This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
Carson PE, Flanagan CL, Ickes C, Alving AS. Enzymatic deficiency in primaquine-sensitive erythrocytes. Science. 1956; 124(3220):484–5.CarsonPEFlanaganCLIckesCAlvingASEnzymatic deficiency in primaquine-sensitive erythrocytes19561243220484510.1126/science.124.3220.484.bSearch in Google Scholar
Efferth T, Fabry U, Glatte P, Osieka R. Increased induction of apoptosis in mononuclear cells of a glucose-6-phosphate dehydrogenase deficient patient. J Mol Med (Berl). 1995; 73:47–9.EfferthTFabryUGlattePOsiekaRIncreased induction of apoptosis in mononuclear cells of a glucose-6-phosphate dehydrogenase deficient patient19957347910.1007/BF00203619Search in Google Scholar
Zhang J, Cao M, Yang W, Sun F, Xu C, Yin L, et al. Inhibition of glucose-6-phosphate dehydrogenase could enhance 1, 4-benzoquinone-induced oxidative damage in K562 cells. Oxid Med Cell Longev. 2016; 2016:3912515. doi: 10.1155/2016/3912515ZhangJCaoMYangWSunFXuCYinLInhibition of glucose-6-phosphate dehydrogenase could enhance 1, 4-benzoquinone-induced oxidative damage in K562 cells20162016391251510.1155/2016/3912515Open DOISearch in Google Scholar
McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969; 244:6049–55.McCordJMFridovichISuperoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)196924460495510.1016/S0021-9258(18)63504-5Search in Google Scholar
Cappellini MD, Fiorelli G. Glucose-6-phosphate dehydrogenase deficiency. Lancet. 2008; 371(9606):64–74.CappelliniMDFiorelliGGlucose-6-phosphate dehydrogenase deficiency20083719606647410.1016/S0140-6736(08)60073-2Search in Google Scholar
Beutler E. Glucose-6-phosphate dehydrogenase deficiency: a historical perspective. Blood. 2008; 111:16–24.BeutlerEGlucose-6-phosphate dehydrogenase deficiency: a historical perspective2008111162410.1182/blood-2007-04-07741218156501Search in Google Scholar
Valencia SH, Ocampo ID, Arce-Plata MI, Recht J, Arévalo-Herrera M. Glucose-6-phosphate dehydrogenase deficiency prevalence and genetic variants in malaria endemic areas of Colombia. Malar J. 2016; 15:291. doi: 10.1186/s12936-016-1343-1ValenciaSHOcampoIDArce-PlataMIRechtJArévalo-HerreraMGlucose-6-phosphate dehydrogenase deficiency prevalence and genetic variants in malaria endemic areas of Colombia20161529110.1186/s12936-016-1343-1488087927225440Open DOISearch in Google Scholar
WHO Scientific Group on the Standardization of Procedures for the Study of Glucose-6-Phosphate Dehydrogenase and World Health Organization. Standardization of procedures for the study of glucose-6-phosphate dehydrogenase: report of a WHO Scientific Group [meeting held in Geneva from 5 to 10 December 1966] [Internet] Geneva: World Health Organization; 1967 [cited 2020 Mar 24]. Available from: https://apps.who.int/iris/handle/10665/40660WHO Scientific Group on the Standardization of Procedures for the Study of Glucose-6-Phosphate Dehydrogenase and World Health OrganizationGenevaWorld Health Organization1967[cited 2020 Mar 24]. Available from: https://apps.who.int/iris/handle/10665/40660Search in Google Scholar
Beutler E, Yoshida A. Genetic variation of glucose-6-phosphate dehydrogenase: a catalog and future prospects. Medicine (Baltimore). 1988; 67:311–34.BeutlerEYoshidaAGenetic variation of glucose-6-phosphate dehydrogenase: a catalog and future prospects1988673113410.1097/00005792-198809000-000033045479Search in Google Scholar
Singh H. Glucose-6-phosphate dehydrogenase deficiency: a preventable cause of mental retardation. Br Med J (Clin Res Ed). 1986; 292(6517):397–8.SinghHGlucose-6-phosphate dehydrogenase deficiency: a preventable cause of mental retardation19862926517397810.1136/bmj.292.6517.39713393653080188Search in Google Scholar
