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Volumn 195, Issue , 2016, Pages 39-49

A novel aldo-keto reductase from Jatropha curcas L. (JcAKR) plays a crucial role in the detoxification of methylglyoxal, a potent electrophile

Author keywords

Abiotic stress tolerance; Aldo keto reductase (AKR); Jatropha curcas; JcAKR; Methylglyoxal (MG); Reactive carbonyls (RCs)

Indexed keywords

ALDEHYDE; ALDEHYDE REDUCTASE; CARBONYL REDUCTASE; KETONE; MACROGOL DERIVATIVE; METHYLGLYOXAL; PLANT PROTEIN; RECOMBINANT PROTEIN; SODIUM CHLORIDE;

EID: 84960890332     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jplph.2016.03.005     Document Type: Article
Times cited : (14)

References (47)
  • 1
    • 0034875879 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae aldose reductase is implied in the metabolism of methylglyoxal in response to stress conditions
    • Aguilera J., Prieto J. The Saccharomyces cerevisiae aldose reductase is implied in the metabolism of methylglyoxal in response to stress conditions. Curr. Genet. 2001, 39:273-283.
    • (2001) Curr. Genet. , vol.39 , pp. 273-283
    • Aguilera, J.1    Prieto, J.2
  • 2
    • 38349022711 scopus 로고    scopus 로고
    • Disruption of aldo-keto reductase genes leads to elevated markers of oxidative stress and inositol auxotrophy in Saccharomyces cerevisiae
    • Chang Q., Petrash J.M. Disruption of aldo-keto reductase genes leads to elevated markers of oxidative stress and inositol auxotrophy in Saccharomyces cerevisiae. BBA Mol. Cell Res. 2008, 1783:237-245.
    • (2008) BBA Mol. Cell Res. , vol.1783 , pp. 237-245
    • Chang, Q.1    Petrash, J.M.2
  • 3
    • 84894285358 scopus 로고    scopus 로고
    • Phenotyping shows improved physiological traits and seed yield of transgenic wheat plants expressing the alfalfa aldose reductase under permanent drought stress
    • Fehér-Juhász E., Majer P., Sass L., Lantos C., Csiszár J., Turóczy Z., Mihály R., Mai A., Horváth G.V., Vass I. Phenotyping shows improved physiological traits and seed yield of transgenic wheat plants expressing the alfalfa aldose reductase under permanent drought stress. Acta Physiol. Plant 2014, 36:663-673.
    • (2014) Acta Physiol. Plant , vol.36 , pp. 663-673
    • Fehér-Juhász, E.1    Majer, P.2    Sass, L.3    Lantos, C.4    Csiszár, J.5    Turóczy, Z.6    Mihály, R.7    Mai, A.8    Horváth, G.V.9    Vass, I.10
  • 4
    • 0036311164 scopus 로고    scopus 로고
    • Cloning and expression of two novel aldo-keto reductases from Digitalis purpurea leaves
    • Gavidia I., Pérez-Bermúdez P., Seitz H.U. Cloning and expression of two novel aldo-keto reductases from Digitalis purpurea leaves. Eur. J. Biochem. 2002, 269:2842-2850.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2842-2850
    • Gavidia, I.1    Pérez-Bermúdez, P.2    Seitz, H.U.3
  • 5
    • 0037458207 scopus 로고    scopus 로고
    • A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity
    • Grant A.W., Steel G., Waugh H., Ellis E.M. A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity. FEMS Microbiol. Lett. 2003, 218:93-99.
    • (2003) FEMS Microbiol. Lett. , vol.218 , pp. 93-99
    • Grant, A.W.1    Steel, G.2    Waugh, H.3    Ellis, E.M.4
  • 6
    • 16544384294 scopus 로고    scopus 로고
    • YBP1 and its homologue YBP2/YBH1 influence oxidative stress tolerance by non-identical mechanisms in Saccharomyces cerevisiae
    • Gulshan K., Rovinsky S.A., Moye-Rowley W.S. YBP1 and its homologue YBP2/YBH1 influence oxidative stress tolerance by non-identical mechanisms in Saccharomyces cerevisiae. Eukaryot. Cell 2004, 3:318-330.
    • (2004) Eukaryot. Cell , vol.3 , pp. 318-330
    • Gulshan, K.1    Rovinsky, S.A.2    Moye-Rowley, W.S.3
  • 8
    • 70349690428 scopus 로고    scopus 로고
    • Purification of glyoxalase I from onion bulbs and molecular cloning of its cDNA
    • Hossain M.A., Fujita M. Purification of glyoxalase I from onion bulbs and molecular cloning of its cDNA. Biosci. Biotechnol. Biochem. 2009, 73:2007-2013.
