M, Reading NS, Perkins SL, Shubair M, Aboud L, Prchal JT. Hemolysis and Mediterranean G6PD mutation (c.563 C>T) and c.1311 C>T polymorphism among Palestinians at Gaza Strip. Blood Cells Mol. Dis. 48(4), 203–208 (2012).
  Medline CASGoogle Scholar
• 23. Sanephonasa A, Cheepsunthorn CL, Khaminsou N, Savongsy O, Nuchprayoon I, Leecharoenkiat K. Molecular characterization of G6PD mutationsreveals the high frequency of G6PD Aures in the Lao Theung population. Malaria Journal 20(1), 1–9 (2021).
  MedlineGoogle Scholar
• 24. Xu W, Westwood B, Bartsocas CS et al. Glucose-6phosphate dehydrogenase mutations and haplotypes in various ethnic groups.. Blood 85(1), 257 (1995).
  Medline CASGoogle Scholar
• 25. Sutton HE, Omenn GS, Fabry's disease: the search for a regulator genemutation in man. American journal of human genetics 24(3), 343(1972).
  Medline CASGoogle Scholar
• 26. Espinosa-Diez C, Fierro-Fernandez M, Sanchez-Gomez F et al. Targeting of gamma-glutamyl-cysteine ligase by miR-433 reduces glutathione biosynthesis and promotes TGF-β-dependent fibrogenesis. Antiox. Redox Sig. 23(14), 1092–1105 (2015).
  Medline CASGoogle Scholar
• 27. Franklin CC, Backos DS, Mohar I, White CC, Forman HJ, Kavanagh TJ. Structure, function, and post-translational regulation of the catalytic and modifier subunits of glutamate cysteine ligase. Mol. Aspects Med. 30(1–2), 86–98 (2009).
  Medline CASGoogle Scholar
• 28. Wang D, Curtis A, Papp AC, Koletar SL, Para MF. Polymorphism in glutamate cysteine ligase catalytic subunit (GCLC) is associated with sulfamethoxazole-induced hypersensitivity in HIV/AIDS patients. BMC Med. Genom. 5(1), 1–9 (2012).
  Medline CASGoogle Scholar
• 29. Campolo J, Penco S, Bianchi E et al. Glutamate-cysteine ligase polymorphism, hypertension, and male sex are associated with cardiovascular events. Biochemical and genetic characterization of Italian subpopulation. Am. Heart J. 154(6), 1123–1129 (2007).
  Medline CASGoogle Scholar
• 30. Lu SC. Glutathione synthesis. Biochim. Biophys. Acta 1830(5), 3143–3153 (2013).
  Medline CASGoogle Scholar
• 31. Xia H, Ye J, Wang L, Zhu J, He Z. A case of severe glutathione synthetase deficiency with novel GSS mutations. Braz. J. Med. Biol. Res. 51(3), e6853 (2018).
  Medline CASGoogle Scholar
• 32. Shi ZZ, Habib GM, Rhead WJ et al. Mutations in the glutathione synthetase gene cause 5–oxoprolinuria. Nat. Genet. 14(3), 361–365 (1996).
  Medline CASGoogle Scholar
• 33. Njålsson R, Ristoff E, Carlsson K, Winkler A, Larsson A, Norgren S. Genotype, enzyme activity, glutathione level, and clinical phenotype in patients with glutathione synthetase deficiency. Human Genet. 116(5), 384–389 (2005).
  MedlineGoogle Scholar
• 34. Li X, Ding Y, Liu Y et al. Five Chinese patients with 5-oxoprolinuria due to glutathione synthetase and 5-oxoprolinase deficiencies. Brain Devel. 37(10), 952–959 (2015).
  MedlineGoogle Scholar
• 35. Soylu Ustkoyuncu P, Mutlu FT, Kiraz A, Tag Balkis Z, Yel S. A rare cause of neonatal hemolytic anemia: glutathione synthetase deficiency. J. Pediatr. Hematol. Oncol. 40(1), e45–e49 (2018).
  MedlineGoogle Scholar
• 36. Dong SC, Sha HH, Xu XY et al. Glutathione S-transferase π: a potential role in antitumor therapy. Drug Design Devel. Ther. 12, 3535 (2018).
