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Volumn 7, Issue 1, 2014, Pages 101-120

High-resolution crystal structure and redox properties of chloroplastic triosephosphate isomerase from chlamydomonas reinhardtii

Author keywords

Thiol based redox regulation; Three dimensional structure; TIM barrel; Transnitrosylation; Triosephosphate isomerase

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); DISULFIDE; GLUTATHIONE DISULFIDE; HYDROGEN PEROXIDE; TRIOSEPHOSPHATE ISOMERASE;

EID: 84891810792     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/sst139     Document Type: Article
Times cited : (35)

References (98)
  • 1
    • 0344441463 scopus 로고    scopus 로고
    • Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: Evidence of conformational heterogeneity
    • Aparicio, R., Ferreira, S.T., and Polikarpov, I. (2003). Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. J. Mol. Biol. 334, 1023-1041.
    • (2003) J. Mol. Biol. , vol.334 , pp. 1023-1041
    • Aparicio, R.1    Ferreira, S.T.2    Polikarpov, I.3
  • 4
    • 0016810498 scopus 로고
    • Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data
    • Banner, D.W., Bloomer, A.C., Petsko, G.A., Phillips, D.C., Pogson, C.I., Wilson, I.A., Corran, P.H., Furth, A.J., Milman, J.D., Offord, R.E., et al. (1975). Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data. Nature. 255, 609-614.
    • (1975) Nature. , vol.255 , pp. 609-614
    • Banner, D.W.1    Bloomer, A.C.2    Petsko, G.A.3    Phillips, D.C.4    Pogson, C.I.5    Wilson, I.A.6    Corran, P.H.7    Furth, A.J.8    Milman, J.D.9    Offord, R.E.10
  • 5
    • 84864327019 scopus 로고    scopus 로고
    • Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro
    • Bedhomme, M., Adamo, M., Marchand, C.H., Couturier, J., Rouhier, N., Lemaire, S.D., Zaffagnini, M., and Trost, P. (2012). Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro. Biochem. J. 445, 337-347.
    • (2012) Biochem. J. , vol.445 , pp. 337-347
    • Bedhomme, M.1    Adamo, M.2    Marchand, C.H.3    Couturier, J.4    Rouhier, N.5    Lemaire, S.D.6    Zaffagnini, M.7    Trost, P.8
  • 7
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: Enzymatic mechanisms and cellular functions
    • Benhar, M., Forrester, M.T., and Stamler, J.S. (2009). Protein denitrosylation: enzymatic mechanisms and cellular functions. Nat. Rev. Mol. Cell Biol. 10, 721-732.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 8
    • 77955576782 scopus 로고    scopus 로고
    • Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach
    • Benhar, M., Thompson, J.W., Moseley, M.A., and Stamler, J.S. (2010). Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach. Biochemistry. 49, 6963-6969.
    • (2010) Biochemistry. , vol.49 , pp. 6963-6969
    • Benhar, M.1    Thompson, J.W.2    Moseley, M.A.3    Stamler, J.S.4
  • 10
    • 0027401730 scopus 로고
    • Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant
    • Borchert, T.V., Pratt, K., Zeelen, J.P., Callens, M., Noble, M.E., Opperdoes, F.R., Michels, P.A., and Wierenga, R.K. (1993). Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant. Eur. J. Biochem. 211, 703-710.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 703-710
    • Borchert, T.V.1    Pratt, K.2    Zeelen, J.P.3    Callens, M.4    Noble, M.E.5    Opperdoes, F.R.6    Michels, P.A.7    Wierenga, R.K.8
  • 13
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan, B.B., and Balmer, Y. (2005). Redox regulation: a broadening horizon. Annu. Rev. Plant Biol. 56, 187-220.
    • (2005) Annu. Rev. Plant Biol. , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 14
    • 77950347534 scopus 로고    scopus 로고
    • The plastid isoform of triose phosphate isomerase is required for the postgerminative transition from heterotrophic to autotrophic growth in Arabidopsis
    • Chen, M., and Thelen, J.J. (2010). The plastid isoform of triose phosphate isomerase is required for the postgerminative transition from heterotrophic to autotrophic growth in Arabidopsis. Plant Cell. 22, 77-90.