Hon A, Balakrishnan S, Ahmad Z. Hyperbilirubinemia and erythocytic glucose 6 phosphate dehydrogenase deficiency in Malaysian children. Med J Malaysia. 1989; 44:30–4.HonABalakrishnanSAhmadZHyperbilirubinemia and erythocytic glucose 6 phosphate dehydrogenase deficiency in Malaysian children198944304Search in Google Scholar
Sulaiman AM, Saghir SAM, Al-Hassan FM, Yusoff NM, Zaki A-HA. Molecular characterization of glucose-6-phosphate dehydrogenase deficiency in a university community in Malaysia. Trop J Pharm Res. 2013; 12:363–7.SulaimanAMSaghirSAMAl-HassanFMYusoffNMZakiA-HAMolecular characterization of glucose-6-phosphate dehydrogenase deficiency in a university community in Malaysia201312363710.4314/tjpr.v12i3.14Search in Google Scholar
Ainoon O, Yu Y, Muhriz AA, Boo N, Cheong S, Hamidah N. Glucose-6-phosphate dehydrogenase (G6PD) variants in Malaysian Malays. Hum Mutat. 2003; 21:1. doi: 10.1002/humu.9103AinoonOYuYMuhrizAABooNCheongSHamidahNGlucose-6-phosphate dehydrogenase (G6PD) variants in Malaysian Malays200321110.1002/humu.910312497642Open DOISearch in Google Scholar
Yusoff NM, Shirakawa T, Nishiyama K, Ee CK, Isa MN, Matsuo M. G6PD Viangchan and G6PD Mediterranean are the main variants in G6PD deficiency in the Malay population of Malaysia. Southeast Asian J Trop Med Public Health. 2004; 34(Suppl. 3):135–7.YusoffNMShirakawaTNishiyamaKEeCKIsaMNMatsuoMG6PD Viangchan and G6PD Mediterranean are the main variants in G6PD deficiency in the Malay population of Malaysia200434Suppl. 31357Search in Google Scholar
Poon M-C, Hall K, Scott CW, Prehal JT. G6PD Viangchan: a new glucose 6-phosphate dehydrogenase variant from Laos. Hum Genet. 1988; 78:98–9.PoonM-CHallKScottCWPrehalJTG6PD Viangchan: a new glucose 6-phosphate dehydrogenase variant from Laos19887898910.1007/BF002912463338798Search in Google Scholar
World Health Organization Working Group. Glucose-6-phosphate dehydrogenase deficiency. WHO Bulletin OMS. 1989; 67:601–11. Available from: https://apps.who.int/iris/handle/10665/47019World Health Organization Working GroupGlucose-6-phosphate dehydrogenase deficiency19896760111Available from: https://apps.who.int/iris/handle/10665/47019Search in Google Scholar
Gómez-Manzo S, Terrón-Hernández J, De la Mora-De la Mora I, González-Valdez A, Marcial-Quino J, García-Torres I, et al. The stability of G6PD is affected by mutations with different clinical phenotypes. Int J Mol Sci. 2014; 15:21179–201.Gómez-ManzoSTerrón-HernándezJDe la Mora-De la MoraIGonzález-ValdezAMarcial-QuinoJGarcía-TorresIThe stability of G6PD is affected by mutations with different clinical phenotypes2014152117920110.3390/ijms151121179426421925407525Search in Google Scholar
Roos D, van Zwieten R, Wijnen JT, Gómez-Gallego F, de Boer M, Stevens D, et al. Molecular basis and enzymatic properties of glucose 6-phosphate dehydrogenase Volendam, leading to chronic nonspherocytic anemia, granulocyte dysfunction, and increased susceptibility to infections. Blood. 1999; 94:2955–62.RoosDvan ZwietenRWijnenJTGómez-GallegoFde BoerMStevensDMolecular basis and enzymatic properties of glucose 6-phosphate dehydrogenase Volendam, leading to chronic nonspherocytic anemia, granulocyte dysfunction, and increased susceptibility to infections199994295562Search in Google Scholar
Huang Y, Choi MY, Au SWN, Au DMY, Lam VMS, Engel PC. Purification and detailed study of two clinically different human glucose 6-phosphate dehydrogenase variants, G6PDPlymouth and G6PDMahidol: evidence for defective protein folding as the basis of disease. Mol Genet Metabol. 2008; 93:44–53.HuangYChoiMYAuSWNAuDMYLamVMSEngelPCPurification and detailed study of two clinically different human glucose 6-phosphate dehydrogenase variants, G6PDPlymouth and G6PDMahidol: evidence for defective protein folding as the basis of disease200893445310.1016/j.ymgme.2007.08.12217959407Search in Google Scholar
