Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity (613 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2010 May; 92(5): 464-474.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.787, 5-year impact factor: 3.728
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77951022274&partnerID=40&md5=0d5d364b736e3efba57602ea96b6f062
Keywords: Gamma-Glutamyltranspeptidase, Geobacillus Thermodenitrificans, Glutathione, N-Terminal Nucleophile Hydrolase, Thermophilic Enzymes, Amide, Amino Acid, Anilide, Gamma Glutamyltransferase, Glutamic Acid, Protein Precursor, Water, Article, Biotechnology, Catalysis, Chemical Analysis, Controlled Study, Drug Targeting, Enzyme Activity, Enzyme Purification, Enzyme Stability, Enzyme Structure, Enzyme Substrate, Enzyme Subunit, Escherichia Coli, Glutathione Metabolism, Hydrolysis, Molecular Cloning, Nonhuman, Oxidative Stress, Protein Cleavage, Protein Expression, Structure Analysis, Temperature, Amino Acid Sequence, Base Sequence, Biocatalysis, Dna Primers, Electrophoresis, Polyacrylamide Gel, Gamma-Glutamyl Hydrolase, Gamma-Glutamyltransferase, Hydrogen-Ion Concentration, Kinetics, Molecular Sequence Data, Molecular Weight, Mutagenesis, Site-Directed, Sequence Homology,
Affiliations:
*** IBB - CNR ***
CNR, Institute of Protein Biochemistry, Via Pietro Castellino 111, I-80131 Naples, Italy
Department of Chemistry, University of Naples 'Federico II', Via Cinthia, I-80126 Naples, Italy
References:
Tate, S.S., Meister, A., Gamma-glutamyl transpeptidase: catalytic, structural and functional aspects (1981) Mol. Cell. Biochem., 39, pp. 357-36
Pompella, A., Corti, A., Paolicchi, A., Giommarelli, C., Zunino, F., Gamma-glutamyltransferase, redox regulation and cancer drug resistance (2007) Curr. Opin. Pharmacol., 7, pp. 360-366
Lee, D.H., Blomhoff, R., Jacobs, D.R., Is serum gamma glutamyltransferase a marker of oxidative stress? (2004) Free Radic. Res., 38, pp. 535-539
Arai, K., Sumi, S.H., Yoshida, K., Komoda, T., A precursor form of human kidney gamma-glutamyl transferase in normal and cancerous tissues, and its possible post-translational modification (1995) Biochim. Biophys. Acta, 1253, pp. 33-38
Yao, D., Jiang, D., Huang, Z., Abnormal expression of hepatoma specific gamma-glutamyl transferase and alteration of gamma-glutamyl transferase gene methylation status in patients with hepatocellular carcinoma (2000) Cancer, 88, pp. 761-769
Schäfer, C., Fels, C., Brucke, M., Gamma-glutamyl transferase expression in higher-grade astrocytic glioma (2001) Acta Oncol., 40, pp. 529-535
Chinta, S.J., Kumar, J.M., Zhang, H., Forman, H.J., Andersen, J.K., Up-regulation of gamma-glutamyl transpeptidase activity following glutathione depletion has a compensatory rather than an inhibitory effect on mitochondrial complex I activity: implications for Parkinson's disease (2006) Free Radic. Biol. Med., 40, pp. 1557-1563
Emdin, M., Pompella, A., Paolicchi, A., Gamma-glutamyltransferase, atherosclerosis, and cardiovascular disease: triggering oxidative stress within the plaque (2005) Circulation, 112, pp. 2130-2137
Pompella, A., De Tata, V., Paolicchi, A., Zunino, F., Expression of gamma-glutamyltransferase in cancer cells and its significance in drug resistance (2006) Biochem. Pharmacol., 71, pp. 231-238
Dufour, D.R., Lott, J.A., Nolte, F.S., Gretch, D.R., Koff, R.S., Seeff, L.B., Diagnosis and monitoring of hepatic injury. I. Performance characteristics of laboratory tests (2001) Clin. Chem., 47, pp. 1133-1135
Marchesini, G., Avagnina, S., Barantani, E.G., Ciccarone, A.M., Aminotransferase and γ-glutamyltranspeptidase levels in obesity are associated with insulin resistance and the metabolic syndrome (2005) J. Endocrinol. Invest., 28, pp. 333-339
Chevalier, C., Thiberge, J.M., Ferrero, R.L., Labigne, A., Essential role of Helicobacter pylori gamma-glutamyltranspeptidase for the colonization of the gastric mucosa of mice (1999) Mol. Microbiol., 31, pp. 1359-1372
McGovern, K.J., Blanchard, T.G., Gutierrez, J.A., Czinn, S.J., Krakowka, S., Youngman, P., Gamma-Glutamyltransferase is a Helicobacter pylori virulence factor but is not essential for colonization (2001) Infect. Immun., 69, pp. 4168-4173
Boanca, G., Sand, A., Barycki, J.J., Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori gamma-glutamyltranspeptidase (2006) J. Biol. Chem., 281, pp. 19029-19037
Suzuki, H., Kumagai, H., Autocatalytic processing of gamma-glutamyltranspeptidase (2002) J. Biol. Chem., 277, pp. 43536-43543
Kinlough, C.L., Poland, P.A., Bruns, J.B., Hughey, R.P., Gamma-glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum (2005) Meth. Enzymol., 401, pp. 426-449. , (Review)
Brannigan, J.A., Dodson, G., Duggleby, H.J., A protein catalytic framework with an N-terminal nucleophile is capable of self-activation (1995) Nature, 78, pp. 416-419
Oinonen, C., Rouvinen, J., Structural comparison of Ntn-hydrolases (2000) Protein Sci., 9, pp. 2329-2337
Okada, T., Suzuki, H., Wada, K., Kumagai, H., Fukuyama, K., Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate (2006) Proc. Natl. Acad. Sci. U.S.A., 103, pp. 6471-6476
Wang, L., Tang, Y., Wang, S., Isolation and characterization of a novel thermophilic Bacillus strain degrading long-chain n-alkanes (2006) Extremophiles, 10, pp. 347-356
Feng, L., Wang, W., Cheng, J., Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir (2007) Proc. Natl. Acad. Sci. U.S.A., 104, pp. 5602-5607
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T 4 (1970) Nature, 227, pp. 680-685
Schwede, T., Kopp, J., Guex, N., Peitsch, M.C., SWISS-MODEL: an automated protein homology-modeling server (2003) Nucleic Acids Res., 31, pp. 3381-3385
Jones, T.A., Bergdoll, M., Kjeldgaard, M., O: a macromolecular modeling environment (1990) Crystallographic and Modeling Methods in Molecular Design, pp. 189-195. , Springer-Verlag Press, C. Bugg, S. Ealick (Eds.)