  Medline CASGoogle Scholar
• 37. Pearson WR, Vorachek WR, Xu SJ et al. Identification of class-mu glutathione transferase genes GSTM1–GSTM5 on human chromosome 1p13. Am. J. Human Genet. 53(1), 220 (1993).
  Medline CASGoogle Scholar
• 38. Hadami K, Dakka N, Bensaid M et al. Evaluation of glutathione S-transferase pi 1 expression and gene promoter methylation in Moroccan patients with urothelial bladder cancer. Mol. Genet. Genom. Med. 6(5), 819–827 (2018).
  Medline CASGoogle Scholar
• 39. Hansen KA, Eyster KM. Genetics and genomics of endometriosis. Clin. Obstet. Gynecol. 53(2), 403 (2010).
  MedlineGoogle Scholar
• 40. Matsumura T, Imamichi Y, Mizutani T et al. Human glutathione S-transferase A (GSTA) family genes are regulated by steroidogenic factor 1 (SF-1) and are involved in steroidogenesis. FASEB J. 27(8), 3198–3208 (2013).
  Medline CASGoogle Scholar
• 41. Nebert DW, Vasiliou V. Analysis of the glutathione S-transferase (GST) gene family. Human Genom. 1(6), 1–5 (2004).
  Google Scholar
• 42. Adams CH, Werely CJ, Victor TC, Hoal EG, Rossouw G, van Helden PD. Allele frequencies for glutathione S-transferase and N-acetyltransferase 2 differ in African population groups and may be associated with oesophageal cancer or tuberculosis incidence. Clin. Chem. Lab. Med. 41(4), 600–605 (2003).
  Medline CASGoogle Scholar
• 43. Roodi N, Dupont WD, Moore JH, Parl FF. Association of homozygous wild-type glutathione S-transferase M1 genotype with increased breast cancer risk. Cancer Res. 64(4), 1233–1236 (2004).
  Medline CASGoogle Scholar
• 44. Sharma A, Pandey A, Sharma S et al. Genetic polymorphism of glutathione S-transferase P1 (GSTP1) in Delhi population and comparison with other global populations. Meta Gene 2, 134–142 (2014).
  MedlineGoogle Scholar
• 45. Cho HJ, Lee SY, Ki CS, Kim JW. GSTM1, GSTT1 and GSTP1 polymorphisms in the Korean population. J. Korean Med. Sci. 20(6), 1089–1092 (2005).
  Medline CASGoogle Scholar
• 46. Bremer S, Fløisand Y, Brinch L, Gedde-Dahl T, Bergan S. Glutathione transferase gene variants influence busulfan pharmacokinetics and outcome after myeloablative conditioning. Therapeut. Drug Monit. 37(4), 493 (2015).
  Medline CASGoogle Scholar
• 47. Sharif MR, Sharif A, Kheirkhah D, Taghavi Ardakan M, Soltani N. Association of GSTO1 A140D and GSTO2 N142D gene variations with breast cancer risk. Asian Pac. J. Cancer Prev. 18(6), 1723–1727 (2017).
  MedlineGoogle Scholar
• 48. White CW, Mimmack RF, Repine JE. Accumulation of lung tissue oxidized glutathione (GSSG) as a marker of oxidant induced lung injury. Chest 89(3), S111–S113 (1986).
  Google Scholar
• 49. Pekkanen L, Rusi M. The effects of dietary niacin and riboflavin on voluntary intake and metabolism of ethanol in rats. Pharmacol. Biochem. Behav. 11(5), 575–579 (1979).
  Medline CASGoogle Scholar
• 50. Baity M, Wang L, Correa AM et al. Glutathione reductase (GSR) gene deletion and chromosome 8 aneuploidy in primary lung cancers detected by fluorescence in situ hybridization. Am. J. Cancer Res. 9(6), 1201 (2019).
  Medline CASGoogle Scholar
• 51. Kitoh R, Nishio SY, Usami SI. Prognostic impact of gene polymorphisms in patients with idiopathic sudden sensorineural hearing loss. Acta Otolaryngol. 137(Suppl. 565), S24–S29 (2017).
