메뉴 건너뛰기




Volumn 2014, Issue , 2014, Pages

Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; VEGETABLE PROTEIN; ENZYME INHIBITOR; PROTEIN SUBUNIT;

EID: 84930989053     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2014/583606     Document Type: Article
Times cited : (12)

References (97)
  • 1
    • 0034730838 scopus 로고    scopus 로고
    • Isolation and characterization of a higher plant ADP-glucose pyrophosphorylase small subunit homotetramer
    • P. R. Salamone, T. W. Greene, I. H. Kavakli, and T. W. Okita, "Isolation and characterization of a higher plant ADP-glucose pyrophosphorylase small subunit homotetramer, " FEBS Letters, vol. 482, no. 1-2, pp. 113-118, 2000.
    • (2000) FEBS Letters , vol.482 , Issue.1-2 , pp. 113-118
    • Salamone, P.R.1    Greene, T.W.2    Kavakli, I.H.3    Okita, T.W.4
  • 2
    • 0029328417 scopus 로고
    • Starch biosynthesis
    • C. Martin and A. M. Smith, "Starch biosynthesis, " Plant Cell, vol. 7, no. 7, pp. 971-985, 1995.
    • (1995) Plant Cell , vol.7 , Issue.7 , pp. 971-985
    • Martin, C.1    Smith, A.M.2
  • 3
    • 0002998420 scopus 로고
    • Biology and molecular biology of starch synthesis and its regulation
    • J. Preiss, "Biology and molecular biology of starch synthesis and its regulation, " Plant Molecular and Cellular Biology, vol. 7, pp. 59-114, 1991.
    • (1991) Plant Molecular and Cellular Biology , vol.7 , pp. 59-114
    • Preiss, J.1
  • 4
    • 0021144092 scopus 로고
    • Bacterial glycogen synthesis and its regulation
    • J. Preiss, "Bacterial glycogen synthesis and its regulation, " Annual Review of Microbiology, vol. 38, pp. 419-458, 1984.
    • (1984) Annual Review of Microbiology , vol.38 , pp. 419-458
    • Preiss, J.1
  • 5
    • 0034235937 scopus 로고    scopus 로고
    • Engineering starch for increased quantity and quality
    • C. J. Slattery, I. H. Kavakli, and T. W. Okita, "Engineering starch for increased quantity and quality, " Trends in Plant Science, vol. 5, no. 7, pp. 291-298, 2000.
    • (2000) Trends in Plant Science , vol.5 , Issue.7 , pp. 291-298
    • Slattery, C.J.1    Kavakli, I.H.2    Okita, T.W.3
  • 6
    • 0442314288 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase: A regulatory enzyme for plant starch synthesis
    • M. A. Ballicora, A. A. Iglesias, and J. Preiss, "ADP-glucose pyrophosphorylase: a regulatory enzyme for plant starch synthesis, " Photosynthesis Research, vol. 79, no. 1, pp. 1-24, 2004.
    • (2004) Photosynthesis Research , vol.79 , Issue.1 , pp. 1-24
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 7
    • 0033989946 scopus 로고    scopus 로고
    • Is leaf ADP-glucose pyrophosphorylase an allosteric enzyme?
    • L. A. Kleczkowski, "Is leaf ADP-glucose pyrophosphorylase an allosteric enzyme?" Biochimicaet Biophysica Acta, vol. 1476, no. 1, pp. 103-108, 2000.
    • (2000) Biochimicaet Biophysica Acta , vol.1476 , Issue.1 , pp. 103-108
    • Kleczkowski, L.A.1
  • 8
    • 0036743460 scopus 로고    scopus 로고
    • Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: A novel regulatory mechanism linking starch synthesis to the sucrose supply
    • A. Tiessen, J. H. M. Hendriks, M. Stitt, et al., "Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: a novel regulatory mechanism linking starch synthesis to the sucrose supply, " The Plant Cell, vol. 14, no. 9, pp. 2191-2213, 2002.
    • (2002) The Plant Cell , vol.14 , Issue.9 , pp. 2191-2213
    • Tiessen, A.1    Hendriks, J.H.M.2    Stitt, M.3
  • 9
    • 0014023725 scopus 로고
    • Starch-deficientmaizemutant lacking adenosine diphosphate glucose pyrophosphorylase activity
    • C. Y. Tsai and O. E. Nelson, "Starch-deficientmaizemutant lacking adenosine diphosphate glucose pyrophosphorylase activity, " Science, vol. 151, no. 3708, pp. 341-343, 1966.