van der Spoel, D., van Druner, R., Berendsen, H.J.C., (1994) Groningen Machine for Chemical Simulation, , Department of Biophysical Chemistry, BIOSON Research Institute, Groningen, The Netherlands
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: a program to check the stereochemical quality of protein structure (1993) J. Appl. Crystallogr., 26, pp. 283-291
Hooft, R.W., Vriend, G., Sander, C., Abola, E.E., Errors in protein structures (1996) Nature, 381, p. 272
Wiederstein, M., Sippl, M.J., ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins (2007) Nucleic Acids Res., 35, pp. 407-410
Kraulis, P.J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Willard, L., Ranjan, A., Zhang, H., Monzavi, H., Boyko, R.F., Sykes, B.D., Wishart, D.S., VADAR: a web server for quantitative evaluation of protein structure quality (2003) Nucleic Acids Res., 31, pp. 3316-3319
McDonald, I.K., Thornton, J.M., Satisfying hydrogen bonding potential in proteins (1994) J. Mol. Biol., 238, pp. 777-793
Costantini, S., Colonna, G., Facchiano, A.M., ESBRI: a web server for evaluating salt bridges in proteins (2008) Bioinformation, 3, pp. 137-138
Figlewicz, D.A., Delattre, O., Guellaen, G., Mapping of human gamma-glutamyl transpeptidase genes on chromosome 22 and other human autosomes (1993) Genomics, 17, pp. 299-305
Xu, K., Strauch, M.A., Identification, sequence, and expression of the gene encoding gamma-glutamyltranspeptidase in Bacillus subtilis (1996) J. Bacteriol., 178, pp. 4319-4322
Tomb, J.F., White, O., Kerlavage, A.R., The complete genome sequence of the gastric pathogen Helicobacter pylori (1997) Nature, 388, pp. 539-547
Larkin, M.A., Blackshields, G., Brown, N.P., Clustal W and Clustal X version 2.0 (2007) Bioinformatics, 23, pp. 2947-2948
Hashimoto, W., Suzuki, H., Nohara, S., Tachi, H., Yamamoto, K., Kumagai, H., Subunit association of gamma-glutamyltranspeptidase of Escherichia coli K-12 (1995) J. Biochem., 118, pp. 1216-1223
Williams, K., Cullati, S., Sand, A., Biterova, E.I., Barycki, J.J., Crystal structure of acivicin-inhibited γ-glutamyltranspeptidase reveals critical roles for its C-Terminus in autoprocessing and catalysis (2009) Biochemistry, 48, pp. 2459-2467
Ikeda, Y., Fujii, J., Anderson, M.E., Taniguchi, N., Meister, A., Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase (1995) J. Biol. Chem., 270, pp. 22223-22228
Szilagyi, A., Zavodsky, P., Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey (2000) Struct. Fold Des., 8, pp. 493-504
De Vendittis, E., Castellano, I., Cotugno, R., Ruocco, M.R., Raimo, G., Masullo, M., Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition (2008) J. Theor. Biol., 250, pp. 156-171
Nakayama, R., Kumagai, H., Tochikura, T., Purification and properties of gamma-glutamyltranspeptidase from Proteus mirabilis (1984) J. Bacteriol., 160, pp. 341-346
Lin, L.L., Chou, P.R., Hua, Y.W., Hsu, W.H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacillus licheniformis (2006) Appl. Microbiol. Biotechnol., 73, pp. 103-112
Suzuki, H., Yamada, C., Kato, K., Gamma-glutamyl compounds and their enzymatic production using bacterial gamma-glutamyltranspeptidase (2007) Amino Acids, 32, pp. 333-340. , (Review)
Minami, H., Suzuki, H., Kumagai, H., A mutant Bacillus subtilis gamma-glutamyltranspeptidase specialized in hydrolysis activity (2003) FEMS Microbiol. Lett., 224, pp. 169-173
Vermeulen, N., Gänzle, M.G., Vogel, R.F., Glutamine deamidation by cereal-associated lactic acid bacteria (2007) J. Appl. Microbiol., 103, pp. 1197-1205
Abe, K., Ito, Y., Ohmachi, T., Asada, Y., Purification and properties of two isozymes of gamma-glutamyltranspeptidase from Bacillus subtilis TAM-4 (1997) Biosci. Biotechnol. Biochem., 61, pp. 1621-1625
Lyu, R.C., Hu, H.Y., Kuo, L.Y., Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis γ-glutamyltranspeptidase as evaluated by mutational analysis (2009) Curr. Microbiol., 59, pp. 101-106
Khan, J.A., Dunn, B.M., Tong, L., Crystal structure of human taspase1, a crucial protease regulating the function of MLL (2005) Structure, 13, pp. 1443-1452
Suzuki, H., Miwa, C., Ishihara, S., Kumagai, H., A single amino acid substitution converts gamma-glutamyltranspeptidase to a class IV cephalosporin acylase (glutaryl-7-aminocephalosporanic acid acylase) (2004) Appl. Environ. Microbiol., 70, pp. 6324-6328
Yamada, C., Kijima, K., Ishihara, S., Improvement of the glutaryl-7-aminocephalosporanic acid acylase activity of a bacterial gamma-glutamyltranspeptidase (2008) Appl. Environ. Microbiol., 74, pp. 3400-3409
Tate, S. S., Meister, A., Gamma-glutamyl transpeptidase: catalytic, structural and functional aspects (1981) Mol. Cell. Biochem., 39, pp. 357-36