    • (2010) Plant Cell. , vol.22 , pp. 77-90
    • Chen, M.1    Thelen, J.J.2
  • 16
    • 33644682396 scopus 로고    scopus 로고
    • Stress-induced protein S-glutathionylation in Arabidopsis
    • Dixon, D.P., Skipsey, M., Grundy, N.M., and Edwards, R. (2005). Stress-induced protein S-glutathionylation in Arabidopsis. Plant Physiol. 138, 2233-2244.
    • (2005) Plant Physiol. , vol.138 , pp. 2233-2244
    • Dixon, D.P.1    Skipsey, M.2    Grundy, N.M.3    Edwards, R.4
  • 17
    • 78049288138 scopus 로고    scopus 로고
    • Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation
    • Doulias, P.T., Greene, J.L., Greco, T.M., Tenopoulou, M., Seeholzer, S.H., Dunbrack, R.L., and Ischiropoulos, H. (2010). Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation. Proc. Natl Acad. Sci. U S A. 107, 16958-16963.
    • (2010) Proc. Natl Acad. Sci. U S A. , vol.107 , pp. 16958-16963
    • Doulias, P.T.1    Greene, J.L.2    Greco, T.M.3    Tenopoulou, M.4    Seeholzer, S.H.5    Dunbrack, R.L.6    Ischiropoulos, H.7
  • 18
  • 21
    • 84855895599 scopus 로고    scopus 로고
    • Proteomics investigation of endogenous S-nitrosylation in Arabidopsis
    • Fares, A., Rossignol, M., and Peltier, J.B. (2011). Proteomics investigation of endogenous S-nitrosylation in Arabidopsis. Biochem. Biophys. Res. Commun. 416, 331-336.
    • (2011) Biochem. Biophys. Res. Commun. , vol.416 , pp. 331-336
    • Fares, A.1    Rossignol, M.2    Peltier, J.B.3
  • 23
    • 70049083635 scopus 로고    scopus 로고
    • Protein S-nitrosylation in health and disease: A current perspective
    • Foster, M.W., Hess, D.T., and Stamler, J.S. (2009). Protein S-nitrosylation in health and disease: a current perspective. Trends Mol. Med. 15, 391-404.
    • (2009) Trends Mol. Med. , vol.15 , pp. 391-404
    • Foster, M.W.1    Hess, D.T.2    Stamler, J.S.3
  • 25
    • 32244445145 scopus 로고    scopus 로고
    • SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures
    • Hao, G., Derakhshan, B., Shi, L., Campagne, F., and Gross, S.S. (2006). SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures. Proc. Natl Acad. Sci. U S A. 103, 1012-1017.
    • (2006) Proc. Natl Acad. Sci. U S A. , vol.103 , pp. 1012-1017
    • Hao, G.1    Derakhshan, B.2    Shi, L.3    Campagne, F.4    Gross, S.S.5
  • 26
    • 0028675654 scopus 로고
    • Chloroplast and cytosolic triosephosphate isomerases from spinach: Purification, microsequencing and cDNA cloning of the chloroplast enzyme
    • Henze, K., Schnarrenberger, C., Kellermann, J., and Martin, W. (1994). Chloroplast and cytosolic triosephosphate isomerases from spinach: purification, microsequencing and cDNA cloning of the chloroplast enzyme. Plant Mol. Biol. 26, 1961-1973.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1961-1973
    • Henze, K.1    Schnarrenberger, C.2    Kellermann, J.3    Martin, W.4
  • 27
    • 84856834347 scopus 로고    scopus 로고
    • Regulation by S-nitrosylation of protein post-translational modification
    • Hess, D.T., and Stamler, J.S. (2012). Regulation by S-nitrosylation of protein post-translational modification. J. Biol. Chem. 287, 4411-4418.