    • (2009) Biosci. Biotechnol. Biochem. , vol.73 , pp. 2007-2013
    • Hossain, M.A.1    Fujita, M.2
  • 10
    • 78651093186 scopus 로고    scopus 로고
    • YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals
    • Jarboe L.R. YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals. Appl. Microbiol. Biotechnol. 2011, 89:249-257.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , pp. 249-257
    • Jarboe, L.R.1
  • 11
    • 0030821699 scopus 로고    scopus 로고
    • Comparative anatomy of the aldo-keto reductase superfamily
    • Jez J., Bennett M., Schlegel B., Lewis M., Penning T. Comparative anatomy of the aldo-keto reductase superfamily. Biochem. J. 1997, 326:625-636.
    • (1997) Biochem. J. , vol.326 , pp. 625-636
    • Jez, J.1    Bennett, M.2    Schlegel, B.3    Lewis, M.4    Penning, T.5
  • 12
    • 0032703938 scopus 로고    scopus 로고
    • Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications
    • Kalapos M.P. Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications. Toxicol. Lett. 1999, 110:145-175.
    • (1999) Toxicol. Lett. , vol.110 , pp. 145-175
    • Kalapos, M.P.1
  • 13
    • 84901835317 scopus 로고    scopus 로고
    • Characterization of an uncharacterized aldo-keto reductase gene from peach and its role in abiotic stress tolerance
    • Kanayama Y., Mizutani R., Yaguchi S., Hojo A., Ikeda H., Nishiyama M., Kanahama K. Characterization of an uncharacterized aldo-keto reductase gene from peach and its role in abiotic stress tolerance. Phytochemistry 2014, 104:30-36.
    • (2014) Phytochemistry , vol.104 , pp. 30-36
    • Kanayama, Y.1    Mizutani, R.2    Yaguchi, S.3    Hojo, A.4    Ikeda, H.5    Nishiyama, M.6    Kanahama, K.7
  • 14
    • 84902655231 scopus 로고    scopus 로고
    • Glyoxalase and methylglyoxal as biomarkers for plant stress tolerance
    • Kaur C., Singla-Pareek S.L., Sopory S.K. Glyoxalase and methylglyoxal as biomarkers for plant stress tolerance. Crit. Rev. Plant Sci. 2014, 33:429-456.
    • (2014) Crit. Rev. Plant Sci. , vol.33 , pp. 429-456
    • Kaur, C.1    Singla-Pareek, S.L.2    Sopory, S.K.3
  • 15
    • 23644445048 scopus 로고    scopus 로고
    • Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases
    • Ko J., Kim I., Yoo S., Min B., Kim K., Park C. Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases. J. Bacteriol. 2005, 187:5782-5789.
    • (2005) J. Bacteriol. , vol.187 , pp. 5782-5789
    • Ko, J.1    Kim, I.2    Yoo, S.3    Min, B.4    Kim, K.5    Park, C.6
  • 16
    • 0034923337 scopus 로고    scopus 로고
    • Disparity Index: a simple statistic to measure and test the homogeneity of substitution patterns between molecular sequences
    • Kumar S., Gadagkar S.R. Disparity Index: a simple statistic to measure and test the homogeneity of substitution patterns between molecular sequences. Genetics 2001, 158:1321-1327.
    • (2001) Genetics , vol.158 , pp. 1321-1327
    • Kumar, S.1    Gadagkar, S.R.2
  • 17
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy R., Bowie J.U., Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature 1992, 356:83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 18
    • 84896722092 scopus 로고    scopus 로고
    • JcLEA, a novel LEA-like protein from Jatropha curcas, confers a high level of tolerance to dehydration and salinity in Arabidopsis thaliana
    • Liang J., Zhou M., Zhou X., Jin Y., Xu M., Lin J. JcLEA, a novel LEA-like protein from Jatropha curcas, confers a high level of tolerance to dehydration and salinity in Arabidopsis thaliana. PLoS One 2013, 8:12. (e83056).
    • (2013) PLoS One , vol.8 , pp. 12
    • Liang, J.1    Zhou, M.2    Zhou, X.3    Jin, Y.4    Xu, M.5    Lin, J.6
  • 19
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2-DDCt method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2-DDCt method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 20
    • 84865987453 scopus 로고    scopus 로고
    • Reactive carbonyl species: their production from lipid peroxides, action in environmental stress, and the detoxification mechanism
    • Mano J.I. Reactive carbonyl species: their production from lipid peroxides, action in environmental stress, and the detoxification mechanism. Plant Physiol. Bioch. 2012, 59:90-97.