Lee, D. H., Blomhoff, R., Jacobs, D. R., Is serum gamma glutamyltransferase a marker of oxidative stress? (2004) Free Radic. Res., 38, pp. 535-539
Arai, K., Sumi, S. H., Yoshida, K., Komoda, T., A precursor form of human kidney gamma-glutamyl transferase in normal and cancerous tissues, and its possible post-translational modification (1995) Biochim. Biophys. Acta, 1253, pp. 33-38
Sch fer, C., Fels, C., Brucke, M., Gamma-glutamyl transferase expression in higher-grade astrocytic glioma (2001) Acta Oncol., 40, pp. 529-535
Chinta, S. J., Kumar, J. M., Zhang, H., Forman, H. J., Andersen, J. K., Up-regulation of gamma-glutamyl transpeptidase activity following glutathione depletion has a compensatory rather than an inhibitory effect on mitochondrial complex I activity: implications for Parkinson's disease (2006) Free Radic. Biol. Med., 40, pp. 1557-1563
Dufour, D. R., Lott, J. A., Nolte, F. S., Gretch, D. R., Koff, R. S., Seeff, L. B., Diagnosis and monitoring of hepatic injury. I. Performance characteristics of laboratory tests (2001) Clin. Chem., 47, pp. 1133-1135
McGovern, K. J., Blanchard, T. G., Gutierrez, J. A., Czinn, S. J., Krakowka, S., Youngman, P., Gamma-Glutamyltransferase is a Helicobacter pylori virulence factor but is not essential for colonization (2001) Infect. Immun., 69, pp. 4168-4173
Kinlough, C. L., Poland, P. A., Bruns, J. B., Hughey, R. P., Gamma-glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum (2005) Meth. Enzymol., 401, pp. 426-449. , (Review)
Brannigan, J. A., Dodson, G., Duggleby, H. J., A protein catalytic framework with an N-terminal nucleophile is capable of self-activation (1995) Nature, 78, pp. 416-419
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T 4 (1970) Nature, 227, pp. 680-685
Jones, T. A., Bergdoll, M., Kjeldgaard, M., O: a macromolecular modeling environment (1990) Crystallographic and Modeling Methods in Molecular Design, pp. 189-195. , Springer-Verlag Press, C. Bugg, S. Ealick (Eds.)
Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., PROCHECK: a program to check the stereochemical quality of protein structure (1993) J. Appl. Crystallogr., 26, pp. 283-291
Hooft, R. W., Vriend, G., Sander, C., Abola, E. E., Errors in protein structures (1996) Nature, 381, p. 272
Kraulis, P. J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
McDonald, I. K., Thornton, J. M., Satisfying hydrogen bonding potential in proteins (1994) J. Mol. Biol., 238, pp. 777-793
Figlewicz, D. A., Delattre, O., Guellaen, G., Mapping of human gamma-glutamyl transpeptidase genes on chromosome 22 and other human autosomes (1993) Genomics, 17, pp. 299-305
Tomb, J. F., White, O., Kerlavage, A. R., The complete genome sequence of the gastric pathogen Helicobacter pylori (1997) Nature, 388, pp. 539-547
Larkin, M. A., Blackshields, G., Brown, N. P., Clustal W and Clustal X version 2. 0 (2007) Bioinformatics, 23, pp. 2947-2948
Lin, L. L., Chou, P. R., Hua, Y. W., Hsu, W. H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacillus licheniformis (2006) Appl. Microbiol. Biotechnol., 73, pp. 103-112
Vermeulen, N., G nzle, M. G., Vogel, R. F., Glutamine deamidation by cereal-associated lactic acid bacteria (2007) J. Appl. Microbiol., 103, pp. 1197-1205
Lyu, R. C., Hu, H. Y., Kuo, L. Y., Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis -glutamyltranspeptidase as evaluated by mutational analysis (2009) Curr. Microbiol., 59, pp. 101-106
Khan, J. A., Dunn, B. M., Tong, L., Crystal structure of human taspase1, a crucial protease regulating the function of MLL (2005) Structure, 13, pp. 1443-1452
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2010 May; 92(5): 464-474.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.787, 5-year impact factor: 3.728
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77951022274&partnerID=40&md5=0d5d364b736e3efba57602ea96b6f062
Keywords: Gamma-Glutamyltranspeptidase, Geobacillus Thermodenitrificans, Glutathione, N-Terminal Nucleophile Hydrolase, Thermophilic Enzymes, Amide, Amino Acid, Anilide, Gamma Glutamyltransferase, Glutamic Acid, Protein Precursor, Water, Article, Biotechnology, Catalysis, Chemical Analysis, Controlled Study, Drug Targeting, Enzyme Activity, Enzyme Purification, Enzyme Stability, Enzyme Structure, Enzyme Substrate, Enzyme Subunit, Escherichia Coli, Glutathione Metabolism, Hydrolysis, Molecular Cloning, Nonhuman, Oxidative Stress, Protein Cleavage, Protein Expression, Structure Analysis, Temperature, Amino Acid Sequence, Base Sequence, Biocatalysis, Dna Primers, Electrophoresis, Polyacrylamide Gel, Gamma-Glutamyl Hydrolase, Gamma-Glutamyltransferase, Hydrogen-Ion Concentration, Kinetics, Molecular Sequence Data, Molecular Weight, Mutagenesis, Site-Directed, Sequence Homology,