Wang X-T, Lam VM, Engel PC. Functional properties of two mutants of human glucose 6-phosphate dehydrogenase, R393G and R393H, corresponding to the clinical variants G6PD Wisconsin and Nashville. Biochim Biophys Acta. 2006; 1762:767–74.WangX-TLamVMEngelPCFunctional properties of two mutants of human glucose 6-phosphate dehydrogenase, R393G and R393H, corresponding to the clinical variants G6PD Wisconsin and Nashville200617627677410.1016/j.bbadis.2006.06.01416934959Search in Google Scholar
Wang X-T, Engel PC. Clinical mutants of human glucose 6-phosphate dehydrogenase: impairment of NADP+ binding affects both folding and stability. Biochim Biophys Acta. 2009; 1792:804–9.WangX-TEngelPCClinical mutants of human glucose 6-phosphate dehydrogenase: impairment of NADP+ binding affects both folding and stability20091792804910.1016/j.bbadis.2009.05.00319465117Search in Google Scholar
Boonyuen U, Chamchoy K, Swangsri T, Saralamba N, Day NP, Imwong M. Detailed functional analysis of two clinical glucose-6-phosphate dehydrogenase (G6PD) variants, G6PDViangchan and G6PDViangchan+Mahidol: decreased stability and catalytic efficiency contribute to the clinical phenotype. Mol Genet Metabol. 2016; 118:84–91.BoonyuenUChamchoyKSwangsriTSaralambaNDayNPImwongMDetailed functional analysis of two clinical glucose-6-phosphate dehydrogenase (G6PD) variants, G6PDViangchan and G6PDViangchan+Mahidol: decreased stability and catalytic efficiency contribute to the clinical phenotype2016118849110.1016/j.ymgme.2016.03.008489429627053284Search in Google Scholar
Gómez-Manzo S, Marcial-Quino J, Vanoye-Carlo A, Serrano-Posada H, González-Valdez A, Martínez-Rosas V, et al. Functional and biochemical characterization of three recombinant human glucose-6-phosphate dehydrogenase mutants: Zacatecas, Vanua-Lava and Viangchan. Int J Mol Sci. 2016; 17:787. doi: 10.3390/ijms17050787Gómez-ManzoSMarcial-QuinoJVanoye-CarloASerrano-PosadaHGonzález-ValdezAMartínez-RosasVFunctional and biochemical characterization of three recombinant human glucose-6-phosphate dehydrogenase mutants: Zacatecas, Vanua-Lava and Viangchan20161778710.3390/ijms17050787488160327213370Open DOISearch in Google Scholar
Boonyuen U, Chamchoy K, Swangsri T, Junkree T, Day NPJ, White NJ, Imwong M. A trade off between catalytic activity and protein stability determines the clinical manifestations of glucose-6-phosphate dehydrogenase (G6PD) deficiency. Int J Biol Macromol. 2017; 104(Pt A):145–56.BoonyuenUChamchoyKSwangsriTJunkreeTDayNPJWhiteNJImwongMA trade off between catalytic activity and protein stability determines the clinical manifestations of glucose-6-phosphate dehydrogenase (G6PD) deficiency2017104Pt A1455610.1016/j.ijbiomac.2017.06.002562599628583873Search in Google Scholar
Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera—a visualization system for exploratory research and analysis. J Comput Chem. 2004; 25:1605–12.PettersenEFGoddardTDHuangCCCouchGSGreenblattDMMengECFerrinTEUCSF Chimera—a visualization system for exploratory research and analysis20042516051210.1002/jcc.2008415264254Search in Google Scholar
Scouras AD, Daggett V. The Dynameomics rotamer library: amino acid side chain conformations and dynamics from comprehensive molecular dynamics simulations in water. Protein Sci. 2011; 20:341–52.ScourasADDaggettVThe Dynameomics rotamer library: amino acid side chain conformations and dynamics from comprehensive molecular dynamics simulations in water2011203415210.1002/pro.565304841921280126Search in Google Scholar
