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Volumn 1, Issue , 2015, Pages

ERRATUM: Degradation of potent Rubisco inhibitor by selective sugar phosphatase (Nature Plants, (2015), 1, 14002, 10.1038/nplants.2014.2);Degradation of potent Rubisco inhibitor by selective sugar phosphatase

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EID: 84937120326     PISSN: None     EISSN: 20550278     Source Type: Journal    
DOI: 10.1038/NPLANTS.2015.6     Document Type: Erratum
Times cited : (48)

References (28)
  • 1
    • 0037001967 scopus 로고    scopus 로고
    • Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme
    • Spreitzer, R. J. & Salvucci, M. E. Rubisco: structure, regulatory interactions, and possibilities for a better enzyme. Ann. Rev. Plant Biol. 53, 449-475 (2002).
    • (2002) Ann. Rev. Plant Biol , vol.53 , pp. 449-475
    • Spreitzer, R.J.1    Salvucci, M.E.2
  • 3
    • 84875734663 scopus 로고    scopus 로고
    • Rubisco activity and regulation as targets for crop improvement
    • Parry, M. A. J. et al. Rubisco activity and regulation as targets for crop improvement. J. Exp. Bot. 64, 717-730 (2013).
    • (2013) J. Exp. Bot , vol.64 , pp. 717-730
    • Parry, M.A.J.1
  • 4
    • 33750550255 scopus 로고    scopus 로고
    • Catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies
    • Pearce, F. G. Catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies. Biochem. J. 399, 525-534 (2006).
    • (2006) Biochem. J , vol.399 , pp. 525-534
    • Pearce, F.G.1
  • 5
    • 0037232721 scopus 로고    scopus 로고
    • Rubisco activase - Rubisco's catalytic chaperone
    • Portis, A. R. Jr Rubisco activase - Rubisco's catalytic chaperone. Photosynth. Res. 75, 11-27 (2003).
    • (2003) Photosynth. Res , vol.75 , pp. 11-27
    • Portis, A.R.1
  • 7
    • 0031023769 scopus 로고    scopus 로고
    • Analysis of the cbbXYZ operon in Rhodobacter sphaeroides
    • Gibson, J. L. & Tabita, F. R. Analysis of the cbbXYZ operon in Rhodobacter sphaeroides. J. Bacteriol. 179, 663-669 (1997).
    • (1997) J. Bacteriol , vol.179 , pp. 663-669
    • Gibson, J.L.1    Tabita, F.R.2
  • 8
    • 0028116826 scopus 로고
    • Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search
    • Koonin, E. V. & Tatusov, R. L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 244, 125-132 (1994).
    • (1994) J. Mol. Biol , vol.244 , pp. 125-132
    • Koonin, E.V.1    Tatusov, R.L.2
  • 9
    • 77953149231 scopus 로고    scopus 로고
    • AT-CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins
    • Ferro, M. et al. AT-CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins. Mol. Cell. Proteomics 9, 1063-1084 (2010).
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1063-1084
    • Ferro, M.1
  • 10
    • 44349099751 scopus 로고    scopus 로고
    • Sorting signals, N-terminal modifications and abundance of the chloroplast proteome
    • Zybailov, B. et al. Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS ONE 3, e1994 (2008).
    • (2008) PLoS ONE , vol.3 , pp. e1994
    • Zybailov, B.1
  • 11
    • 0006918387 scopus 로고
    • Photosynthesis and ribulose 15-bisphosphate levels in intact chloroplasts
    • Sicher, R. C. & Jensen, R. G. Photosynthesis and ribulose 1,5-bisphosphate levels in intact chloroplasts. Plant Physiol. 64, 880-883 (1979).
    • (1979) Plant Physiol , vol.64 , pp. 880-883
    • Sicher, R.C.1    Jensen, R.G.2
  • 12
    • 84857864015 scopus 로고    scopus 로고
    • 2-carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: Evidence for a wider role in plant Rubisco regulation
    • Andralojc, P. J. et al. 2-carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation. Biochem. J. 442, 733-742 (2012).