    • (1966) Science , vol.151 , Issue.3708 , pp. 341-343
    • Tsai, C.Y.1    Nelson, O.E.2
  • 10
    • 0017151912 scopus 로고
    • Characterization of ADP glucose pyrophosphorylase from shrunken 2 and brittle 2 mutants of maize
    • L. C. Hannah and O. E. Nelson Jr., "Characterization of ADP glucose pyrophosphorylase from shrunken 2 and brittle 2 mutants of maize, " BiochemicalGenetics, vol. 14, no. 7-8, pp. 547-560, 1976.
    • (1976) BiochemicalGenetics , vol.14 , Issue.7-8 , pp. 547-560
    • Hannah, L.C.1    Nelson, O.E.2
  • 11
    • 0000984370 scopus 로고
    • A starchdeficientmutant of Arabidopsis thaliana with low ADP-glucose pyrophosphorylase activity lacks one of the two subunits of the enzyme
    • T. P. Lin, T. Casper, C. R. Sommerville, and J. Preiss, "A starchdeficientmutant of Arabidopsis thaliana with low ADP-glucose pyrophosphorylase activity lacks one of the two subunits of the enzyme, " Plant Physiology, vol. 88, pp. 1175-1181, 1988.
    • (1988) Plant Physiology , vol.88 , pp. 1175-1181
    • Lin, T.P.1    Casper, T.2    Sommerville, C.R.3    Preiss, J.4
  • 12
    • 0026533580 scopus 로고
    • Inhibition of the ADP-glucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes
    • B. Muller-Rober, U. Sonnewald, and L. Willmitzer, "Inhibition of the ADP-glucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes, " The EMBO Journal, vol. 11, no. 4, pp. 1229-1238, 1992.
    • (1992) The EMBO Journal , vol.11 , Issue.4 , pp. 1229-1238
    • Muller-Rober, B.1    Sonnewald, U.2    Willmitzer, L.3
  • 13
    • 0026458333 scopus 로고
    • Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase
    • D. M. Stark, K. P. Timmerman, G. I. Barry, J. Preiss, and G. M. Kishore, "Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase, " Science, vol. 258, no. 5080, pp. 287-292, 1992.
    • (1992) Science , vol.258 , Issue.5080 , pp. 287-292
    • Stark, D.M.1    Timmerman, K.P.2    Barry, G.I.3    Preiss, J.4    Kishore, G.M.5
  • 14
    • 0027398378 scopus 로고
    • Expression of the potato tuber ADP-glucose pyrophosphorylase in Escherichia coli
    • A. A. Iglesias, G. F. Barry, C. Meyer, et al., "Expression of the potato tuber ADP-glucose pyrophosphorylase in Escherichia coli, " The Journal of Biological Chemistry, vol. 268, no. 2, pp. 1081-1086, 1993.
    • (1993) The Journal of Biological Chemistry , vol.268 , Issue.2 , pp. 1081-1086
    • Iglesias, A.A.1    Barry, G.F.2    Meyer, C.3
  • 15
    • 0017046055 scopus 로고
    • Biosynthesis of bacterial glycogen. Characterization of the subunit structure of Escherichia coli B glucose 1 phosphate adenyltransferase (EC 2. 7. 7. 27)
    • T. H. Haugen, A. Ishaque, and J. Preiss, "Biosynthesis of bacterial glycogen. Characterization of the subunit structure of Escherichia coli B glucose 1 phosphate adenyltransferase (EC 2. 7. 7. 27), "The Journal of Biological Chemistry, vol. 251, no. 24, pp. 7880-7885, 1976.
    • (1976) The Journal of Biological Chemistry , vol.251 , Issue.24 , pp. 7880-7885
    • Haugen, T.H.1    Ishaque, A.2    Preiss, J.3
  • 17
    • 0038653402 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis
    • M. A. Ballicora, A. A. Iglesias, and J. Preiss, "ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis, " Microbiology and Molecular Biology Reviews, vol. 67, no. 2, pp. 213-225, 2003.
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.2 , pp. 213-225
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 18
    • 0026767213 scopus 로고
    • Comparison of proteins of ADP-glucose pyrophosphorylase fromdiverse sources
    • B. J. Smith-White and J. Preiss, "Comparison of proteins of ADP-glucose pyrophosphorylase fromdiverse sources, " Journal of Molecular Evolution, vol. 34, no. 5, pp. 449-464, 1992.
    • (1992) Journal of Molecular Evolution , vol.34 , Issue.5 , pp. 449-464
    • Smith-White, B.J.1    Preiss, J.2
  • 19
    • 0028138290 scopus 로고
    • Allosteric sites of the large subunit of the spinach leaf ADPglucose pyrophosphorylase
    • K. Ball and J. Preiss, "Allosteric sites of the large subunit of the spinach leaf ADPglucose pyrophosphorylase, " Journal of Biological Chemistry, vol. 269, no. 40, pp. 24706-24711, 1994.