    • (2012) J. Biol. Chem. , vol.287 , pp. 4411-4418
    • Hess, D.T.1    Stamler, J.S.2
  • 29
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg, N. (2002). The biochemistry and physiology of S-nitrosothiols. Annu. Rev. Pharmacol. Toxicol. 42, 585-600.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 585-600
    • Hogg, N.1
  • 31
    • 0043199342 scopus 로고    scopus 로고
    • The sugar-metabolic enzymes aldolase and triose-phosphate isomerase are targets of glutathionylation in Arabidopsis thaliana: Detection using biotinylated glutathione
    • Ito, H., Iwabuchi, M., and Ogawa, K. (2003). The sugar-metabolic enzymes aldolase and triose-phosphate isomerase are targets of glutathionylation in Arabidopsis thaliana: detection using biotinylated glutathione. Plant Cell. Physiol. 44, 655-660.
    • (2003) Plant Cell. Physiol. , vol.44 , pp. 655-660
    • Ito, H.1    Iwabuchi, M.2    Ogawa, K.3
  • 32
    • 84878390747 scopus 로고    scopus 로고
    • Central carbon metabolism and electron transport in Chlamydomonas reinhardtii: Metabolic constraints for carbon partitioning between oil and starch
    • Johnson, X., and Alric, J. (2013). Central carbon metabolism and electron transport in Chlamydomonas reinhardtii: metabolic constraints for carbon partitioning between oil and starch. Eukaryot. Cell. 12, 776-793.
    • (2013) Eukaryot. Cell. , vol.12 , pp. 776-793
    • Johnson, X.1    Alric, J.2
  • 33
    • 0025015392 scopus 로고
    • Anatomy of a conformational change: Hinged 'lid' motion of the triosephosphate isomerase loop
    • Joseph, D., Petsko, G.A., and Karplus, M. (1990). Anatomy of a conformational change: hinged 'lid' motion of the triosephosphate isomerase loop. Science. 249, 1425-1428.
    • (1990) Science. , vol.249 , pp. 1425-1428
    • Joseph, D.1    Petsko, G.A.2    Karplus, M.3
  • 37
    • 0023428359 scopus 로고
    • Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei: A comparison with the rabbit muscle and yeast enzymes
    • Lambeir, A.M., Opperdoes, F.R., and Wierenga, R.K. (1987). Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei: a comparison with the rabbit muscle and yeast enzymes. Eur. J. Biochem. 168, 69-74.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 69-74
    • Lambeir, A.M.1    Opperdoes, F.R.2    Wierenga, R.K.3
  • 40
    • 84855263017 scopus 로고    scopus 로고
    • Nitric oxide and protein S-nitrosylation are integral to hydrogen peroxide-induced leaf cell death in rice
    • Lin, A., Wang, Y., Tang, J., Xue, P., Li, C., Liu, L., Hu, B., Yang, F., Loake, G.J., and Chu, C. (2012). Nitric oxide and protein S-nitrosylation are integral to hydrogen peroxide-induced leaf cell death in rice. Plant Physiol. 158, 451-464.
    • (2012) Plant Physiol. , vol.158 , pp. 451-464
    • Lin, A.1    Wang, Y.2    Tang, J.3    Xue, P.4    Li, C.5    Liu, L.6    Hu, B.7    Yang, F.8    Loake, G.J.9    Chu, C.10
  • 41
    • 79957441981 scopus 로고    scopus 로고
    • The disulfide proteome and other reactive cysteine proteomes: Analysis and functional significance
    • Lindahl, M., Mata-Cabana, A., and Kieselbach, T. (2011). The disulfide proteome and other reactive cysteine proteomes: analysis and functional significance. Antioxid. Redox Signal. 14, 2581-2642.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 2581-2642
    • Lindahl, M.1    Mata-Cabana, A.2    Kieselbach, T.3
  • 42
    • 20344377809 scopus 로고    scopus 로고
    • Proteomic identification of S-nitrosylated proteins in Arabidopsis
    • Lindermayr, C., Saalbach, G., and Durner, J. (2005). Proteomic identification of S-nitrosylated proteins in Arabidopsis. Plant Physiol. 137, 921-930.