    • (2012) Biochem. J , vol.442 , pp. 733-742
    • Andralojc, P.J.1
  • 13
    • 0242585345 scopus 로고    scopus 로고
    • The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction
    • Lahiri, S. D., Zhang, G., Dunaway-Mariano, D. & Allen, K. N. The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction. Science 299, 2067-2071 (2003).
    • (2003) Science , vol.299 , pp. 2067-2071
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 14
    • 64549129548 scopus 로고    scopus 로고
    • Analysis of the structural determinants underlying discrimination between substrate and solvent in β-phosphoglucomutase catalysis
    • Dai, J. et al. Analysis of the structural determinants underlying discrimination between substrate and solvent in β-phosphoglucomutase catalysis. Biochem. 48, 1984-1995 (2009).
    • (2009) Biochem , vol.48 , pp. 1984-1995
    • Dai, J.1
  • 15
    • 77949537262 scopus 로고    scopus 로고
    • Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes
    • Baxter, N. J. et al. Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes. Proc. Natl Acad. Sci. USA 107, 4555-4560 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 4555-4560
    • Baxter, N.J.1
  • 16
    • 0037008092 scopus 로고    scopus 로고
    • Caught in the act: The structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis
    • Lahiri, S. D., Zhang, G., Dunaway-Mariano, D. & Allen, K. N. Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis. Biochemistry 41, 8351-8359 (2002).
    • (2002) Biochemistry , vol.41 , pp. 8351-8359
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 17
    • 0026631188 scopus 로고
    • Reversible inactivation and characterization of purified inactivated form i ribulose 1,5-bisphosphate carboxylase/oxygenase of Rhodobacter sphaeroides
    • Wang, X. & Tabita, F. R. Reversible inactivation and characterization of purified inactivated form I ribulose 1,5-bisphosphate carboxylase/oxygenase of Rhodobacter sphaeroides. J. Bacteriol. 174, 3593-3600 (1992).
    • (1992) J. Bacteriol , vol.174 , pp. 3593-3600
    • Wang, X.1    Tabita, F.R.2
  • 18
    • 0017253134 scopus 로고
    • The activation of ribulose-1,5- bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications
    • Lorimer, G. H., Badger, M. R. & Andrews, T. J. The activation of ribulose-1,5- bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications. Biochemistry 15, 529-536 (1976).
    • (1976) Biochemistry , vol.15 , pp. 529-536
    • Lorimer, G.H.1    Badger, M.R.2    Andrews, T.J.3
  • 19
    • 12044257526 scopus 로고
    • Fallover of ribulose 1,5-bisphosphate carboxylase/oxygenase activity: Decarbamylation of catalytic sites depends on pH
    • Zhu, G. & Jensen, R. G. Fallover of ribulose 1,5-bisphosphate carboxylase/oxygenase activity: decarbamylation of catalytic sites depends on pH. Plant Physiol. 97, 1354-1358 (1991).
    • (1991) Plant Physiol , vol.97 , pp. 1354-1358
    • Zhu, G.1    Jensen, R.G.2
  • 20
    • 12044257739 scopus 로고
    • Xylulose 1,5-bisphosphate synthesized by ribulose 1,5- bisphosphate carboxylase/oxygenase during catalysis binds to decarbamylated enzyme
    • Zhu, G. & Jensen, R. G. Xylulose 1,5-bisphosphate synthesized by ribulose 1,5- bisphosphate carboxylase/oxygenase during catalysis binds to decarbamylated enzyme. Plant Physiol. 97, 1348-1353 (1991).
    • (1991) Plant Physiol , vol.97 , pp. 1348-1353
    • Zhu, G.1    Jensen, R.G.2
  • 21
    • 0026564085 scopus 로고
    • The Calvin cycle enzyme pentose-5-phosphate 3-epimerase is encoded within the cfx operons of the chemoautotroph Alcaligenes eutrophus
    • Kusian, B., Yoo, J. G., Bednarski, R. & Bowien, B. The Calvin cycle enzyme pentose-5-phosphate 3-epimerase is encoded within the cfx operons of the chemoautotroph Alcaligenes eutrophus. J. Bacteriol. 174, 7337-7344 (1992).