  Medline CASGoogle Scholar
• 52. Sharma V, Ichikawa M, Freeze HH. Mannose metabolism: more than meets the eye. Biochem. Biophys. Res. Commun. 453(2), 220–228 (2014).
  Medline CASGoogle Scholar
• 53. Medrano A, García-Gil N, Ramió L et al. Hexose-specificity of hexokinase and ADP-dependence of pyruvate kinase play important roles in the control of monosaccharide utilization in freshly diluted boar spermatozoa. Mol. Reprod. Devel. 73(9), 1179–1194 (2006).
  Medline CASGoogle Scholar
• 54. Zhang Z, Yang Z, Zhu B et al. Increasing glucose 6-phosphate dehydrogenase activity restores redox balance in vascular endothelial cells exposed to high glucose. PloS ONE 7(11), e49128 (2012).
  Medline CASGoogle Scholar
• 55. Harrington GN, Bush DR. The bifunctional role of hexokinase in metabolism and glucose signaling. Plant Cell 15(11), 2493–2496 (2003).
  Medline CASGoogle Scholar
• 56. Sullivan LS, Koboldt DC, Bowne SJ et al. A dominant mutation in hexokinase 1 (HK1) causes retinitis pigmentosa. Invest. Ophthalmol. Visual Sci. 55(11), 7147–7158 (2014).
  Medline CASGoogle Scholar
• 57. Suazo J, Pardo R, Castillo S et al. Family-based association study between SLC2A1, HK1, and LEPR polymorphisms with myelomeningocele in Chile. Reprod. Sci. 20(10), 1207–1214 (2013).
  MedlineGoogle Scholar
• 58. Sevilla T, Martínez-Rubio D, Márquez C et al. Genetics of the Charcot–Marie–Tooth disease in the Spanish Gypsy population: the hereditary motor and sensory neuropathy–Russe in depth. Clin. Genet. 83(6), 565–570 (2013).
  Medline CASGoogle Scholar
• 59. Gabrikova D, Mistrik M, Bernasovska J et al. Founder mutations in NDRG1 and HK1 genes are common causes of inherited neuropathies among Roma/Gypsies in Slovakia. J. Appl. Genet. 54(4), 455–460 (2013).
  Medline CASGoogle Scholar
• 60. Liu H, Yang H, Wang X, Tu Y. The contribution of hexokinase 2 in glioma. Cancer Transl. Med. 4(2), 54 (2018).
  CASGoogle Scholar
• 61. Lehto M, Huang X, Davis EM et al. Human hexokinase II gene: exon–intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia 38(12), 1466–1474 (1995).
  Medline CASGoogle Scholar
• 62. Echwald SM, Bjørbaek C, Hansen T et al. Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes 44(3), 347–353 (1995).
  Medline CASGoogle Scholar
• 63. Ardehali H, Tiller GE, Printz RL, Mochizuki H, Prochazka M, Granner DK. A novel (TA)n polymorphism in the hexokinase II gene: application to noninsulin-dependent diabetes mellitus in the Pima Indians. Human Genet. 97(4), 482–485 (1996).
  Medline CASGoogle Scholar
• 64. Roberts DJ, Miyamoto S. Hexokinase II integrates energy metabolism and cellular protection: AKTing on mitochondria and TORCing to autophagy. Cell Death Diff. 22(2), 248–257 (2015).
  Medline CASGoogle Scholar
• 65. Rabbani N, Thornalley PJ. Hexokinase-2 glycolytic overload in diabetes and ischemia–reperfusion injury. Trends Endocrinol. Metab. 30(7), 419–431 (2019).
  Medline CASGoogle Scholar
• 66. Colosimo A, Calabrese G, Gennarelli M et al. Assignment of the hexokinase type 3 gene (HK3) to human chromosome band 5q35.3 by somatic cell hybrids and in situ hybridization. Cytogenet. Genome Res. 74(3), 187–188 (1996).
  CASGoogle Scholar
• 67. Qin Y, Sun M, You L et al. ESR1, HK3 and BRSK1 gene variants are associated with both age at natural menopause and premature ovarian failure. Orphanet J. Rare Dis. 7(1), 1–6 (2012).