    • (2012) Plant Physiol. Bioch. , vol.59 , pp. 90-97
    • Mano, J.I.1
  • 21
    • 0035876322 scopus 로고    scopus 로고
    • In situ analysisof methylglyoxal metabolism in Saccharomyces cerevisiae
    • Martins A.M., Cordeiro C.A., Ponces Freire A.M. In situ analysisof methylglyoxal metabolism in Saccharomyces cerevisiae. FEBS Lett. 2001, 499:41-44.
    • (2001) FEBS Lett. , vol.499 , pp. 41-44
    • Martins, A.M.1    Cordeiro, C.A.2    Ponces Freire, A.M.3
  • 24
    • 84891953471 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of metallothionein type 2a gene from Jatropha curcas L., a promising biofuel plant
    • Mudalkar S., Golla R., Sengupta D., Ghatty S., Reddy A.R. Molecular cloning and characterisation of metallothionein type 2a gene from Jatropha curcas L., a promising biofuel plant. Mol. Biol. Rep. 2014, 41:113-124.
    • (2014) Mol. Biol. Rep. , vol.41 , pp. 113-124
    • Mudalkar, S.1    Golla, R.2    Sengupta, D.3    Ghatty, S.4    Reddy, A.R.5
  • 25
    • 84888384944 scopus 로고    scopus 로고
    • De novo transcriptome analysis of an imminent biofuel crop: Camelina sativa L. using Illumina GAIIX sequencing platform and identification of SSR markers
    • Mudalkar S., Golla R., Ghatty S., Reddy A.R. De novo transcriptome analysis of an imminent biofuel crop: Camelina sativa L. using Illumina GAIIX sequencing platform and identification of SSR markers. Plant Mol. Biol. 2014, 84:159-171.
    • (2014) Plant Mol. Biol. , vol.84 , pp. 159-171
    • Mudalkar, S.1    Golla, R.2    Ghatty, S.3    Reddy, A.R.4
  • 26
    • 77954044170 scopus 로고    scopus 로고
    • Metabolic engineering of glyoxalase pathway for enhancing stress tolerance in plants
    • Mustafiz A., Sahoo K.K., Singla-Pareek S.L., Sopory S.K. Metabolic engineering of glyoxalase pathway for enhancing stress tolerance in plants. Methods Mol. Biol. 2010, 639:95-118.
    • (2010) Methods Mol. Biol. , vol.639 , pp. 95-118
    • Mustafiz, A.1    Sahoo, K.K.2    Singla-Pareek, S.L.3    Sopory, S.K.4
  • 27
    • 84859634390 scopus 로고    scopus 로고
    • Cloning and characterization of AKR4C14 a rice aldo-keto reductase, from Thai Jasmine rice
    • Narawongsanont R., Kabinpong S., Auiyawong B., Tantitadapitak C. Cloning and characterization of AKR4C14 a rice aldo-keto reductase, from Thai Jasmine rice. Protein J. 2012, 31:35-42.
    • (2012) Protein J. , vol.31 , pp. 35-42
    • Narawongsanont, R.1    Kabinpong, S.2    Auiyawong, B.3    Tantitadapitak, C.4
  • 28
    • 0034541782 scopus 로고    scopus 로고
    • A novel aldose/aldehyde reductase protects transgenic plants against lipid peroxidation under chemical and drought stresses
    • Oberschall A., Deak M., Török K., Sass L., Vass I., Kovács I., Fehér A., Dudits D., Horváth G.V. A novel aldose/aldehyde reductase protects transgenic plants against lipid peroxidation under chemical and drought stresses. Plant J. 2000, 24:437-446.
    • (2000) Plant J. , vol.24 , pp. 437-446
    • Oberschall, A.1    Deak, M.2    Török, K.3    Sass, L.4    Vass, I.5    Kovács, I.6    Fehér, A.7    Dudits, D.8    Horváth, G.V.9
  • 29
    • 80053268689 scopus 로고    scopus 로고
    • Identification and expression analysis of two small heat shock protein cDNAs from developing seeds of biodiesel feedstock plant Jatropha curcas
    • Omar S.A., Fu Q.-T., Chen M.-S., Wang G.-J., Song S.-Q., Elsheery N.I., Xu Z.F. Identification and expression analysis of two small heat shock protein cDNAs from developing seeds of biodiesel feedstock plant Jatropha curcas. Plant Sci. 2011, 181:632-637.