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.40 , pp. 24706-24711
    • Ball, K.1    Preiss, J.2
  • 20
    • 0029360584 scopus 로고
    • Adenosine 5′-diphosphate-glucose pyrophosphorylase from potato tuber: Significance of the N terminus of the small subunit for catalytic properties and heat stability
    • M. A. Ballicora, M. J. Laughlin, Y. Fu, T. W. Okita, G. F. Barry, and J. Preiss, "Adenosine 5′-diphosphate-glucose pyrophosphorylase from potato tuber: significance of the N terminus of the small subunit for catalytic properties and heat stability, " Plant Physiology, vol. 109, no. 1, pp. 245-251, 1995.
    • (1995) Plant Physiology , vol.109 , Issue.1 , pp. 245-251
    • Ballicora, M.A.1    Laughlin, M.J.2    Fu, Y.3    Okita, T.W.4    Barry, G.F.5    Preiss, J.6
  • 22
    • 0032161364 scopus 로고    scopus 로고
    • ADPglucose pyrophosphorylase from potato tubers. Site-directed mutagenesis studies of the regulatory sites
    • M. A. Ballicora, Y. Fu, N. M. Nesbitt, and J. Preiss, "ADPglucose pyrophosphorylase from potato tubers. Site-directed mutagenesis studies of the regulatory sites, " Plant Physiology, vol. 118, no. 1, pp. 265-274, 1998.
    • (1998) Plant Physiology , vol.118 , Issue.1 , pp. 265-274
    • Ballicora, M.A.1    Fu, Y.2    Nesbitt, N.M.3    Preiss, J.4
  • 23
    • 0032007679 scopus 로고    scopus 로고
    • Substrate binding mutants of the higher plant ADP-glucose pyrophosphorylase
    • M. J. Laughlin, J. W. Payne, and T. W. Okita, "Substrate binding mutants of the higher plant ADP-glucose pyrophosphorylase, " Phytochemistry, vol. 47, no. 4, pp. 621-629, 1998.
    • (1998) Phytochemistry , vol.47 , Issue.4 , pp. 621-629
    • Laughlin, M.J.1    Payne, J.W.2    Okita, T.W.3
  • 24
    • 0035798634 scopus 로고    scopus 로고
    • Analysis of allosteric effector binding sites of potatoADP-glucose pyrophosphorylase through reverse genetics
    • I. H. Kavakli, J. S. Park, C. J. Slattery, P. R. Salamone, J. Frohlick, and T. W. Okita, "Analysis of allosteric effector binding sites of potatoADP-glucose pyrophosphorylase through reverse genetics, "The Journal of Biological Chemistry, vol. 276, no. 44, pp. 40834-40840, 2001.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.44 , pp. 40834-40840
    • Kavakli, I.H.1    Park, J.S.2    Slattery, C.J.3    Salamone, P.R.4    Frohlick, J.5    Okita, T.W.6
  • 27
    • 34347372235 scopus 로고    scopus 로고
    • ATP binding site in the plant ADP-glucose pyrophosphorylase large subunit
    • S. K. Hwang, S. Hamada, and T. W. Okita, "ATP binding site in the plant ADP-glucose pyrophosphorylase large subunit, " FEBS Letters, vol. 580, no. 28-29, pp. 6741-6748, 2006.
    • (2006) FEBS Letters , vol.580 , Issue.28-29 , pp. 6741-6748
    • Hwang, S.K.1    Hamada, S.2    Okita, T.W.3
  • 28
    • 43749106494 scopus 로고    scopus 로고
    • Direct appraisal of the potato tuber ADP-glucose pyrophosphorylase large subunit in enzyme function by study of a novel mutant form
    • S. K. Hwang, Y. Nagai, D. Kim, and T. W. Okita, "Direct appraisal of the potato tuber ADP-glucose pyrophosphorylase large subunit in enzyme function by study of a novel mutant form, " The Journal of Biological Chemistry, vol. 283, no. 11, pp. 6640-6647, 2008.
    • (2008) The Journal of Biological Chemistry , vol.283 , Issue.11 , pp. 6640-6647
    • Hwang, S.K.1    Nagai, Y.2    Kim, D.3    Okita, T.W.4
  • 29
    • 14644409834 scopus 로고    scopus 로고
    • A polymorphic motif in the small subunit of ADP-glucose pyrophosphorylase modulates interactions between the small and large subunits
    • J. M. Cross, M. Clancy, J. R. Shaw, et al., "A polymorphic motif in the small subunit of ADP-glucose pyrophosphorylase modulates interactions between the small and large subunits, " The Plant Journal, vol. 41, no. 4, pp. 501-511, 2005.