    • (2005) Plant Physiol. , vol.137 , pp. 921-930
    • Lindermayr, C.1    Saalbach, G.2    Durner, J.3
  • 44
    • 0032709104 scopus 로고    scopus 로고
    • The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures
    • Maes, D., Zeelen, J.P., Thanki, N., Beaucamp, N., Alvarez, M., Thi, M.H., Backmann, J., Martial, J.A., Wyns, L., Jaenicke, R., et al. (1999). The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures. Proteins. 37, 441-453.
    • (1999) Proteins. , vol.37 , pp. 441-453
    • Maes, D.1    Zeelen, J.P.2    Thanki, N.3    Beaucamp, N.4    Alvarez, M.5    Thi, M.H.6    Backmann, J.7    Martial, J.A.8    Wyns, L.9    Jaenicke, R.10
  • 45
    • 0037067778 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum triose-phosphate isomerase by chemical modification of an interface cysteine: Electrospray ionization mass spectrometric analysis of differential cysteine reactivities
    • Maithal, K., Ravindra, G., Balaram, H., and Balaram, P. (2002). Inhibition of Plasmodium falciparum triose-phosphate isomerase by chemical modification of an interface cysteine: electrospray ionization mass spectrometric analysis of differential cysteine reactivities. J. Biol. Chem. 277, 25106-25114.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25106-25114
    • Maithal, K.1    Ravindra, G.2    Balaram, H.3    Balaram, P.4
  • 46
    • 0028298146 scopus 로고
    • Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution: Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme
    • Mande, S.C., Mainfroid, V., Kalk, K.H., Goraj, K., Martial, J.A., and Hol, W.G. (1994). Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution: triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme. Protein Sci. 3, 810-821.
    • (1994) Protein Sci. , vol.3 , pp. 810-821
    • Mande, S.C.1    Mainfroid, V.2    Kalk, K.H.3    Goraj, K.4    Martial, J.A.5    Hol, W.G.6
  • 48
    • 84870716652 scopus 로고    scopus 로고
    • S-nitrosothiols and the S-nitrosoproteome of the cardiovascular system
    • Maron, B.A., Tang, S.S., and Loscalzo, J. (2013). S-nitrosothiols and the S-nitrosoproteome of the cardiovascular system. Antioxid. Redox Signal. 18, 270-287.
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 270-287
    • Maron, B.A.1    Tang, S.S.2    Loscalzo, J.3
  • 49
    • 33744502382 scopus 로고    scopus 로고
    • Structure of a high-resolution crystal form of human triosephosphate isomerase: Improvement of crystals using the gel-tube method
    • Maruki, R., Kinoshita, T., Warizaya, M., Nakajima, H., and Nishimura, S. (2005). Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method. Acta Crystallogr. Sect. F. 61, 346-349.
    • (2005) Acta Crystallogr. Sect. F. , vol.61 , pp. 346-349
    • Maruki, R.1    Kinoshita, T.2    Warizaya, M.3    Nakajima, H.4    Nishimura, S.5
  • 50
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, BW. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 54
    • 20444479515 scopus 로고    scopus 로고
    • Diatom plastids possess a phosphoribulokinase with an altered regulation and no oxidative pentose phosphate pathway
    • Michels, A.K., Wedel, N., and Kroth, P.G. (2005). Diatom plastids possess a phosphoribulokinase with an altered regulation and no oxidative pentose phosphate pathway. Plant Physiol. 137, 911-920.
    • (2005) Plant Physiol. , vol.137 , pp. 911-920
    • Michels, A.K.1    Wedel, N.2    Kroth, P.G.3
  • 55
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • Mieyal, J.J., Gallogly, M.M., Qanungo, S., Sabens. E.A., and Shelton, M.D. (2008). Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signal. 10, 1941-1988.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5
  • 56
    • 84856717563 scopus 로고    scopus 로고
    • Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay
    • M111.013441
    • Murray, C.I., Uhrigshardt, H., O'Meally, R.N., Cole, R.N., and Van Eyk, J.E. (2012). Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay. Mol. Cell. Proteomics. 11, M111.013441.