Hess B, Kutzner C, van der Spoel D, Lindahl E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput. 2008; 4(3):435–47.HessBKutznerCvan der SpoelDLindahlEGROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation2008434354710.1021/ct700301q26620784Search in Google Scholar
Rizvi SM, Shakil S, Haneef M. A simple click by click protocol to perform docking: AutoDock 4.2 made easy for non-bioinformaticians. EXCLI J. 2013; 12:831–57.RizviSMShakilSHaneefMA simple click by click protocol to perform docking: AutoDock 4.2 made easy for non-bioinformaticians20131283157Search in Google Scholar
Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ. Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase. Acta Crystallogr D Biol Crystallogr. 2005; 61:495–504.KotakaMGoverSVandeputte-RuttenLAuSWLamVMAdamsMJStructural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase20056149550410.1107/S090744490500235015858258Search in Google Scholar
Laskowski RA, Swindells MB. LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J Chem Inf Model. 2011; 51:2778–86.LaskowskiRASwindellsMBLigPlot+: multiple ligand-protein interaction diagrams for drug discovery20115127788610.1021/ci200227u21919503Search in Google Scholar
Rao ST, Rossmann MG. Comparison of super-secondary structures in proteins. J Mol Biol. 1973; 76:241–56.RaoSTRossmannMGComparison of super-secondary structures in proteins1973762415610.1142/9789814513357_0013Search in Google Scholar
Hanukoglu I. Proteopedia: Rossmann fold: a beta-alpha-beta fold at dinucleotide binding sites. Biochem Mol Biol Educ. 2015; 43:206–9.HanukogluIProteopedia: Rossmann fold: a beta-alpha-beta fold at dinucleotide binding sites201543206910.1002/bmb.2084925704928Search in Google Scholar
Gómez-Manzo S, Terrón-Hernández J, de la Mora-de la Mora I, García-Torres I, López-Velázquez G, Reyes-Vivas H, Oria-Hernández J. Cloning, expression, purification and characterization of His-Tagged human glucose-6-phosphate dehydrogenase: a simplified method for protein yield. Protein J. 2013; 32:585–92.Gómez-ManzoSTerrón-HernándezJde la Mora-de la MoraIGarcía-TorresILópez-VelázquezGReyes-VivasHOria-HernándezJCloning, expression, purification and characterization of His-Tagged human glucose-6-phosphate dehydrogenase: a simplified method for protein yield2013325859210.1007/s10930-013-9518-x24146346Search in Google Scholar
Minucci A, Giardina B, Zuppi C, Capoluongo E. Glucose-6-phosphate dehydrogenase laboratory assay: how, when, and why? IUBMB Life. 2009; 61:27–34.MinucciAGiardinaBZuppiCCapoluongoEGlucose-6-phosphate dehydrogenase laboratory assay: how, when, and why?200961273410.1002/iub.13718942156Search in Google Scholar
von Seidlein L, Auburn S, Espino F, Shanks D, Cheng Q, McCarthy J, et al. Review of key knowledge gaps in glucose-6-phosphate dehydrogenase deficiency detection with regard to the safe clinical deployment of 8-aminoquinoline treatment regimens: a workshop report. Malar J. 2013; 12:112. doi: 10.1186/1475-2875-12-112von SeidleinLAuburnSEspinoFShanksDChengQMcCarthyJReview of key knowledge gaps in glucose-6-phosphate dehydrogenase deficiency detection with regard to the safe clinical deployment of 8-aminoquinoline treatment regimens: a workshop report20131211210.1186/1475-2875-12-112361683723537118Open DOISearch in Google Scholar
Blacker TS, Duchen MR. Investigating mitochondrial redox state using NADH and NADPH autofluorescence. Free Radic Biol Med. 2016; 100:53–65.BlackerTSDuchenMRInvestigating mitochondrial redox state using NADH and NADPH autofluorescence2016100536510.1016/j.freeradbiomed.2016.08.010514580327519271Search in Google Scholar