    • (2005) The Plant Journal , vol.41 , Issue.4 , pp. 501-511
    • Cross, J.M.1    Clancy, M.2    Shaw, J.R.3
  • 30
    • 15444377849 scopus 로고    scopus 로고
    • Crystal structure of potato tuberADP-glucose pyrophosphorylase
    • X. S. Jin, M. A. Ballicora, J. Preies, and J. H. Geiger, "Crystal structure of potato tuberADP-glucose pyrophosphorylase, "The EMBO Journal, vol. 24, no. 4, pp. 694-704, 2005.
    • (2005) The EMBO Journal , vol.24 , Issue.4 , pp. 694-704
    • Jin, X.S.1    Ballicora, M.A.2    Preies, J.3    Geiger, J.H.4
  • 31
    • 0032540222 scopus 로고    scopus 로고
    • Assessing protein structures with a non-local atomic interaction energy
    • F. Melo and E. Feytmans, "Assessing protein structures with a non-local atomic interaction energy, " Journal of Molecular Biology, vol. 277, no. 5, pp. 1141-1152, 1998.
    • (1998) Journal of Molecular Biology , vol.277 , Issue.5 , pp. 1141-1152
    • Melo, F.1    Feytmans, E.2
  • 33
    • 84898009362 scopus 로고    scopus 로고
    • Structure-function relationship of a plantNCS1member-homologymodeling and mutagenesis identified residues critical for substrate specificity of PLUTO, a nucleobase transporter from arabidopsis
    • Article IDe91343
    • S. Witz, P. Panwar, M. Schober, et al., "Structure-function relationship of a plantNCS1member-homologymodeling and mutagenesis identified residues critical for substrate specificity of PLUTO, a nucleobase transporter from arabidopsis, " PLoS ONE, vol. 9, Article IDe91343, 2014.
    • (2014) PLoS ONE , vol.9
    • Witz, S.1    Panwar, P.2    Schober, M.3
  • 34
    • 84883652794 scopus 로고    scopus 로고
    • In-silico analysis of Betaine AldehydeDehydrogenase2 of Oryza sativa and significantmutations responsible for fragrance
    • B. Kamaraj and R. Purohit, "In-silico analysis of Betaine AldehydeDehydrogenase2 of Oryza sativa and significantmutations responsible for fragrance, " Journal of Plant Interactions, vol. 8, pp. 321-333, 2013.
    • (2013) Journal of Plant Interactions , vol.8 , pp. 321-333
    • Kamaraj, B.1    Purohit, R.2
  • 35
    • 84893406338 scopus 로고    scopus 로고
    • Genome-wide comparative in silico analysis of the RNA helicase gene family in Zea mays and Glycine max: A comparison with arabidopsis and Oryza sativa
    • Article IDe78982
    • R. Xu, S. Zhang, J. Huang, and C. Zheng, "Genome-wide comparative in silico analysis of the RNA helicase gene family in Zea mays and Glycine max: a comparison with arabidopsis and Oryza sativa, " PLoS ONE, vol. 8, Article IDe78982, 2013.
    • (2013) PLoS ONE , vol.8
    • Xu, R.1    Zhang, S.2    Huang, J.3    Zheng, C.4
  • 36
    • 84884925570 scopus 로고    scopus 로고
    • Identifying essential genes/reactions of the rice photorespiration by in silico model-based analysis
    • M. Lakshmanan, B. Mohanty, and D. Y. Lee, "Identifying essential genes/reactions of the rice photorespiration by in silico model-based analysis, " Rice, vol. 6, pp. 1-5, 2013.
    • (2013) Rice , vol.6 , pp. 1-5
    • Lakshmanan, M.1    Mohanty, B.2    Lee, D.Y.3
  • 37
    • 84876246609 scopus 로고    scopus 로고
    • From protein structure to function via computational tools and approaches
    • R. Kolodny and M. Koslof f, "From protein structure to function via computational tools and approaches, " Israel Journal of Chemistry, vol. 53, no. 3-4, pp. 147-156, 2013.
    • (2013) Israel Journal of Chemistry , vol.53 , Issue.3-4 , pp. 147-156
    • Kolodny, R.1    Kosloff, M.2
  • 39
    • 84884534252 scopus 로고    scopus 로고
    • Structure-function analysis of the human ferroportin iron exporter (SLC40A1): Effect of hemochromatosis type 4 diseasemutations and identification of critical residues
    • G. L. Gac, C. Ka, R. Joubrel, et al., "Structure-function analysis of the human ferroportin iron exporter (SLC40A1): effect of hemochromatosis type 4 diseasemutations and identification of critical residues, " Human Mutation, vol. 34, pp. 1371-1380, 2013.
    • (2013) Human Mutation , vol.34 , pp. 1371-1380
    • Gac, G.L.1    Ka, C.2    Joubrel, R.3
  • 40
    • 84879238294 scopus 로고    scopus 로고
    • Computational identification and analysis of arsenate reductase protein in Cronobacter sakazakii ATCC BAA-894 suggests potential microorganism for reducing arsenate
    • N. Chaturvedi, V. K. Singh, and P. N. Pandey, "Computational identification and analysis of arsenate reductase protein in Cronobacter sakazakii ATCC BAA-894 suggests potential microorganism for reducing arsenate, " Journal of Structural and Functional Genomics, vol. 14, no. 2, pp. 37-45, 2013.