  Medline CASGoogle Scholar
• 68. Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J. Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p13. Diabetologia 35(8), 743–747 (1992).
  Medline CASGoogle Scholar
• 69. Matschinsky FM, Wilson DF. The central role of glucokinase in glucose homeostasis: a perspective 50 years after demonstrating the presence of the enzyme in islets of Langerhans. Front. Physiol. 10, 148 (2019).
  MedlineGoogle Scholar
• 70. Wędrychowicz A, Tobór E, Wilk M et al. Phenotype heterogeneity in glucokinase–maturity-onset diabetes of the young (GCK-MODY) patients. J. Clin. Res. Pediatr. Endocrinol. 9(3), 246 (2017).
  MedlineGoogle Scholar
• 71. Tinto N, Zagari A, Capuano M et al. Glucokinase gene mutations: structural and genotype-phenotype analyses in MODY children from South Italy. PloS ONE 3(4), e1870 (2008).
  MedlineGoogle Scholar
• 72. Bonfig W, Hermanns S, Warncke K et al. GCK-MODY (MODY 2) caused by a novel p.Phe330Ser mutation. Int. Schol. Res. Notices 2011, 676549 (2011).
  Google Scholar
• 73. Lukášová P, Vcelak J, Vankova M, Vejražková D, Andelova K, Bendlova B. Screening of mutations and polymorphisms in the glucokinase gene in Czech diabetic and healthy control populations. Physiol. Res. 57(Suppl. 1), S99–S108 (2008).
  Medline CASGoogle Scholar
• 74. Beer NL, Osbak KK, van de Bunt M et al. Insights into the pathogenicity of rare missense GCK variants from the identification and functional characterization of compound heterozygous and double mutations inherited in cis. Diabetes Care 35(7), 1482–1484 (2012).
  Medline CASGoogle Scholar
• 75. Osbak KK, Colclough K, Saint-Martin C et al. Update on mutations in glucokinase (GCK), which cause maturity-onset diabetes of the young, permanent neonatal diabetes, and hyperinsulinemic hypoglycemia. Hum. Mutat. 30(11), 1512–1526 (2009).
  Medline CASGoogle Scholar
• 76. Khalil R, Al-Sheyab F, Khamaiseh E, Halaweh MA, Abder-Rahman HA. Screening of mutations in the GCK gene in Jordanian maturity-onset diabetes of the young type 2 (MODY2) patients. Genet. Mol. Res. 8(2), 500–506 (2009).
  Medline CASGoogle Scholar
• 77. Hassan SM, Iyer AP, Al-Abbasi FA. Screening for glucokinase (GCK) gene mutation in gestational diabetes women in western region of Saudi Arabia. Br. J. Med. Med. Res. 13(8), 1–10 (2016).
  Google Scholar
• 78. Gallogly MM, Starke DW, Mieyal JJ. Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation. Antiox. Redox Sig. 11(5), 1059–1081 (2009).
  Medline CASGoogle Scholar
• 79. Rodrıguez-Manzaneque MT, Tamarit J, Bellı G, Ros J, Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol. Biol. Cell 13(4), 1109–1121 (2002).
  Medline CASGoogle Scholar
• 80. Hoffmann B, Uzarska MA, Berndt C et al. The multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional group. Antiox. Redox Sig. 15(1), 19–30 (2011).
  Medline CASGoogle Scholar
• 81. Gladyshev VN, Liu A, Novoselov SV et al. Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2. J. Biol. Chem. 276(32), 30374–30380 (2001).
  Medline CASGoogle Scholar
• 82. Park JB, Levine M. Cloning, sequencing, and characterization of alternatively spliced glutaredoxin 1 cDNA and its genomic gene: chromosomal localization, mRNA stability, and origin of pseudogenes. J. Biol. Chem. 280(11), 10427–10434 (2005).
  Medline CASGoogle Scholar
• 83. Wu H, Lin L, Giblin F, Ho YS, Lou MF. Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells. Free Rad. Biol. Med. 51(11), 2108–2117 (2011).
  Medline CASGoogle Scholar
• 84. Lillig CH, Berndt C, Vergnolle O et al. Characterization of human glutaredoxin 2 as iron–sulfur protein: a possible role as redox sensor. Proc. Natl Acad. Sci. USA 102(23), 8168–8173 (2005).