Affiliations:
*** IBB - CNR ***
CNR, Institute of Protein Biochemistry, Via Pietro Castellino 111, I-80131 Naples, Italy
Department of Chemistry, University of Naples 'Federico II', Via Cinthia, I-80126 Naples, Italy
References:
Tate, S.S., Meister, A., Gamma-glutamyl transpeptidase: catalytic, structural and functional aspects (1981) Mol. Cell. Biochem., 39, pp. 357-36
Pompella, A., Corti, A., Paolicchi, A., Giommarelli, C., Zunino, F., Gamma-glutamyltransferase, redox regulation and cancer drug resistance (2007) Curr. Opin. Pharmacol., 7, pp. 360-366
Lee, D.H., Blomhoff, R., Jacobs, D.R., Is serum gamma glutamyltransferase a marker of oxidative stress? (2004) Free Radic. Res., 38, pp. 535-539
Arai, K., Sumi, S.H., Yoshida, K., Komoda, T., A precursor form of human kidney gamma-glutamyl transferase in normal and cancerous tissues, and its possible post-translational modification (1995) Biochim. Biophys. Acta, 1253, pp. 33-38
Yao, D., Jiang, D., Huang, Z., Abnormal expression of hepatoma specific gamma-glutamyl transferase and alteration of gamma-glutamyl transferase gene methylation status in patients with hepatocellular carcinoma (2000) Cancer, 88, pp. 761-769
Schäfer, C., Fels, C., Brucke, M., Gamma-glutamyl transferase expression in higher-grade astrocytic glioma (2001) Acta Oncol., 40, pp. 529-535
Chinta, S.J., Kumar, J.M., Zhang, H., Forman, H.J., Andersen, J.K., Up-regulation of gamma-glutamyl transpeptidase activity following glutathione depletion has a compensatory rather than an inhibitory effect on mitochondrial complex I activity: implications for Parkinson's disease (2006) Free Radic. Biol. Med., 40, pp. 1557-1563
Emdin, M., Pompella, A., Paolicchi, A., Gamma-glutamyltransferase, atherosclerosis, and cardiovascular disease: triggering oxidative stress within the plaque (2005) Circulation, 112, pp. 2130-2137
Pompella, A., De Tata, V., Paolicchi, A., Zunino, F., Expression of gamma-glutamyltransferase in cancer cells and its significance in drug resistance (2006) Biochem. Pharmacol., 71, pp. 231-238
Dufour, D.R., Lott, J.A., Nolte, F.S., Gretch, D.R., Koff, R.S., Seeff, L.B., Diagnosis and monitoring of hepatic injury. I. Performance characteristics of laboratory tests (2001) Clin. Chem., 47, pp. 1133-1135
Marchesini, G., Avagnina, S., Barantani, E.G., Ciccarone, A.M., Aminotransferase and γ-glutamyltranspeptidase levels in obesity are associated with insulin resistance and the metabolic syndrome (2005) J. Endocrinol. Invest., 28, pp. 333-339
Chevalier, C., Thiberge, J.M., Ferrero, R.L., Labigne, A., Essential role of Helicobacter pylori gamma-glutamyltranspeptidase for the colonization of the gastric mucosa of mice (1999) Mol. Microbiol., 31, pp. 1359-1372
McGovern, K.J., Blanchard, T.G., Gutierrez, J.A., Czinn, S.J., Krakowka, S., Youngman, P., Gamma-Glutamyltransferase is a Helicobacter pylori virulence factor but is not essential for colonization (2001) Infect. Immun., 69, pp. 4168-4173
Boanca, G., Sand, A., Barycki, J.J., Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori gamma-glutamyltranspeptidase (2006) J. Biol. Chem., 281, pp. 19029-19037
Suzuki, H., Kumagai, H., Autocatalytic processing of gamma-glutamyltranspeptidase (2002) J. Biol. Chem., 277, pp. 43536-43543
Kinlough, C.L., Poland, P.A., Bruns, J.B., Hughey, R.P., Gamma-glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum (2005) Meth. Enzymol., 401, pp. 426-449. , (Review)
Brannigan, J.A., Dodson, G., Duggleby, H.J., A protein catalytic framework with an N-terminal nucleophile is capable of self-activation (1995) Nature, 78, pp. 416-419
Oinonen, C., Rouvinen, J., Structural comparison of Ntn-hydrolases (2000) Protein Sci., 9, pp. 2329-2337
Okada, T., Suzuki, H., Wada, K., Kumagai, H., Fukuyama, K., Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate (2006) Proc. Natl. Acad. Sci. U.S.A., 103, pp. 6471-6476
Wang, L., Tang, Y., Wang, S., Isolation and characterization of a novel thermophilic Bacillus strain degrading long-chain n-alkanes (2006) Extremophiles, 10, pp. 347-356
Feng, L., Wang, W., Cheng, J., Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir (2007) Proc. Natl. Acad. Sci. U.S.A., 104, pp. 5602-5607
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T 4 (1970) Nature, 227, pp. 680-685
Schwede, T., Kopp, J., Guex, N., Peitsch, M.C., SWISS-MODEL: an automated protein homology-modeling server (2003) Nucleic Acids Res., 31, pp. 3381-3385
Jones, T.A., Bergdoll, M., Kjeldgaard, M., O: a macromolecular modeling environment (1990) Crystallographic and Modeling Methods in Molecular Design, pp. 189-195. , Springer-Verlag Press, C. Bugg, S. Ealick (Eds.)