    • (2013) Journal of Structural and Functional Genomics , vol.14 , Issue.2 , pp. 37-45
    • Chaturvedi, N.1    Singh, V.K.2    Pandey, P.N.3
  • 41
    • 84887451808 scopus 로고    scopus 로고
    • In Silico modeling and functional interpretations of Cry1Ab15 toxin from Bacillus thuringiensis BtB-Hm-16
    • Article ID 471636
    • S. Kashyap, "In Silico modeling and functional interpretations of Cry1Ab15 toxin from Bacillus thuringiensis BtB-Hm-16, " BioMed Research International, vol. 2013, Article ID 471636, 10 pages, 2013.
    • (2013) BioMed Research International , vol.2013 , pp. 10
    • Kashyap, S.1
  • 42
    • 84870536995 scopus 로고    scopus 로고
    • A comparative proteomic approach to analyse structure, function and evolution of rice chitinases: A step towards increasing plant fungal resistance
    • K. Sarma, B. Dehury, J. Sahu, et al., "A comparative proteomic approach to analyse structure, function and evolution of rice chitinases: a step towards increasing plant fungal resistance, " Journal of Molecular Modeling, vol. 18, no. 11, pp. 4761-4780, 2012.
    • (2012) Journal of Molecular Modeling , vol.18 , Issue.11 , pp. 4761-4780
    • Sarma, K.1    Dehury, B.2    Sahu, J.3
  • 43
    • 84864338259 scopus 로고    scopus 로고
    • Homology modeling and analysis of structure predictions of the bovine rhinitis B virus RNA dependent RNA polymerase (RdRp)
    • D. K. Rai and E. Rieder, "Homology modeling and analysis of structure predictions of the bovine rhinitis B virus RNA dependent RNA polymerase (RdRp), " International Journal of Molecular Sciences, vol. 13, no. 7, pp. 8998-9013, 2012.
    • (2012) International Journal of Molecular Sciences , vol.13 , Issue.7 , pp. 8998-9013
    • Rai, D.K.1    Rieder, E.2
  • 44
    • 84894477749 scopus 로고    scopus 로고
    • Homologymodeling and functional annotation of bubaline pregnancy associated glycoprotein 2
    • article 13
    • B. Ganguly and S. Prasad, "Homologymodeling and functional annotation of bubaline pregnancy associated glycoprotein 2, " Journal of Animal Science and Biotechnology, vol. 3, article 13, 2012.
    • (2012) Journal of Animal Science and Biotechnology , vol.3
    • Ganguly, B.1    Prasad, S.2
  • 45
    • 79959701884 scopus 로고    scopus 로고
    • Comparative structural analysis of lipid binding START domains
    • Article ID e19521
    • A. G. Thorsell, W. H. Lee, C. Persson, et al., "Comparative structural analysis of lipid binding START domains, " PLoS ONE, vol. 6, no. 6, Article ID e19521, 2011.
    • (2011) PLoS ONE , vol.6 , Issue.6
    • Thorsell, A.G.1    Lee, W.H.2    Persson, C.3
  • 46
    • 77955724819 scopus 로고    scopus 로고
    • In silico structure-function analysis of pathological variation in the HSD11B2 gene sequence
    • J. R. Manning, M. A. Bailey, D. C. Soares, D. R. Dunbar, and J. J. Mullins, "In silico structure-function analysis of pathological variation in the HSD11B2 gene sequence, " Physiological Genomics, vol. 42, no. 3, pp. 319-330, 2010.
    • (2010) Physiological Genomics , vol.42 , Issue.3 , pp. 319-330
    • Manning, J.R.1    Bailey, M.A.2    Soares, D.C.3    Dunbar, D.R.4    Mullins, J.J.5
  • 47
    • 1642387872 scopus 로고    scopus 로고
    • Identification of functionally important residues in proteins using comparative models
    • S. W. Chen and J. L. Pellequer, "Identification of functionally important residues in proteins using comparative models, " Current Medicinal Chemistry, vol. 11, no. 5, pp. 595-605, 2004.
    • (2004) Current Medicinal Chemistry , vol.11 , Issue.5 , pp. 595-605
    • Chen, S.W.1    Pellequer, J.L.2
  • 48
    • 0032530250 scopus 로고    scopus 로고
    • Aclose family resemblance: The importance of structure in understand ing cytochromes P450
    • J. A. Peterson and S. E. Graham, "Aclose family resemblance: the importance of structure in understand ing cytochromes P450, " Structure, vol. 6, no. 9, pp. 1079-1085, 1998.