    • (2011) Plant Sci. , vol.181 , pp. 632-637
    • Omar, S.A.1    Fu, Q.-T.2    Chen, M.-S.3    Wang, G.-J.4    Song, S.-Q.5    Elsheery, N.I.6    Xu, Z.F.7
  • 30
    • 43149093576 scopus 로고    scopus 로고
    • Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation derived aldehydes
    • Pérez J.M., Arenas F.A., Pradenas G.A., Sandoval J.M., Vásquez C.C. Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation derived aldehydes. J. Biol. Chem. 2008, 283:7346-7353.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7346-7353
    • Pérez, J.M.1    Arenas, F.A.2    Pradenas, G.A.3    Sandoval, J.M.4    Vásquez, C.C.5
  • 33
    • 9644276693 scopus 로고    scopus 로고
    • Drought induced responses of photosynthesis and antioxidant metabolism in higher plants
    • Reddy A.R., Chaitanya K.V., Vivekanandan M. Drought induced responses of photosynthesis and antioxidant metabolism in higher plants. J. Plant Physiol. 2004, 161:1189-1202.
    • (2004) J. Plant Physiol. , vol.161 , pp. 1189-1202
    • Reddy, A.R.1    Chaitanya, K.V.2    Vivekanandan, M.3
  • 34
    • 33845499750 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase: a new member of the aldo-keto reductase enzyme superfamily from higher plants
    • Rosenthal C., Mueller U., Panjikar S., Sun L., Ruppert M., Zhao Y., Stöckigt J. Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase: a new member of the aldo-keto reductase enzyme superfamily from higher plants. Acta Crystallogr. Sect. F: Struct. Biol. Cryst. Commun. 2006, 62:1286-1289.
    • (2006) Acta Crystallogr. Sect. F: Struct. Biol. Cryst. Commun. , vol.62 , pp. 1286-1289
    • Rosenthal, C.1    Mueller, U.2    Panjikar, S.3    Sun, L.4    Ruppert, M.5    Zhao, Y.6    Stöckigt, J.7
  • 35
    • 84886702989 scopus 로고    scopus 로고
    • Functional analysis of the AKR4C subfamily of Arabidopsis thaliana: model structures, substrate specificity, acrolein toxicity, and responses to light and [CO2]
    • Saito R., Shimakawa G., Nishi A., Iwamoto T., Sakamoto K., Yamamoto H., Amako K., Makino A., Miyake C. Functional analysis of the AKR4C subfamily of Arabidopsis thaliana: model structures, substrate specificity, acrolein toxicity, and responses to light and [CO2]. Biosci. Biotechnol. Biochem. 2013, 77:2038-2045.
    • (2013) Biosci. Biotechnol. Biochem. , vol.77 , pp. 2038-2045
    • Saito, R.1    Shimakawa, G.2    Nishi, A.3    Iwamoto, T.4    Sakamoto, K.5    Yamamoto, H.6    Amako, K.7    Makino, A.8    Miyake, C.9
  • 36
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 37
    • 84866900523 scopus 로고    scopus 로고
    • Detoxification potential and expression analysis of eutypine reducing aldehyde reductase (VrALR) during progressive drought and recovery in Vigna radiata (L.) Wilczek roots
    • Sengupta D., Mudalkar S., Reddy A.R. Detoxification potential and expression analysis of eutypine reducing aldehyde reductase (VrALR) during progressive drought and recovery in Vigna radiata (L.) Wilczek roots. Planta 2012, 236:1339-1349.
    • (2012) Planta , vol.236 , pp. 1339-1349
    • Sengupta, D.1    Mudalkar, S.2    Reddy, A.R.3
  • 38
    • 84964228756 scopus 로고    scopus 로고
    • Plant aldo-keto reductases (AKRs) as multi-tasking soldiers involved in diverse plant metabolic processes and stress defense: a structure-function update
    • Sengupta D., Naik D., Reddy A.R. Plant aldo-keto reductases (AKRs) as multi-tasking soldiers involved in diverse plant metabolic processes and stress defense: a structure-function update. J. Plant Physiol. 2015, 179:40-55.
    • (2015) J. Plant Physiol. , vol.179 , pp. 40-55
    • Sengupta, D.1    Naik, D.2    Reddy, A.R.3
  • 39
    • 68949211011 scopus 로고    scopus 로고
    • Characterization of two novel aldo-keto reductases from Arabidopsis: expression patterns, broad substrate specificity, and an open active-site structure suggest a role in toxicant metabolism following stress
    • Simpson P.J., Tantitadapitak C., Reed A.M., Mather O.C., Bunce C.M., White S.A., Ride J.P. Characterization of two novel aldo-keto reductases from Arabidopsis: expression patterns, broad substrate specificity, and an open active-site structure suggest a role in toxicant metabolism following stress. J. Mol. Biol. 2009, 392:465-480.