van der Spoel, D., van Druner, R., Berendsen, H.J.C., (1994) Groningen Machine for Chemical Simulation, , Department of Biophysical Chemistry, BIOSON Research Institute, Groningen, The Netherlands
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: a program to check the stereochemical quality of protein structure (1993) J. Appl. Crystallogr., 26, pp. 283-291
Hooft, R.W., Vriend, G., Sander, C., Abola, E.E., Errors in protein structures (1996) Nature, 381, p. 272
Wiederstein, M., Sippl, M.J., ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins (2007) Nucleic Acids Res., 35, pp. 407-410
Kraulis, P.J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Willard, L., Ranjan, A., Zhang, H., Monzavi, H., Boyko, R.F., Sykes, B.D., Wishart, D.S., VADAR: a web server for quantitative evaluation of protein structure quality (2003) Nucleic Acids Res., 31, pp. 3316-3319
McDonald, I.K., Thornton, J.M., Satisfying hydrogen bonding potential in proteins (1994) J. Mol. Biol., 238, pp. 777-793
Costantini, S., Colonna, G., Facchiano, A.M., ESBRI: a web server for evaluating salt bridges in proteins (2008) Bioinformation, 3, pp. 137-138
Figlewicz, D.A., Delattre, O., Guellaen, G., Mapping of human gamma-glutamyl transpeptidase genes on chromosome 22 and other human autosomes (1993) Genomics, 17, pp. 299-305
Xu, K., Strauch, M.A., Identification, sequence, and expression of the gene encoding gamma-glutamyltranspeptidase in Bacillus subtilis (1996) J. Bacteriol., 178, pp. 4319-4322
Tomb, J.F., White, O., Kerlavage, A.R., The complete genome sequence of the gastric pathogen Helicobacter pylori (1997) Nature, 388, pp. 539-547
Larkin, M.A., Blackshields, G., Brown, N.P., Clustal W and Clustal X version 2.0 (2007) Bioinformatics, 23, pp. 2947-2948
Hashimoto, W., Suzuki, H., Nohara, S., Tachi, H., Yamamoto, K., Kumagai, H., Subunit association of gamma-glutamyltranspeptidase of Escherichia coli K-12 (1995) J. Biochem., 118, pp. 1216-1223
Williams, K., Cullati, S., Sand, A., Biterova, E.I., Barycki, J.J., Crystal structure of acivicin-inhibited γ-glutamyltranspeptidase reveals critical roles for its C-Terminus in autoprocessing and catalysis (2009) Biochemistry, 48, pp. 2459-2467
Ikeda, Y., Fujii, J., Anderson, M.E., Taniguchi, N., Meister, A., Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase (1995) J. Biol. Chem., 270, pp. 22223-22228
Szilagyi, A., Zavodsky, P., Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey (2000) Struct. Fold Des., 8, pp. 493-504
De Vendittis, E., Castellano, I., Cotugno, R., Ruocco, M.R., Raimo, G., Masullo, M., Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition (2008) J. Theor. Biol., 250, pp. 156-171
Nakayama, R., Kumagai, H., Tochikura, T., Purification and properties of gamma-glutamyltranspeptidase from Proteus mirabilis (1984) J. Bacteriol., 160, pp. 341-346
Lin, L.L., Chou, P.R., Hua, Y.W., Hsu, W.H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacillus licheniformis (2006) Appl. Microbiol. Biotechnol., 73, pp. 103-112
Suzuki, H., Yamada, C., Kato, K., Gamma-glutamyl compounds and their enzymatic production using bacterial gamma-glutamyltranspeptidase (2007) Amino Acids, 32, pp. 333-340. , (Review)
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Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity
Gamma-glutamyltranspeptidases (gamma-GTs) catalyze the transfer of the gamma-glutamyl moiety of glutathione and related gamma-glutamyl amides to water (hydrolysis) or to amino acids and peptides (transpeptidation) and play a key role in glutathione metabolism. Recently, gamma-GTs have been considered attractive pharmaceutical targets for cancer and useful tools to produce gamma-glutamyl compounds. To find out gamma-GTs with special properties we have chosen microorganisms belonging to Geobacillus species which are source of several thermostable enzymes of potential interest for biotechnology. gamma-GT from Geobacillus thermodenitrificans (GthGT) was cloned, expressed in Escherichia coli, purified to homogeneity and characterized. The enzyme, synthesized as a precursor homotetrameric protein of 61-kDa per subunit, undergoes an internal post-translational cleavage of the 61 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits. The kinetic characterization of the hydrolysis reaction using L-glutamic acid gamma-(4-nitroanilide) as the substrate reveals that the active enzyme has K-m 7.6 mu M and V-max 0.36 mu mol min/mg. The optimum pH and temperature for the hydrolysis activity are 7.8 and 52 degrees C. respectively. GthGT hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress. Unlike other gamma-GTs, the mutation of the highly conserved catalytic nucleophile, Thr353, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action. Furthermore, GthGT does not show any transpeptidase activity, suggesting that the enzyme is a specialized gamma-glutamyl hydrolase. The GthGT homology-model structure reveals peculiar structural features, which should be responsible for the different functional properties of the enzyme and suggests the structural bases of protein thermostability. (C) 2010 Elsevier Masson SAS. All rights reserved.