  Medline CASGoogle Scholar
• 85. Johansson C, Lillig CH, Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J. Biol. Chem. 279(9), 7537–7543 (2004).
  Medline CASGoogle Scholar
• 86. Čiuladaitė Ž, Burnytė B, Vansevičiūtė D, Dagytė E, Kučinskas V, Utkus A. Clinical, cytogenetic and molecular study of a case of ring chromosome 10. Mol. Cytogenet. 8(1), 1–6 (2015).
  MedlineGoogle Scholar
• 87. Haunhorst P, Berndt C, Eitner S, Godoy JR, Lillig CH. Characterization of the human monothiol glutaredoxin 3 (PICOT) as iron–sulfur protein. Biochem. Biophys. Res. Commun. 394(2), 372–376 (2010).
  Medline CASGoogle Scholar
• 88. Frey AG, Palenchar DJ, Wildemann JD, Philpott CC. A glutaredoxin·BolA complex serves as an iron–sulfur cluster chaperone for the cytosolic cluster assembly machinery. J. Biol. Chem. 291(43), 22344–22356 (2016).
  Medline CASGoogle Scholar
• 89. Fernandes AP, Fladvad M, Berndt C et al. A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase. J. Biol. Chem. 280(26), 24544–24552 (2005).
  Medline CASGoogle Scholar
• 90. Ojeda L, Keller G, Muhlenhoff U, Rutherford JC, Lill R, Winge DR. Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae. J. Biol. Chem. 281(26), 17661–17669 (2006).
  Medline CASGoogle Scholar
• 91. Ye H, Jeong SY, Ghosh MC et al. Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts. J. Clin. Invest. 120(5), 1749–1761 (2010).
  Medline CASGoogle Scholar
• 92. Feng WX, Zhuo XW, Liu ZM et al. Case report: a variant non-ketotic hyperglycinemia with GLRX5 mutations: manifestation of deficiency of activities of the respiratory chain enzymes. Front. Genet. 12, 605778 (2021).
  Medline CASGoogle Scholar
• 93. Wingert RA, Galloway JL, Barut B et al. Deficiency of glutaredoxin 5 reveals Fe–S clusters are required for vertebrate haem synthesis. Nature 436(7053), 1035–1039 (2005).
  Medline CASGoogle Scholar
• 94. Tong WH, Rouault TA. Metabolic regulation of citrate and iron by aconitases: role of iron–sulfur cluster biogenesis. Biometals 20(3), 549–564 (2007).
  Medline CASGoogle Scholar
• 95. Fuss JO, Tsai CL, Ishida JP, Tainer JA. Emerging critical roles of Fe–S clusters in DNA replication and repair. Biochim. Biophys. Acta Mol. Cell Res. 1853(6), 1253–1271 (2015).
  CASGoogle Scholar
• 96. McCarthy EL, Booker SJ. Destruction and reformation of an iron–sulfur cluster during catalysis by lipoyl synthase. Science 358(6361), 373–377 (2017).
  Medline CASGoogle Scholar
• 97. Ugulava NB, Gibney BR, Jarrett JT. Biotin synthase contains two distinct iron–sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron–sulfur cluster interconversions. Biochemistry 40(28), 8343–8351 (2001).
  Medline CASGoogle Scholar
• 98. Dern RJ, McCurdy PR, Yoshida A. A new structural variant of glucose-6-phosphate dehydrogenase with a high production rate (G6PD Hektoen). J. Lab. Clin. Med. 73(2), 283–290 (1969).
  Medline CASGoogle Scholar
• 99. Su J, Zheng N, Li Z et al. Association of GCK gene DNA methylation with the risk of clopidogrel resistance in acute coronary syndrome patients. J. Clin. Lab. Anal. 34(2), e23040 (2020).
  Medline CASGoogle Scholar
• 100. Hagihara K, Kazui M, Kurihara A, Ikeda T, Izumi T. Glutaredoxin is involved in the formation of the pharmacologically active metabolite of clopidogrel from its GSH conjugate. Drug Metab. Dispos. 40(9), 1854–1859 (2012).
  Medline CASGoogle Scholar