    • (2009) J. Mol. Biol. , vol.392 , pp. 465-480
    • Simpson, P.J.1    Tantitadapitak, C.2    Reed, A.M.3    Mather, O.C.4    Bunce, C.M.5    White, S.A.6    Ride, J.P.7
  • 41
    • 79952038830 scopus 로고    scopus 로고
    • Overproduction of a rice aldo-keto reductase increases oxidative and heat stress tolerance by malondialdehyde and methylglyoxal detoxification
    • Turóczy Z., Kis P., Török K., Cserháti M., Lendvai Á., Dudits D., Horváth G.V. Overproduction of a rice aldo-keto reductase increases oxidative and heat stress tolerance by malondialdehyde and methylglyoxal detoxification. Plant Mol. Biol. 2011, 75:399-412.
    • (2011) Plant Mol. Biol. , vol.75 , pp. 399-412
    • Turóczy, Z.1    Kis, P.2    Török, K.3    Cserháti, M.4    Lendvai, Á.5    Dudits, D.6    Horváth, G.V.7
  • 42
    • 0026646131 scopus 로고
    • Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications
    • Vander Jagt D., Robinson B., Taylor K., Hunsaker L. Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications. J. Biol. Chem. 1992, 267:4364-4369.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4364-4369
    • Vander Jagt, D.1    Robinson, B.2    Taylor, K.3    Hunsaker, L.4
  • 43
    • 33746207862 scopus 로고    scopus 로고
    • Methylglyoxal detoxification by an aldo-keto reductase in the cyanobacterium Synechococcus sp. PCC 7002
    • Xu D., Liu X., Guo C., Zhao J. Methylglyoxal detoxification by an aldo-keto reductase in the cyanobacterium Synechococcus sp. PCC 7002. Microbiology 2006, 152:2013-2021.
    • (2006) Microbiology , vol.152 , pp. 2013-2021
    • Xu, D.1    Liu, X.2    Guo, C.3    Zhao, J.4
  • 44
    • 25844456887 scopus 로고    scopus 로고
    • Methylglyoxal levels in plants under salinity stress are dependent on glyoxalase I and glutathione
    • Yadav S.K., Singla-Pareek S.L., Ray M., Reddy M.K., Sopory S.K. Methylglyoxal levels in plants under salinity stress are dependent on glyoxalase I and glutathione. Biochem. Bioph. Res. Commun. 2005, 337:61-67.
    • (2005) Biochem. Bioph. Res. Commun. , vol.337 , pp. 61-67
    • Yadav, S.K.1    Singla-Pareek, S.L.2    Ray, M.3    Reddy, M.K.4    Sopory, S.K.5
  • 45
    • 79953221151 scopus 로고    scopus 로고
    • NADPH-dependent reductases involved in the detoxification of reactive carbonyls in plants
    • Yamauchi Y., Hasegawa A., Taninaka A., Mizutani M., Sugimoto Y. NADPH-dependent reductases involved in the detoxification of reactive carbonyls in plants. J. Biol. Chem. 2011, 286:6999-7009.
    • (2011) J. Biol. Chem. , vol.286 , pp. 6999-7009
    • Yamauchi, Y.1    Hasegawa, A.2    Taninaka, A.3    Mizutani, M.4    Sugimoto, Y.5
  • 46
    • 84938420032 scopus 로고    scopus 로고
    • Osmoregulation as a key factor in drought hardening-induced drought tolerance in Jatropha curcas
    • Yang S., Chen K., Wang S., Gong M. Osmoregulation as a key factor in drought hardening-induced drought tolerance in Jatropha curcas. Biol. Plant. 2015, 1-8.
    • (2015) Biol. Plant. , pp. 1-8
    • Yang, S.1    Chen, K.2    Wang, S.3    Gong, M.4
  • 47
    • 84885162016 scopus 로고    scopus 로고
    • Production of acetol from glycerol using engineered E. coli
    • Zhu H., Yi X., Liu Y., Hu H., Wood T.K., Zhang X. Production of acetol from glycerol using engineered E. coli. Bioresour. Technol. 2013, 149:238-243.
    • (2013) Bioresour. Technol. , vol.149 , pp. 238-243
    • Zhu, H.1    Yi, X.2    Liu, Y.3    Hu, H.4    Wood, T.K.5    Zhang, X.6


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