Gamma-glutamyltranspeptidases (gamma-GTs) catalyze the transfer of the gamma-glutamyl moiety of glutathione and related gamma-glutamyl amides to water (hydrolysis) or to amino acids and peptides (transpeptidation) and play a key role in glutathione metabolism. Recently, gamma-GTs have been considered attractive pharmaceutical targets for cancer and useful tools to produce gamma-glutamyl compounds. To find out gamma-GTs with special properties we have chosen microorganisms belonging to Geobacillus species which are source of several thermostable enzymes of potential interest for biotechnology. gamma-GT from Geobacillus thermodenitrificans (GthGT) was cloned, expressed in Escherichia coli, purified to homogeneity and characterized. The enzyme, synthesized as a precursor homotetrameric protein of 61-kDa per subunit, undergoes an internal post-translational cleavage of the 61 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits. The kinetic characterization of the hydrolysis reaction using L-glutamic acid gamma-(4-nitroanilide) as the substrate reveals that the active enzyme has K-m 7.6 mu M and V-max 0.36 mu mol min/mg. The optimum pH and temperature for the hydrolysis activity are 7.8 and 52 degrees C. respectively. GthGT hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress. Unlike other gamma-GTs, the mutation of the highly conserved catalytic nucleophile, Thr353, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action. Furthermore, GthGT does not show any transpeptidase activity, suggesting that the enzyme is a specialized gamma-glutamyl hydrolase. The GthGT homology-model structure reveals peculiar structural features, which should be responsible for the different functional properties of the enzyme and suggests the structural bases of protein thermostability. (C) 2010 Elsevier Masson SAS. All rights reserved.
Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity
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Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity
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Bonomo RP, De Flora A, Rizzarelli E, Santoro AM, Tabbì G, Tonetti M
Copper(II) complexes encapsulated in human red blood cells (587 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 1995 Sep; 59(4): 773-784.
Impact Factor: 1.342
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* Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins (62 views)
Sci Rep (ISSN: 2045-2322linking, 2045-2322electronic), 2020 Jun 2; 10(1): 8943-8943.
Impact Factor: 3.998
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Sgarlata C, Arena G, Bonomo RP, Giuffrida A, Tabbì G
* Simple and mixed complexes of copper(II) with 8-hydroxyquinoline derivatives and amino acids: Characterization in solution and potential biological implications (406 views) (PDF 160 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2017 Dec 8; 180: 89-100.
Impact Factor: 3.063
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Limauro D, De Simone G, Pirone L, Bartolucci S, D'Ambrosio K, Pedone E
* Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase (429 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2014 Mar; 18(2): 219-228.
Impact Factor: 2.306
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Sica F, Pica A, Merlino A, Russo Krauss I, Ercole C, Picone D
* The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer (328 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2013 Nov 29; 587(23): 3755-3762.
Impact Factor: 3.341
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Bera S, De Rosa V, Rachidi W, Diamond AM
* Does a role for selenium in DNA damage repair explain apparent controversies in its use in chemoprevention? (624 views)
Mutagenesismutagenesis (ISSN: 0267-8357, 1464-3804electronic, 0267-8357linking), 2013 Mar; 28(2): 127-134.
Impact Factor: 3.497
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Pica A, Russo Krauss I, Castellano I, La Cara F, Graziano G, Sica F, Merlino A
* Effect Of Nacl On The Conformational Stability Of The Thermophilic Gamma-Glutamyltranspeptidase From Geobacillus Thermodenitrificans: Implication For Globular Protein Halotolerance (334 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Jan; 1834(1): 149-157.
Impact Factor: 3.191
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Messori L, Scaletti F, Massai L, Cinellu MA, Gabbiani C, Vergara A, Merlino A
* The mode of action of anticancer gold-based drugs: a structural perspective (366 views)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2013; 49(86): 10100-10102.
Impact Factor: 6.718
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Pica A, Russo Krauss I, Castellano I, Rossi M, La Cara F, Graziano G, Sica F, Merlino A
* Exploring The Unfolding Mechanism Of Gamma-Glutamyltranspeptidases: The Case Of The Thermophilic Enzyme From Geobacillus Thermodenitrificans (422 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2012 Apr; 1824(4): 571-577.
Impact Factor: 3.733
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Truppo E, Supuran CT, Sandomenico A, Vullo D, Innocenti A, Di Fiore A, Alterio V, De Simone G, Monti SM
* Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors (384 views)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2012 Feb 15; 22(4): 1560-1564.
Impact Factor: 2.338
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Cirillo G, Colangelo AM, Bianco MR, Cavaliere C, Zaccaro L, Sarmientos P, Alberghina L, Papa M
* BB14, a Nerve Growth Factor (NGF)-like peptide shown to be effective in reducing reactive astrogliosis and restoring synaptic homeostasis in a rat model of peripheral nerve injury (402 views)
Biotechnology Advances (ISSN: 0734-9750), 2012 Jan; 30(1): 223-232.