    • (2012) Mol. Cell. Proteomics. , pp. 11
    • Murray, C.I.1    Uhrigshardt, H.2    O'Meally, R.N.3    Cole, R.N.4    Van Eyk, J.E.5
  • 58
    • 69249205644 scopus 로고    scopus 로고
    • Redox regulation of chloroplastic glucose-6-phosphate dehydrogenase: A new role for f-type thioredoxin
    • Née, G., Zaffagnini, M., Trost, P., and Issakidis-Bourguet, E. (2009). Redox regulation of chloroplastic glucose-6-phosphate dehydrogenase: a new role for f-type thioredoxin. FEBS Lett. 583, 2827-2832.
    • (2009) FEBS Lett. , vol.583 , pp. 2827-2832
    • Née, G.1    Zaffagnini, M.2    Trost, P.3    Issakidis-Bourguet, E.4
  • 59
    • 0025882523 scopus 로고
    • The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes
    • Noble, M.E., Wierenga, R.K., Lambeir, A.M., Opperdoes, F.R., Thunnissen, A.M., Kalk, K.H., Groendijk, H., and Hol, W.G. (1991). The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. Proteins. 10, 50-56.
    • (1991) Proteins. , vol.10 , pp. 50-56
    • Noble, M.E.1    Wierenga, R.K.2    Lambeir, A.M.3    Opperdoes, F.R.4    Thunnissen, A.M.5    Kalk, K.H.6    Groendijk, H.7    Hol, W.G.8
  • 61
  • 62
    • 0025276041 scopus 로고
    • Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase
    • Pompliano, D.L., Peyman, A., and Knowles, J.R. (1990). Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase. Biochemistry. 29, 3186-3194.
    • (1990) Biochemistry. , vol.29 , pp. 3186-3194
    • Pompliano, D.L.1    Peyman, A.2    Knowles, J.R.3
  • 64
    • 84868206533 scopus 로고    scopus 로고
    • Understanding the pK(a) of redox cysteines: The key role of hydrogen bonding
    • Roos, G., Foloppe, N., and Messens, J. (2013). Understanding the pK(a) of redox cysteines: the key role of hydrogen bonding. Antioxid. Redox Signal. 18, 94-127.
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 94-127
    • Roos, G.1    Foloppe, N.2    Messens, J.3
  • 65
    • 42949085825 scopus 로고    scopus 로고
    • The role of glutathione in photosynthetic organisms: Emerging functions for glutaredoxins and glutathionylation
    • Rouhier, N., Lemaire, S.D., and Jacquot, J.P. (2008). The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation. Annu. Rev. Plant Biol. 59, 143-166.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 143-166
    • Rouhier, N.1    Lemaire, S.D.2    Jacquot, J.P.3
  • 67
    • 0015115188 scopus 로고
    • Studies on human triosephosphate isomerase. I. Isolation and Properties of the Enzyme from Erythrocytes
    • Rozacky, E.E., Sawyer, T.H., Barton, R.A., and Gracy, R.W. (1971). Studies on human triosephosphate isomerase. I. Isolation and properties of the enzyme from erythrocytes. Arch. Biochem. Biophys. 146, 312-320.
    • (1971) Arch. Biochem. Biophys. , vol.146 , pp. 312-320
    • Rozacky, E.E.1    Sawyer, T.H.2    Barton, R.A.3    Gracy, R.W.4
  • 68
    • 0035967856 scopus 로고    scopus 로고
    • Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics
    • Rozovsky, S., Jog, G., Tong, L., and McDermott, A.E. (2001). Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. J. Mol. Biol. 310, 271-280.
    • (2001) J. Mol. Biol. , vol.310 , pp. 271-280
    • Rozovsky, S.1    Jog, G.2    Tong, L.3    McDermott, A.E.4
  • 69
    • 0032922625 scopus 로고    scopus 로고
    • Regulation of chloroplast enzyme activities by thioredoxins: Activation or relief from inhibition?
