메뉴 건너뛰기




Volumn 376, Issue 4, 2008, Pages 700-705

Identification of Fructose-1,6-bisphosphate aldolase cytosolic class I as an NMH7 MADS domain associated protein

Author keywords

Aldolase; MADS domain proteins; Medicago sativa; Moonlighting protein; Symbiosis

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE; MADS DOMAIN PROTEIN; PROTEIN NMH7; UNCLASSIFIED DRUG;

EID: 53449085785     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.09.064     Document Type: Article
Times cited : (18)

References (23)
  • 1
    • 0141991995 scopus 로고    scopus 로고
    • Role of MADS box proteins and their cofactors in combinatorial control of gene expression and cell development
    • Messenguy F., and Dubois E. Role of MADS box proteins and their cofactors in combinatorial control of gene expression and cell development. Gene 16 (2003) 1-21
    • (2003) Gene , vol.16 , pp. 1-21
    • Messenguy, F.1    Dubois, E.2
  • 2
    • 33846890433 scopus 로고    scopus 로고
    • Serum response factor binding sites differ in three human cell types
    • Cooper S.J., Trinklein N.D., Nguyen L., and Myers R.M. Serum response factor binding sites differ in three human cell types. Genome Res. 17 (2007) 136-144
    • (2007) Genome Res. , vol.17 , pp. 136-144
    • Cooper, S.J.1    Trinklein, N.D.2    Nguyen, L.3    Myers, R.M.4
  • 3
    • 0035542945 scopus 로고    scopus 로고
    • Ngl9: a third MADS box gene expressed in alfalfa root nodules
    • Zucchero J.C., Caspi J.C., and Dunn K. Ngl9: a third MADS box gene expressed in alfalfa root nodules. Mol. Plant Microbe Interact. 14 (2001) 1463-1467
    • (2001) Mol. Plant Microbe Interact. , vol.14 , pp. 1463-1467
    • Zucchero, J.C.1    Caspi, J.C.2    Dunn, K.3
  • 5
    • 0035834601 scopus 로고    scopus 로고
    • Floral Transcription Factor AGAMOUS Interacts in vitro with a leucine-rich repeat and an acid phosphatase protein complex
    • Gamboa A., Páez-Valencia J., Acevedo F., Vazquez-Moreno L., and Alvarez-Buylla R.E. Floral Transcription Factor AGAMOUS Interacts in vitro with a leucine-rich repeat and an acid phosphatase protein complex. Biochem. Biophys. Res. Commun. 288 (2001) 1018-1026
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 1018-1026
    • Gamboa, A.1    Páez-Valencia, J.2    Acevedo, F.3    Vazquez-Moreno, L.4    Alvarez-Buylla, R.E.5
  • 6
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., and Mann M. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68 (1996) 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 7
    • 0037444512 scopus 로고    scopus 로고
    • Fast-response proteomics by accelerated in-gel digestion of proteins
    • Havlis J., Thomas H., Sebela M., and Shevchenko A. Fast-response proteomics by accelerated in-gel digestion of proteins. Anal. Chem. 75 (2003) 1300-1306
    • (2003) Anal. Chem. , vol.75 , pp. 1300-1306
    • Havlis, J.1    Thomas, H.2    Sebela, M.3    Shevchenko, A.4
  • 8
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A., Nesvizhskii A.I., Kolker E., and Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74 (2002) 5383-5392
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 9
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii A.I., Keller A., Kolker E., and Aebersold R. A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75 (2003) 4646-4658
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 10
    • 0842267072 scopus 로고    scopus 로고
    • Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70
    • Matambo T.S., Odunuga O.O., Boshoff A., and Blatch G.L. Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70. Protein Expr. Purif. 33 (2004) 214-222
    • (2004) Protein Expr. Purif. , vol.33 , pp. 214-222
    • Matambo, T.S.1    Odunuga, O.O.2    Boshoff, A.3    Blatch, G.L.4
  • 11
    • 26844451007 scopus 로고    scopus 로고
    • Both chloroplastic and cytosolic phosphofructoaldolase isozymes are present in the pea leaf nucleus
    • Anderson L.E., Ringenberg M.R., Brown V.K., and Carol A.A. Both chloroplastic and cytosolic phosphofructoaldolase isozymes are present in the pea leaf nucleus. Protoplasma 225 (2005) 235-242
    • (2005) Protoplasma , vol.225 , pp. 235-242
    • Anderson, L.E.1    Ringenberg, M.R.2    Brown, V.K.3    Carol, A.A.4
  • 12
    • 0017719153 scopus 로고
    • Kinetics of reactivation of rabbit muscle aldolase after denaturation and dissociation in various solvent media