    • (1998) Structure , vol.6 , Issue.9 , pp. 1079-1085
    • Peterson, J.A.1    Graham, S.E.2
  • 49
    • 84880797602 scopus 로고    scopus 로고
    • Insight into the 3D structure of ADP-glucose pyrophosphorylase fromrice (Oryza sativa L.)
    • C. Dawar, S. Jain, and S. Kumar, "Insight into the 3D structure of ADP-glucose pyrophosphorylase fromrice (Oryza sativa L.), " Journal of MolecularModeling, vol. 19, no. 8, pp. 3351-3367, 2013.
    • (2013) Journal of Molecular Modeling , vol.19 , Issue.8 , pp. 3351-3367
    • Dawar, C.1    Jain, S.2    Kumar, S.3
  • 50
    • 84855609128 scopus 로고    scopus 로고
    • Analysis of ADP-glucose pyrophosphorylase expression during turion formation induced by abscisic acid in Spirodela polyrhiza (greater duckweed)
    • article 5
    • W. Wang and J. Messing, "Analysis of ADP-glucose pyrophosphorylase expression during turion formation induced by abscisic acid in Spirodela polyrhiza (greater duckweed), " BMC Plant Biology, vol. 12, article 5, 2012.
    • (2012) BMC Plant Biology , vol.12
    • Wang, W.1    Messing, J.2
  • 51
    • 77952568259 scopus 로고    scopus 로고
    • Characterization of the AGPase large subunit isof orms fromtomato indicates that the recombinant L3 subunit is active as a monomer
    • M. Petreikov, M. Eisenstein, Y. Yeselson, J. Preiss, and A. A. Schaffer, "Characterization of the AGPase large subunit isof orms fromtomato indicates that the recombinant L3 subunit is active as a monomer, " Biochemical Journal, vol. 428, no. 2, pp. 201-212, 2010.
    • (2010) Biochemical Journal , vol.428 , Issue.2 , pp. 201-212
    • Petreikov, M.1    Eisenstein, M.2    Yeselson, Y.3    Preiss, J.4    Schaffer, A.A.5
  • 52
    • 73549111066 scopus 로고    scopus 로고
    • Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase
    • Article IDe1000546
    • I. Baris, A. Tuncel, N. Ozber, O. Keskin, and I. H. Kavakli, "Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase, " PLoS Computational Biology, vol. 5, no. 10, Article IDe1000546, 2009.
    • (2009) PLoS Computational Biology , vol.5 , Issue.10
    • Baris, I.1    Tuncel, A.2    Ozber, N.3    Keskin, O.4    Kavakli, I.H.5
  • 53
    • 70349223021 scopus 로고    scopus 로고
    • Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme
    • N. Georgelis, J. R. Shaw, and L. C. Hannah, "Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme, " Plant Physiology, vol. 151, no. 1, pp. 67-77, 2009.
    • (2009) Plant Physiology , vol.151 , Issue.1 , pp. 67-77
    • Georgelis, N.1    Shaw, J.R.2    Hannah, L.C.3
  • 54
    • 56049114881 scopus 로고    scopus 로고
    • Insights into subunit interactions in the heterotetrameric structure of potato ADPglucose pyrophosphorylase
    • A. Tuncel, I. H. Kavakli, and O. Keskin, "Insights into subunit interactions in the heterotetrameric structure of potato ADPglucose pyrophosphorylase, " Biophysical Journal, vol. 95, no. 8, pp. 3628-3639, 2008.
    • (2008) Biophysical Journal , vol.95 , Issue.8 , pp. 3628-3639
    • Tuncel, A.1    Kavakli, I.H.2    Keskin, O.3
  • 55
    • 47549083279 scopus 로고    scopus 로고
    • Isolation of a heat-stable maize endosperm ADP-glucose pyrophosphorylase variant
    • N. Georgelis and L. C. Hannah, "Isolation of a heat-stable maize endosperm ADP-glucose pyrophosphorylase variant, " Plant Science, vol. 175, no. 3, pp. 247-254, 2008.
    • (2008) Plant Science , vol.175 , Issue.3 , pp. 247-254
    • Georgelis, N.1    Hannah, L.C.2
  • 56
    • 34548241238 scopus 로고    scopus 로고
    • Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase
    • D. Kim, S. K. Hwang, and T. W. Okita, "Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase, " Biochemical and Biophysical Research Communications, vol. 362, no. 2, pp. 301-306, 2007.
    • (2007) Biochemical and Biophysical Research Communications , vol.362 , Issue.2 , pp. 301-306
    • Kim, D.1    Hwang, S.K.2    Okita, T.W.3
  • 57
    • 34447549169 scopus 로고    scopus 로고
    • Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis
    • M. A. Ballicora, E. D. Erben, T. Yazaki, et al., "Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis, " Journal of Bacteriology, vol. 189, no. 14, pp. 5325-5333, 2007.