    • Ruelland, E., and Miginiac-Maslow, M. (1999). Regulation of chloroplast enzyme activities by thioredoxins: activation or relief from inhibition? Trends Plant Sci. 4, 136-141.
    • (1999) Trends Plant Sci. , vol.4 , pp. 136-141
    • Ruelland, E.1    Miginiac-Maslow, M.2
  • 70
    • 79961124367 scopus 로고    scopus 로고
    • Revisiting the mechanism of the triosephosphate isomerase reaction: The role of the fully conserved glutamic acid 97 residue
    • Samanta, M., Murthy, M.R., Balaram, H., and Balaram, P. (2011). Revisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residue. Chembiochem. 12, 1886-1896.
    • (2011) Chembiochem. , vol.12 , pp. 1886-1896
    • Samanta, M.1    Murthy, M.R.2    Balaram, H.3    Balaram, P.4
  • 71
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system of oxygenic photosynthesis
    • Schürmann, P., and Buchanan, B.B. (2008). The ferredoxin/thioredoxin system of oxygenic photosynthesis. Antioxid. Redox Signal. 10, 1235-1274.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1235-1274
    • Schürmann, P.1    Buchanan, B.B.2
  • 72
    • 84860497776 scopus 로고    scopus 로고
    • The role of thioredoxin in the regulation of cellular processes by S-nitrosylation
    • Sengupta, R., and Holmgren, A. (2011). The role of thioredoxin in the regulation of cellular processes by S-nitrosylation. Biochim. Biophys. Acta. 1820, 689-700.
    • (2011) Biochim. Biophys. Acta. , vol.1820 , pp. 689-700
    • Sengupta, R.1    Holmgren, A.2
  • 73
    • 85045352324 scopus 로고    scopus 로고
    • Characterization of stress and methylglyoxal inducible triose phosphate isomerase (OscTPI) from rice
    • Sharma, S., Mustafiz, A., Singla-Pareek, S.L., Shankar Srivastava, P., and Sopory, S.K. (2012). Characterization of stress and methylglyoxal inducible triose phosphate isomerase (OscTPI) from rice. Plant Signal. Behav. 7, 1337-1345.
    • (2012) Plant Signal. Behav. , vol.7 , pp. 1337-1345
    • Sharma, S.1    Mustafiz, A.2    Singla-Pareek, S.L.3    Shankar Srivastava, P.4    Sopory, S.K.5
  • 74
    • 0042261992 scopus 로고    scopus 로고
    • Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae
    • Shenton, D., and Grant, C.M. (2003). Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. Biochem. J. 374, 513-519.
    • (2003) Biochem. J. , vol.374 , pp. 513-519
    • Shenton, D.1    Grant, C.M.2
  • 75
    • 4544325179 scopus 로고    scopus 로고
    • Thioredoxin Ch1 of Chlamydomonas reinhardtii displays an unusual resistance toward one-electron oxidation
    • Sicard-Roselli, C., Lemaire, S., Jacquot, J.P., Favaudon, V., Marchand, C., and Houée-Levin, C. (2004). Thioredoxin Ch1 of Chlamydomonas reinhardtii displays an unusual resistance toward one-electron oxidation. Eur. J. Biochem. 271, 3481-3487.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3481-3487
    • Sicard-Roselli, C.1    Lemaire, S.2    Jacquot, J.P.3    Favaudon, V.4    Marchand, C.5    Houée-Levin, C.6
  • 76
    • 0035854727 scopus 로고    scopus 로고
    • Synthetic peptides as inactivators of multimeric enzymes: Inhibition of Plasmodium falciparum triosephosphate isomerase by interface peptides
    • Singh, S.K., Maithal, K., Balaram, H., and Balaram, P. (2001). Synthetic peptides as inactivators of multimeric enzymes: inhibition of Plasmodium falciparum triosephosphate isomerase by interface peptides. FEBS Lett. 501, 19-23.