    • Gerschitz J., Rudolph R., and Jaenicke R. Kinetics of reactivation of rabbit muscle aldolase after denaturation and dissociation in various solvent media. Biophys. Struct. Mech. 3 (1977) 291-302
    • (1977) Biophys. Struct. Mech. , vol.3 , pp. 291-302
    • Gerschitz, J.1    Rudolph, R.2    Jaenicke, R.3
  • 14
    • 0029444684 scopus 로고
    • Class I aldolases: substrate specificity, mechanism, inhibitors and structural aspects
    • Gefflaut T., Blonski C., Perie J., and Willson M. Class I aldolases: substrate specificity, mechanism, inhibitors and structural aspects. Prog. Biophys. Mol. Biol. 63 (1995) 301-340
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 301-340
    • Gefflaut, T.1    Blonski, C.2    Perie, J.3    Willson, M.4
  • 15
    • 0029975931 scopus 로고    scopus 로고
    • The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants
    • Wang J., Morris A.J., Tolan D.R., and Pagliaro L. The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants. J. Biol. Chem. 271 (1996) 6861-6865
    • (1996) J. Biol. Chem. , vol.271 , pp. 6861-6865
    • Wang, J.1    Morris, A.J.2    Tolan, D.R.3    Pagliaro, L.4
  • 16
    • 18244397436 scopus 로고    scopus 로고
    • Aldolases A and C are ribonucleolytic components of a neuronal complex that regulates the stability of the light-neurofilament mRNA
    • Cañete-Soler R., Reddy K.S., Tolan D.R., and Zhai J. Aldolases A and C are ribonucleolytic components of a neuronal complex that regulates the stability of the light-neurofilament mRNA. J. Neurosci. 27 (2005) 4353-4364
    • (2005) J. Neurosci. , vol.27 , pp. 4353-4364
    • Cañete-Soler, R.1    Reddy, K.S.2    Tolan, D.R.3    Zhai, J.4
  • 17
    • 0036659906 scopus 로고    scopus 로고
    • Band 3 is an anchor protein and a target for SHP-2 tyrosyne phosphatase in human erythrocytes
    • Bordin L., Brunati A.M., Donella-Deana A., Baggio B., Toninello A., and Clari G. Band 3 is an anchor protein and a target for SHP-2 tyrosyne phosphatase in human erythrocytes. Blood 100 (2002) 276-282
    • (2002) Blood , vol.100 , pp. 276-282
    • Bordin, L.1    Brunati, A.M.2    Donella-Deana, A.3    Baggio, B.4    Toninello, A.5    Clari, G.6
  • 18
    • 43249089827 scopus 로고    scopus 로고
    • Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant
    • Sherawat M., Tolan D.R., and Allen K.N. Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant. Acta Crystallogr. D: Biol. Crystallogr. 64 (2008) 543-550
    • (2008) Acta Crystallogr. D: Biol. Crystallogr. , vol.64 , pp. 543-550
    • Sherawat, M.1    Tolan, D.R.2    Allen, K.N.3
  • 20
    • 34447098032 scopus 로고    scopus 로고
    • Colocalization of aldolase and FBPase in cytoplasm and nucleus of cardiomyocytes
    • Mamczur P., Dus D., and Dzugaj A. Colocalization of aldolase and FBPase in cytoplasm and nucleus of cardiomyocytes. Cell Biol. Int. 31 (2007) 1122-1130
    • (2007) Cell Biol. Int. , vol.31 , pp. 1122-1130
    • Mamczur, P.1    Dus, D.2    Dzugaj, A.3
  • 21
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the Histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • Zheng L., Roeder R.G., and Luo Y. S phase activation of the Histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 114 (2003) 255-266
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3
  • 22
    • 33747463644 scopus 로고    scopus 로고
    • Metabolite profiles of nodulated alfalfa plants indicate that distinct stages of nodules organogenesis are accompanied by global physiological adaptations
    • Barsch A., Tellström V., Patschlkowski T., Küster H., and Niehaus K. Metabolite profiles of nodulated alfalfa plants indicate that distinct stages of nodules organogenesis are accompanied by global physiological adaptations. Mol. Plant Microbe Interact. 19 (2006) 998-1013
    • (2006) Mol. Plant Microbe Interact. , vol.19 , pp. 998-1013
    • Barsch, A.1    Tellström, V.2    Patschlkowski, T.3    Küster, H.4    Niehaus, K.5
  • 23
    • 0033580846 scopus 로고    scopus 로고
    • Aldolase mediates the association of F-actine with the insuline-responsive glucose transporter GLUT-4
    • Kao A.W., Noda Y., Johnson J.H., Pessin J.E., and Saltiel A.R. Aldolase mediates the association of F-actine with the insuline-responsive glucose transporter GLUT-4. J. Biol. Chem. 274 (1999) 17742-17747
    • (1999) J. Biol. Chem. , vol.274 , pp. 17742-17747
    • Kao, A.W.1    Noda, Y.2    Johnson, J.H.3    Pessin, J.E.4    Saltiel, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.