    • (2007) Journal of Bacteriology , vol.189 , Issue.14 , pp. 5325-5333
    • Ballicora, M.A.1    Erben, E.D.2    Yazaki, T.3
  • 58
    • 33845982238 scopus 로고    scopus 로고
    • Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases
    • C. M. Bejar, X. Jin, M. A. Ballicora, and J. Preiss, "Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases, "The Journal of Biological Chemistry, vol. 281, no. 52, pp. 40473-40484, 2006.
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 40473-40484
    • Bejar, C.M.1    Jin, X.2    Ballicora, M.A.3    Preiss, J.4
  • 59
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification and analysis tools on the ExPASy server
    • J.M. Walker, Ed. Humana Press, New Jersey, NJ, USA
    • E. Gasteiger, C. Hoogl, A. Gattiker, et al., "Protein identification and analysis tools on the ExPASy server, " in The Proteomics Protocols Hand book, J. M. Walker, Ed., pp. 571-607, Humana Press, New Jersey, NJ, USA, 2005.
    • (2005) The Proteomics Protocols Hand Book , pp. 571-607
    • Gasteiger, E.1    Hoogl, C.2    Gattiker, A.3
  • 60
    • 84863395869 scopus 로고    scopus 로고
    • CONCORD: A consensus method for protein secondary structure prediction via mixed integer linear optimization
    • Y. Wei, J. Thompson, and C. A. Floudas, "CONCORD: a consensus method for protein secondary structure prediction via mixed integer linear optimization, " Proceedings of the Royal Society A, vol. 468, no. 2139, pp. 831-850, 2012.
    • (2012) Proceedings of the Royal Society A , vol.468 , Issue.2139 , pp. 831-850
    • Wei, Y.1    Thompson, J.2    Floudas, C.A.3
  • 61
    • 44349192171 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins based on the meta approach
    • T. Ishida and K. Kinoshita, "Prediction of disordered regions in proteins based on the meta approach, " Bioinformatics, vol. 24, no. 11, pp. 1344-1348, 2008.
    • (2008) Bioinformatics , vol.24 , Issue.11 , pp. 1344-1348
    • Ishida, T.1    Kinoshita, K.2
  • 62
    • 16644363065 scopus 로고    scopus 로고
    • Delineation of modular proteins: Domain boundary prediction from sequence information
    • L. Kong and S. Ranganathan, "Delineation of modular proteins: domain boundary prediction from sequence information, " Briefings in bioinformatics, vol. 5, no. 2, pp. 179-192, 2004.
    • (2004) Briefings in Bioinformatics , vol.5 , Issue.2 , pp. 179-192
    • Kong, L.1    Ranganathan, S.2
  • 63
    • 23144458473 scopus 로고    scopus 로고
    • InterProScan: Protein domains identifier
    • E. Quevillon, V. Silventoinen, S. Pillai, et al., "InterProScan: protein domains identifier, " Nucleic Acids Research, vol. 33, no. 2, pp. W116-W120, 2005.
    • (2005) Nucleic Acids Research , vol.33 , Issue.2 , pp. W116-W120
    • Quevillon, E.1    Silventoinen, V.2    Pillai, S.3
  • 64
    • 84858077472 scopus 로고    scopus 로고
    • The Pfamprotein families database
    • M. Punta, P. C. Coggill, R. Y. Eberhardt, et al., "The Pfamprotein families database, " Nucleic Acids Research, vol. 40, no. 1, pp. D290-D301, 2012.
    • (2012) Nucleic Acids Research , vol.40 , Issue.1 , pp. D290-D301
    • Punta, M.1    Coggill, P.C.2    Eberhardt, R.Y.3
  • 65
    • 84875445608 scopus 로고    scopus 로고
    • CDD: Conserved domains and protein three-dimensional structure
    • A. Marchler-Bauer, C. Zheng, F. Chitsaz, et al., "CDD: conserved domains and protein three-dimensional structure, " Nucleic Acids Research, vol. 41, no. 1, pp. D348-D352, 2013.
    • (2013) Nucleic Acids Research , vol.41 , Issue.1 , pp. D348-D352
    • Marchler-Bauer, A.1    Zheng, C.2    Chitsaz, F.3
  • 66
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • I. Letunic, T. Doerks, and P. Bork, "SMART 7: recent updates to the protein domain annotation resource, " Nucleic Acids Research, vol. 40, no. 1, pp. D302-D305, 2012.
