Glyceraldehyde-3-phosphate dehydrogenase is involved in the pathogenesis of Alzheimer's disease von Schmalhausen, E.V., Medvedeva, M.V., Muronetz, V.I.

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S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase induces formation of C150-C154 intrasubunit disulfide bond in the active site of the enzyme von Barinova, K.V., Serebryakova, M.V., Muronetz, V.I., Schmalhausen, E.V.

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S-nitrosylation and S-glutathionylation of GAPDH: Similarities, differences, and relationships von Medvedeva, M.V., Kleimenov, S. Yu, Samygina, V.R., Muronetz, V.I., Schmalhausen, E.V.

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Products of S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase: Relation between S-nitrosylation and oxidation von Schmalhausen, E.V., Medvedeva, M.V., Serebryakova, M.V., Chagovets, V.V., Muronetz, V.I.

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Mechanism of inactivation of glyceraldehyde-3-phosphate dehydrogenase in the presence of methylglyoxal von Barinova, K.V., Serebryakova, M.V., Melnikova, A.K., Medvedeva, M.V., Muronetz, V.I., Schmalhausen, E.V.

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S-glutathionylation of human glyceraldehyde-3-phosphate dehydrogenase and possible role of Cys152-Cys156 disulfide bridge in the active site of the protein von Barinova, K.V., Serebryakova, M.V., Eldarov, M.A., Kulikova, A.A., Mitkevich, V.A., Muronetz, V.I., Schmalhausen, E.V.

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Oxidation of glyceraldehyde-3-phosphate dehydrogenase decreases sperm motility von Elkina, Yu. L, Atroshchenko, M. M, Bragina, E. E, Muronetz, V. I, Schmalhausen, E. V

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Inhibitors of Glyceraldehyde 3-Phosphate Dehydrogenase and Unexpected Effects of Its Reduced Activity von Muronetz, V. I., Melnikova, A. K., Barinova, K. V., Schmalhausen, E. V.

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Glycation, glycolysis, and neurodegenerative diseases: Is there any connection? von Muronetz, V. I., Melnikova, A. K., Seferbekova, Z. N., Barinova, K. V., Schmalhausen, E. V.

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Post-Translational Modifications of the Sulfhydryl Group of the Cysteine Residue of Glyceraldehyde-3-phosphate Dehydrogenase von Muronetz, V. I., Medvedeva, M. V., Schmalhausen, E. V.

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Expression of glyceraldehyde-3-phosphate dehydrogenase from M. tuberculosis in E. coli. Purification and characteristics of the untagged recombinant enzyme von Schmalhausen, E.V., Shumkov, M.S., Muronetz, V.I., Švedas, V.K.

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Isolation of recombinant human untagged glyceraldehyde-3-phosphate dehydrogenase from E. coli producer strain von Barinova, K.V., Eldarov, M.A., Khomyakova, E.V., Muronetz, V.I., Schmalhausen, E.V.

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Dimerization of Tyr136Cys alpha-synuclein prevents amyloid transformation of wild type alpha-synuclein von Barinova, K.V., Kuravsky, M.L., Arutyunyan, A.M., Serebryakova, M.V., Schmalhausen, E.V., Muronetz, V.I.

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Denaturing action of adjuvant affects specificity of polyclonal antibodies von Barinova, K.V., Khomyakova, E.V., Kuravsky, M.L., Schmalhausen, E.V., Muronetz, V.I.

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Low concentrations of hydrogen peroxide activate the antioxidant defense system in human sperm cells von Evdokimov, V. V., Barinova, K. V., Turovetskii, V. B., Muronetz, V. I., Schmalhausen, E. V.

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Structural basis for the NAD binding cooperativity and catalytic characteristics of sperm-specific glyceraldehyde-3-phosphate dehydrogenase von Kuravsky, M.L., Barinova, K.V., Asryants, R.A., Schmalhausen, E.V., Muronetz, V.I.

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Sperm-Specific Glyceraldehyde-3-Phosphate Dehydrogenase–An Evolutionary Acquisition of Mammals von Muronetz, V. I., Kuravsky, M. L., Barinova, K. V., Schmalhausen, E. V.

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Mildly Oxidized Glyceraldehyde‐3‐Phosphate Dehydrogenase as a Possible Regulator of Glycolysis von Danshina, P. V., Schmalhausen, E. V., Avetisyan, A. V., Muronetz, V. I.

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Ascorbate-induced oxidation of glyceraldehyde-3-phosphate dehydrogenase von Schmalhausen, E.V., Pleten’, A.P., Muronetz, V.I.

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Recombinant human sperm-specific glyceraldehyde-3-phosphate dehydrogenase: Structural basis for enhanced stability von Elkina, Yu. L., Kuravsky, M.L., El'darov, M.A., Stogov, S.V., Muronetz, V.I., Schmalhausen, E.V.

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