Masum A, Arman M, Ghosh A
PLoS One. 2024; 19(6):e0304039.
PMID: 38865327
PMC: 11168688.
DOI: 10.1371/journal.pone.0304039.
Nguyen R, Stagliano C, Liu A
Curr Opin Chem Biol. 2023; 75:102332.
PMID: 37269676
PMC: 10528533.
DOI: 10.1016/j.cbpa.2023.102332.
Chen A, Adamek R, Dick B, Credille C, Morrison C, Cohen S
Chem Rev. 2018; 119(2):1323-1455.
PMID: 30192523
PMC: 6405328.
DOI: 10.1021/acs.chemrev.8b00201.
Kaur C, Sharma S, Hasan M, Pareek A, Singla-Pareek S, Sopory S
Int J Mol Sci. 2017; 18(4).
PMID: 28358304
PMC: 5412262.
DOI: 10.3390/ijms18040250.
Nigro C, Leone A, Raciti G, Longo M, Mirra P, Formisano P
Int J Mol Sci. 2017; 18(1).
PMID: 28106778
PMC: 5297820.
DOI: 10.3390/ijms18010188.
Genome-wide analysis and expression profiling of glyoxalase gene families in soybean (Glycine max) indicate their development and abiotic stress specific response.
Ghosh A, Islam T
BMC Plant Biol. 2016; 16:87.
PMID: 27083416
PMC: 4833937.
DOI: 10.1186/s12870-016-0773-9.
Structure of the novel monomeric glyoxalase I from Zea mays.
Turra G, Agostini R, Fauguel C, Presello D, Andreo C, Gonzalez J
Acta Crystallogr D Biol Crystallogr. 2015; 71(Pt 10):2009-20.
PMID: 26457425
PMC: 4601366.
DOI: 10.1107/S1399004715015205.
Comparison of trace element concentration in bone and intervertebral disc tissue by atomic absorption spectrometry techniques.
Kubaszewski L, Ziola-Frankowska A, Frankowski M, Rogala P, Gasik Z, Kaczmarczyk J
J Orthop Surg Res. 2014; 9:99.
PMID: 25342441
PMC: 4220064.
DOI: 10.1186/s13018-014-0099-y.
Force field independent metal parameters using a nonbonded dummy model.
Duarte F, Bauer P, Barrozo A, Amrein B, Purg M, Aqvist J
J Phys Chem B. 2014; 118(16):4351-62.
PMID: 24670003
PMC: 4180081.
DOI: 10.1021/jp501737x.
Nonredox nickel enzymes.
Maroney M, Ciurli S
Chem Rev. 2013; 114(8):4206-28.
PMID: 24369791
PMC: 5675112.
DOI: 10.1021/cr4004488.
Five decades with glutathione and the GSTome.
Mannervik B
J Biol Chem. 2012; 287(9):6072-83.
PMID: 22247548
PMC: 3307307.
DOI: 10.1074/jbc.X112.342675.
Structural variation in bacterial glyoxalase I enzymes: investigation of the metalloenzyme glyoxalase I from Clostridium acetobutylicum.
Suttisansanee U, Lau K, Lagishetty S, Rao K, Swaminathan S, Sauder J
J Biol Chem. 2011; 286(44):38367-38374.
PMID: 21914803
PMC: 3207458.
DOI: 10.1074/jbc.M111.251603.
Glyoxalase I gene deletion mutants of Leishmania donovani exhibit reduced methylglyoxal detoxification.
Chauhan S, Madhubala R
PLoS One. 2009; 4(8):e6805.
PMID: 19710909
PMC: 2728510.
DOI: 10.1371/journal.pone.0006805.
A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major.
Vickers T, Greig N, Fairlamb A
Proc Natl Acad Sci U S A. 2004; 101(36):13186-91.
PMID: 15329410
PMC: 516525.
DOI: 10.1073/pnas.0402918101.
Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes.
Sukdeo N, Clugston S, Daub E, Honek J
Biochem J. 2004; 384(Pt 1):111-7.
PMID: 15270717
PMC: 1134094.
DOI: 10.1042/BJ20041006.
Investigation of metal binding and activation of Escherichia coli glyoxalase I: kinetic, thermodynamic and mutagenesis studies.
Clugston S, Yajima R, Honek J
Biochem J. 2003; 377(Pt 2):309-16.
PMID: 14556652
PMC: 1223881.
DOI: 10.1042/BJ20030271.
Mutagenesis of residue 157 in the active site of human glyoxalase I.
Ridderstrom M, Cameron A, Jones T, Mannervik B
Biochem J. 1998; 328 ( Pt 1):231-5.
PMID: 9359858
PMC: 1218911.
DOI: 10.1042/bj3280231.
Optimized heterologous expression of the human zinc enzyme glyoxalase I.
Ridderstrom M, Mannervik B
Biochem J. 1996; 314 ( Pt 2):463-7.
PMID: 8670058
PMC: 1217073.
DOI: 10.1042/bj3140463.
Probing the active site of glyoxalase I from human erythrocytes by use of the strong reversible inhibitor S-p-bromobenzylglutathione and metal substitutions.
Aronsson A, Sellin S, Tibbelin G, Mannervik B
Biochem J. 1981; 197(1):67-75.
PMID: 7317034
PMC: 1163055.
DOI: 10.1042/bj1970067.
13-Hydroperoxylinoleic acid inhibits rat liver glyoxalase II.
Gillespie E
Inflammation. 1981; 5(3):203-11.
PMID: 7298161
DOI: 10.1007/BF00914444.