    • (2001) FEBS Lett. , vol.501 , pp. 19-23
    • Singh, S.K.1    Maithal, K.2    Balaram, H.3    Balaram, P.4
  • 77
    • 84861065569 scopus 로고    scopus 로고
    • Sirover, subcellular dynamics of multifunctional protein regulation: Mechanisms of GAPDH intracellular translocation
    • Sirover, M.A. (2012). Sirover, subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation. J. Cell. Biochem. 113, 2193-2200.
    • (2012) J. Cell. Biochem. , vol.113 , pp. 2193-2200
    • Sirover, M.A.1
  • 79
    • 0030956929 scopus 로고    scopus 로고
    • (S) NO signals: Translocation, regulation, and a consensus motif
    • Stamler, J.S., Toone, E.J., Lipton, S.A., and Sucher, N.J. (1997). (S) NO signals: translocation, regulation, and a consensus motif. Neuron. 18, 691-696.
    • (1997) Neuron. , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 80
    • 84868503178 scopus 로고    scopus 로고
    • Oxidative and nitrosative-based signaling and associated post-translational modifications orchestrate the acclimation of citrus plants to salinity stress
    • Tanou, G., Filippou, P., Belghazi, M., Job, D., Diamantidis, G., Fotopoulos, V., and Molassiotis, A. (2012). Oxidative and nitrosative-based signaling and associated post-translational modifications orchestrate the acclimation of citrus plants to salinity stress. Plant J. 72, 585-599.
    • (2012) Plant J. , vol.72 , pp. 585-599
    • Tanou, G.1    Filippou, P.2    Belghazi, M.3    Job, D.4    Diamantidis, G.5    Fotopoulos, V.6    Molassiotis, A.7
  • 81
    • 71949124535 scopus 로고    scopus 로고
    • Proteomics reveals the overlapping roles of hydrogen peroxide and nitric oxide in the acclimation of citrus plants to salinity
    • Tanou, G., Job, C., Rajjou, L., Arc, E., Belghazi, M., Diamantidis, G., Molassiotis, A., and Job, D. (2009). Proteomics reveals the overlapping roles of hydrogen peroxide and nitric oxide in the acclimation of citrus plants to salinity. Plant J. 60, 795-804.
    • (2009) Plant J. , vol.60 , pp. 795-804
    • Tanou, G.1    Job, C.2    Rajjou, L.3    Arc, E.4    Belghazi, M.5    Diamantidis, G.6    Molassiotis, A.7    Job, D.8
  • 82
    • 33749840484 scopus 로고    scopus 로고
    • Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3- phosphate dehydrogenase: Autonomous vs. CP12-dependent mechanisms
    • Trost, P., Fermani, S., Marri, L., Zaffagnini, M., Falini, G., Scagliarini S., Pupillo, P., and Sparla, F. (2006). Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: autonomous vs. CP12-dependent mechanisms. Photosynth. Res. 89, 263-275.
    • (2006) Photosynth. Res. , vol.89 , pp. 263-275
    • Trost, P.1    Fermani, S.2    Marri, L.3    Zaffagnini, M.4    Falini, G.5    Scagliarini, S.6    Pupillo, P.7    Sparla, F.8
  • 84
    • 0031570683 scopus 로고    scopus 로고
    • Triosephosphate isomerase from Plasmodium falciparum: The crystal structure provides insights into antimalarial drug design
    • Velanker, S.S., Ray, S.S., Gokhale, R.S., Suma, S., Balaram, H., Balaram, P., and Murthy, M.R.N. (1997). Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. Structure. 5, 751-761.
    • (1997) Structure. , vol.5 , pp. 751-761
    • Velanker, S.S.1    Ray, S.S.2    Gokhale, R.S.3    Suma, S.4    Balaram, H.5    Balaram, P.6    Murthy, M.R.N.7
  • 85
    • 84877044940 scopus 로고    scopus 로고
    • Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots
    • Vescovi, M., Zaffagnini, M., Festa, M., Trost, P., Lo Schiavo, F., and Costa, A. (2013). Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots. Plant Physiol. 162, 333-346.