Impact Factor: 9.599
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Castellano I, Merlino A
* γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications (422 views)
Cell Mol Life Sci (ISSN: 1420-682x), 2012; 69(20): 3381-3394.
Impact Factor: 5.615
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De Rosa V, Erkekoǧlu P, Forestier A, Favier A, Hincal F, Diamond AM, Douki T, Rachidi W
* Low doses of selenium specifically stimulate the repair of oxidative DNA damage in LNCaP prostate cancer cells (535 views)
Free Radic Res Free Radical Research (ISSN: 1071-5762), 2012; 46(2): 105-115.
Impact Factor: 3.279
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Merlino A, Russo Krauss I, Albino A, Pica A, Vergara A, Masullo M, De Vendittis E, Sica F
* Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis (361 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2011 Sep; 12(9): 6312-6319.
Impact Factor: 2.598
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Cirillo G, Bianco MR, Colangelo AM, Cavaliere C, Daniele DL, Zaccaro L, Alberghina L, Papa M
* Reactive astrocytosis-induced perturbation of synaptic homeostasis is restored by nerve growth factor (455 views)
Neurobiology Of Disease (ISSN: 0969-9961), 2011 Mar; 41(3): 630-639.
Impact Factor: 5.403
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Castellano I, Di Salle A, Merlino A, Rossi M, La Cara F
* Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts (340 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2011; 15(2): 259-270.
Impact Factor: 2.941
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Alterio V, Aurilia V, Romanelli A, Parracino A, Saviano M, D'Auria S, De Simone G
* Crystal structure of an S-formylglutathione hydrolase from pseudoalteromonas haloplanktis TAC125 (370 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2010 Sep; 93(8): 669-677.
Impact Factor: 2.572
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Erkekoǧlu P, Rachidi W, De Rosa V, Giray B, Favier A, Hincal F
* Protective effect of selenium supplementation on the genotoxicity of di(2-ethylhexyl)phthalate and mono(2-ethylhexyl)phthalate treatment in LNCaP cells (554 views)
Free Radic Biol Med (ISSN: 0891-5849, 0891-5849linking, 1873-4596electronic), 2010 Aug 15; 49(4): 559-566.
Impact Factor: 5.707
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Pedone E, Limauro D, Bartolucci S
* The Machinery for Oxidative Protein Folding in Thermophiles (vol 10, pg 157, 2008) (315 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2010 Jan; 12(1): 157-169.
Impact Factor: 8.209
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Doti N, Marasco D, Pedone C, Sabatella M, Ruvo M
* Optimizing A Kinase Assay For Ikkbeta On An Hts Station (373 views)
J Biomol Screen (ISSN: 1087-0571, 1552-454x, 1552-454xelectronic), 2009 Dec; 14(10): 1263-1268.
Impact Factor: 2.395
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Bellia F, Calabrese V, Guarino F, Cavallaro M, Cornelius C, De Pinto V, Rizzarelli E
* Carnosinase levels in aging brain: redox state induction and cellular stress response (415 views)
Antioxid Redox Signal (ISSN: 1557-7716, 1523-0864, 1523-0864linking), 2009 Nov; 11(11): 2759-2775.
Impact Factor: 7.581
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Calabrese V, Cornelius C, Rizzarelli E, Owen JB, Dinkova-Kostova AT, Butterfield DA
* Nitric oxide in cell survival: a janus molecule (850 views)
Antioxid Redox Signal (ISSN: 1557-7716, 1523-0864, 1523-0864linking), 2009 Nov; 11(11): 2717-2739.
Impact Factor: 7.581
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Limauro D, Saviano M, Galdi I, Rossi M, Bartolucci S, Pedone E
* Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (234 views)
Protein Engineering Design & Selection (ISSN: 1741-0126), 2009 Jan; 22(1): 19-26.
Impact Factor: 2.596
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Pedone E, Limauro D, Bartolucci S
* The machinery for oxidative protein folding in thermophiles (337 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2008 Jan; 10(1): 157-169.
Impact Factor: 6.19
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Agostini S, Bolzati C, Didonè E, Cavazza-Ceccato M, Refosco F, Aloj L, Arra C, Aurilio M, Tornesello AL, Tesauro D, Morelli G
* The (Tc(N)(PNP))2+ metal fragment labeled cholecystokinin-8 (CCK8) peptide for CCK-2 receptors imaging: In vitro and in vivo studies (400 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2007 Apr; 13(4): 211-219.
Impact Factor: 1.768
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Pedone E, Limauro D, D'Alterio R, Rossi M, Bartolucci S
* Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (328 views)
Febs Journal (ISSN: 1742-464x), 2006 Dec; 273(23): 5407-5420.
Impact Factor: 3.033
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D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S
* A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics (475 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Sep 29; 362(4): 743-752.
Impact Factor: 4.89
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Cappiello M, Alterio V, Amodeo P, Del Corso A, Scaloni A, Pedone C, Moschini R, De Donatis GM, De Simone G, Mura U
* A new spot test for sulfhydryl-containing compounds (450 views)
Anal Biochem, 2006 Mar 14; 79(1-2): 610-611.
Impact Factor: 2.305
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Cappiello M, Alterio V, Amodeo P, Del Corso A, Scaloni A, Pedone C, Moschini R, De Donatis GM, De Simone G, Mura U
* Metal ion substitution in the catalytic site greatly affects the binding of sulfhydryl-containing compounds to leucyl aminopeptidase (723 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2006 Mar 14; 45(10): 3226-3234.