    • (1992) J. Bacteriol , vol.174 , pp. 7337-7344
    • Kusian, B.1    Yoo, J.G.2    Bednarski, R.3    Bowien, B.4
  • 22
    • 0027433252 scopus 로고
    • The cbb operons of the facultative chemoautotroph Alcaligenes eutrophus encode phosphoglycolate phosphatase
    • Schaferjohann, J., Yoo, J. G., Kusian, B. & Bowien, B. The cbb operons of the facultative chemoautotroph Alcaligenes eutrophus encode phosphoglycolate phosphatase. J. Bacteriol. 175, 7329-7340 (1993).
    • (1993) J. Bacteriol , vol.175 , pp. 7329-7340
    • Schaferjohann, J.1    Yoo, J.G.2    Kusian, B.3    Bowien, B.4
  • 23
    • 0034712708 scopus 로고    scopus 로고
    • Role of metal ions in the reaction catalysed by L-ribulose-5-phosphate 4-epimerase
    • Lee, L. V., Poyner, R. R., Vu, M. V. & Cleland, W. W. Role of metal ions in the reaction catalysed by L-ribulose-5-phosphate 4-epimerase. Biochemistry 39, 4821-4830 (2000).
    • (2000) Biochemistry , vol.39 , pp. 4821-4830
    • Lee, L.V.1    Poyner, R.R.2    Vu, M.V.3    Cleland, W.W.4
  • 24
    • 80855131519 scopus 로고    scopus 로고
    • Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
    • Mueller-Cajar, O. et al. Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Nature 479, 194-199 (2011).
    • (2011) Nature , vol.479 , pp. 194-199
    • Mueller-Cajar, O.1
  • 25
    • 1942537173 scopus 로고    scopus 로고
    • An efficient system for high-level expression and easy purification of authentic recombinant proteins
    • Catanzariti, A. M., Soboleva, T. A., Jans, D. A., Board, P. G. & Baker, R. T. An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci. 13, 1331-1339 (2004).
    • (2004) Protein Sci , vol.13 , pp. 1331-1339
    • Catanzariti, A.M.1    Soboleva, T.A.2    Jans, D.A.3    Board, P.G.4    Baker, R.T.5
  • 26
    • 0025967969 scopus 로고
    • A malachite green colorimetric assay for protein phosphatase activity
    • Geladopoulos, T. P., Sotiroudis, T. G. & Evangelopoulos, A. E. A malachite green colorimetric assay for protein phosphatase activity. Anal. Biochem. 192, 112-116 (1991).
    • (1991) Anal. Biochem , vol.192 , pp. 112-116
    • Geladopoulos, T.P.1    Sotiroudis, T.G.2    Evangelopoulos, A.E.3
  • 27
    • 0024485948 scopus 로고
    • Adenosine triphosphate hydrolysis by purified Rubisco activase
    • Robinson, S. P. & Portis, A. R. Jr Adenosine triphosphate hydrolysis by purified Rubisco activase. Arch. Biochem. Biophys. 268, 93-99 (1989).
    • (1989) Arch. Biochem. Biophys , vol.268 , pp. 93-99
    • Robinson, S.P.1    Portis, A.R.2
  • 28
    • 70450177317 scopus 로고    scopus 로고
    • MgF3- and α-galactose 1-phosphate in the active site of β-phosphoglucomutase form a transition state analogue of phosphoryl transfer
    • Baxter, N. J. et al. MgF3- and α-galactose 1-phosphate in the active site of β-phosphoglucomutase form a transition state analogue of phosphoryl transfer. J. Am. Chem. Soc. 131, 16334-16335 (2009).
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 16334-16335
    • Baxter, N.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.