    • (2013) Plant Physiol. , vol.162 , pp. 333-346
    • Vescovi, M.1    Zaffagnini, M.2    Festa, M.3    Trost, P.4    Lo Schiavo, F.5    Costa, A.6
  • 86
  • 87
    • 0026681342 scopus 로고
    • Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues
    • Wierenga, R.K., Borchert, T.V., and Noble, M.E. (1992a). Crystallographic binding studies with triosephosphate isomerases: conformational changes induced by substrate and substrate-analogues. FEBS Lett. 307, 34-39.
    • (1992) FEBS Lett. , vol.307 , pp. 34-39
    • Wierenga, R.K.1    Borchert, T.V.2    Noble, M.E.3
  • 88
  • 89
    • 0026519169 scopus 로고
    • Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase
    • Wierenga, R.K., Noble, M.E., and Davenport, R.C. (1992b). Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase. J. Mol. Biol. 224, 1115-1126.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1115-1126
    • Wierenga, R.K.1    Noble, M.E.2    Davenport, R.C.3
  • 90
    • 0025785056 scopus 로고
    • Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate: A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex
    • Wierenga, R.K., Noble, M.E., Vriend, G., Nauche, S., and Hol, W.G. (1991). Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate: a comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex. J. Mol. Biol. 220, 995-1015.
    • (1991) J. Mol. Biol. , vol.220 , pp. 995-1015
    • Wierenga, R.K.1    Noble, M.E.2    Vriend, G.3    Nauche, S.4    Hol, W.G.5
  • 91
    • 0029000872 scopus 로고
    • Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated
    • Williams, J.C., and McDermott, A.E. (1995). Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated. Biochemistry. 34, 8309-8319.
    • (1995) Biochemistry. , vol.34 , pp. 8309-8319
    • Williams, J.C.1    McDermott, A.E.2
  • 92
    • 0037628370 scopus 로고    scopus 로고
    • Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics
    • Wong, J.H., Balmer, Y., Cai, N., Tanaka, C.K., Vensel, W.H., Hurkman, W.J., and Buchanan, B.B. (2003). Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics. FEBS Lett. 547, 151-156.
    • (2003) FEBS Lett. , vol.547 , pp. 151-156
    • Wong, J.H.1    Balmer, Y.2    Cai, N.3    Tanaka, C.K.4    Vensel, W.H.5    Hurkman, W.J.6    Buchanan, B.B.7
  • 96
    • 44049097906 scopus 로고    scopus 로고
    • Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin
    • Zaffagnini, M., Michelet, L., Massot, V., Trost, P., and Lemaire, S.D. (2008). Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin. J. Biol. Chem. 283, 8868-8876.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8868-8876
    • Zaffagnini, M.1    Michelet, L.2    Massot, V.3    Trost, P.4    Lemaire, S.D.5
  • 97
    • 84881253817 scopus 로고    scopus 로고
    • Mechanisms of nitrosylation and denitrosylation of cytoplasmic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana
    • 7 June, 10.1074/jbc.M113.475467
    • Zaffagnini, M., Morisse, S., Bedhomme, M., Marchand, C.H., Festa, M., Rouhier, N., Lemaire, S.D., and Trost, P. (2013). Mechanisms of nitrosylation and denitrosylation of cytoplasmic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana. J. Biol. Chem. 7 June, 10.1074/jbc.M113.475467.
    • (2013) J. Biol. Chem.
    • Zaffagnini, M.1    Morisse, S.2    Bedhomme, M.3    Marchand, C.H.4    Festa, M.5    Rouhier, N.6    Lemaire, S.D.7    Trost, P.8
  • 98
    • 0028934478 scopus 로고
    • Terminal marking of avian triosephosphate isomerases by deamidation and oxidation
    • Zhang, Y., Yüksel, K.U., and Gracy, R.W. (1995). Terminal marking of avian triosephosphate isomerases by deamidation and oxidation. Arch. Biochem. Biophys. 317, 112-120.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 112-120
    • Zhang, Y.1    Yüksel, K.U.2    Gracy, R.W.3


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