Impact Factor: 3.633
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Mannini R, Rivieccio V, D'Auria S, Tanfani F, Ausili A, Pedone C, Grimaldi G, Facchiano A
* Structure/function of KRAB repression domains: Structural properties of KRAB modules inferred from hydrodynamic, circular dichroism, and FTIR spectroscopic analyses (587 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Feb 15; 62(3): 604-616.
Impact Factor: 3.73
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Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S
* Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (391 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Feb 10; 356(1): 155-164.
Impact Factor: 4.89
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Pedone E, Saviano M, Bartolucci S, Rossi M, Ausili A, Scire A, Bertoli E, Tanfani F
* Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: A dynamic simulation and fourier transform infrared spectroscopic study (318 views)
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Impact Factor: 6.901
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Pedone E, Ren B, Ladenstein R, Rossi M, Bartolucci S
* Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase (390 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
Impact Factor: 3.26
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D'Ambrosio K, Kauffmann B, Rouhier N, Benedetti E, Jacquot JP, Aubry A, Corbier C
* Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione (304 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2003 Jun; 59: 1043-1045.
Impact Factor: 2.208
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Orru S, Vitagliano L, Esposito L, Mazzarella L, Marino G, Ruoppolo M
Effect of deamidation on folding of ribonuclease (385 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Dec; 9(12): 2577-2582.
Impact Factor: 3.869
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Del Vecchio S, Ciarmiello A, Salvatore M
Clinical imaging of multidrug resistance in cancer (361 views)
Q J Nucl Med (ISSN: 1124-3937, 1125-0135), 1999 Jun; 43(2): 125-131.
Impact Factor: 2.125
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Wink DA, Vodovotz Y, Grisham MB, DeGraff W, Cook JC, Pacelli R, Krishna M, Mitchell JB
Antioxidant effects of nitric oxide (351 views)
Method Enzymol (ISSN: 0076-6879, 1557-7988electronic), 1998; 301: 413-424.
Impact Factor: 2.823
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Cook JA, Krishna MC, Pacelli R, DeGraff W, Liebmann J, Mitchell JB, Russo A, Wink DA
Nitric oxide enhancement of melphalan-induced cytotoxicity (486 views)
Br J Cancer (ISSN: 0007-0920, 0007-0920print, 0007-0920linking), 1997 Sep; 76(3): 325-334.
Impact Factor: 2.938
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Wink DA, Cook JA, Kim SY, Vodovotz Y, Pacelli R, Krishna MC, Russo A, Mitchell JB, Jourd'heuil D, Miles AM, Grisham MB
Superoxide modulates the oxidation and nitrosation of thiols by nitric oxide-derived reactive intermediates (336 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 1997 Apr 25; 272(17): 11147-11151.
Impact Factor: 6.963
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Wink DA, Cook JA, Christodoulou D, Krishna MC, Pacelli R, Kim S, DeGraff W, Gamson J, Vodovotz Y, Russo A, Mitchell JB
Nitric oxide and some nitric oxide donor compounds enhance the cytotoxicity of cisplatin (472 views)
Nitric Oxide Biology And Chemistry (ISSN: 1089-8603), 1997 Feb; 1(1): 88-94.
Impact Factor: 2.151
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Wink DA, Cook JA, Pacelli R, DeGraff W, Gamson J, Liebmann J, Krishna MC, Mitchell JB
The effect of various nitric oxide-donor agents on hydrogen peroxide-mediated toxicity: A direct correlation between nitric oxide formation and protection (685 views)
Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 1996 Jul 15; 331(2): 241-248.
Impact Factor: 2.649
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Wink DA, Grisham MB, Miles AM, Nims RW, Krishna MC, Pacelli R, Teague D, Poore CM, Cook JA, Ford PC
Determination of selectivity of reactive nitrogen oxide species for various substrates (366 views)
Method Enzymol (ISSN: 0076-6879, 1557-7988electronic, 0076-6879linking), 1996; 268: 120-130.
Impact Factor: 2.435
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Wink DA, Cook JA, Pacelli R, Liebmann J, Krishna MC, Mitchell JB
Nitric oxide (NO) protects against cellular damage by reactive oxygen species (526 views)
Toxicology Letters (ISSN: 0378-4274), 1995 Dec; 82-3: 221-226.
Impact Factor: 1.128
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Pacelli R, Wink DA, Cook JA, Krishna MC, DeGraff W, Friedman N, Tsokos M, Samuni A, Mitchell JB
NITRIC-OXIDE POTENTIATES HYDROGEN PEROXIDE-INDUCED KILLING OF ESCHERICHIA-COLI (428 views)
Journal Of Experimental Medicine (ISSN: 0022-1007), 1995 Nov 1; 182(5): 1469-1479.
Impact Factor: 14.384
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Bonomo RP, De Flora A, Rizzarelli E, Santoro AM, Tabbì G, Tonetti M
Copper(II) complexes encapsulated in human red blood cells (587 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 1995 Sep; 59(4): 773-784.
Impact Factor: 1.342
View Export to BibTeX Export to EndNote
44 Records (44 excluding Abstracts).
Total impact factor: 183.876 (183.876 excluding Abstracts).
Total 5 year impact factor: 191.928 (191.928 excluding Abstracts).
Total impact factor: 183.876 (183.876 excluding Abstracts).
Total 5 year impact factor: 191.928 (191.928 excluding Abstracts).
613 views. Last view on Friday 24 March 2023, 0:51:33
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