    • (2012) Nucleic Acids Research , vol.40 , Issue.1 , pp. D302-D305
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 67
    • 0028501914 scopus 로고
    • Non-globular domains in protein sequences: Automated segmentation using complexity measures
    • J. C. Wootton, "Non-globular domains in protein sequences: automated segmentation using complexity measures, " Computers and Chemistry, vol. 18, no. 3, pp. 269-285, 1994.
    • (1994) Computers and Chemistry , vol.18 , Issue.3 , pp. 269-285
    • Wootton, J.C.1
  • 68
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J. D. Thompson, D. G. Higgins, and T. J. Gibson, "CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, " Nucleic Acids Research, vol. 22, no. 22, pp. 4673-4680, 1994.
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 69
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • P. Gouet, E. Courcelle, D. I. Stuart, and F. Metoz, "ESPript: analysis of multiple sequence alignments in PostScript, " Bioinformatics, vol. 15, no. 4, pp. 305-308, 1999.
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 70
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch and C. Sander, "Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features., " Biopolymers, vol. 22, no. 12, pp. 2577-2637, 1983.
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 71
    • 0043123216 scopus 로고    scopus 로고
    • GeneSilico protein structure prediction meta-server
    • M. A. Kurowski and J. M. Bujnicki, "GeneSilico protein structure prediction meta-server, " Nucleic Acids Research, vol. 31, no. 13, pp. 3305-3307, 2003.
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3305-3307
    • Kurowski, M.A.1    Bujnicki, J.M.2
  • 72
    • 81255123286 scopus 로고    scopus 로고
    • Improving the physical realism and structural accuracy of protein models by a two-step atomiclevel energy minimization
    • D. Xu and Y. Zhang, "Improving the physical realism and structural accuracy of protein models by a two-step atomiclevel energy minimization, " Biophysical Journal, vol. 101, no. 10, pp. 2525-2534, 2011.
    • (2011) Biophysical Journal , vol.101 , Issue.10 , pp. 2525-2534
    • Xu, D.1    Zhang, Y.2
  • 73
    • 39749085824 scopus 로고    scopus 로고
    • LOOPER: A molecular mechanics-based algorithm for protein loop prediction
    • V. Z. Spassov, P. K. Flook, and L. Yan, "LOOPER: a molecular mechanics-based algorithm for protein loop prediction, " Protein Engineering, Design and Selection, vol. 21, no. 2, pp. 91-100, 2008.
    • (2008) Protein Engineering, Design and Selection , vol.21 , Issue.2 , pp. 91-100
    • Spassov, V.Z.1    Flook, P.K.2    Yan, L.3
  • 74
    • 33847261239 scopus 로고    scopus 로고
    • The dominant role of side-chain backbone interactions in structural realization of amino acid code. ChiRotor: A side-chain prediction algorithm based on side-chain backbone interactions
    • V. Z. Spassov, L. Yan, and P. K. Flook, "The dominant role of side-chain backbone interactions in structural realization of amino acid code. ChiRotor: a side-chain prediction algorithm based on side-chain backbone interactions, " Protein Science, vol. 16, no. 3, pp. 494-506, 2007.
    • (2007) Protein Science , vol.16 , Issue.3 , pp. 494-506
    • Spassov, V.Z.1    Yan, L.2    Flook, P.K.3
  • 77
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • C. Colovos and T. O. Yeates, "Verification of protein structures: patterns of nonbonded atomic interactions, " Protein Science, vol. 2, no. 9, pp. 1511-1519, 1993.
    • (1993) Protein Science , vol.2 , Issue.9 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 78
    • 0026610767 scopus 로고
    • Assesment of protein models with three-dimensional profiles
    • R. Luthy, J. U. Bowie, and D. Eisenberg, "Assesment of protein models with three-dimensional profiles, " Nature, vol. 356, no. 6364, pp. 83-85, 1992.
    • (1992) Nature , vol.356 , Issue.6364 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 79
    • 54949097750 scopus 로고    scopus 로고
    • MetaMQAP: A meta-server for the quality assessment of protein models
    • article 403
    • M. Pawlowski, M. J. Gajda, R. Matlak, and J. M. Bujnicki, "MetaMQAP: a meta-server for the quality assessment of protein models, " BMC Bioinformatics, vol. 9, article 403, 2008.
    • (2008) BMC Bioinformatics , vol.9
    • Pawlowski, M.1    Gajda, M.J.2    Matlak, R.3    Bujnicki, J.M.4
  • 80
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • D. Frishman and P. Argos, "Knowledge-based protein secondary structure assignment, " Proteins: Structure, Function and Genetics, vol. 23, no. 4, pp. 566-579, 1995.
    • (1995) Proteins: Structure, Function and Genetics , vol.23 , Issue.4 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 81
    • 84855229636 scopus 로고    scopus 로고
    • PIC: Protein interactions calculator
    • K. G. Tina, R. Bhadra, and N. Srinivasan, "PIC: protein interactions calculator, "Nucleic Acids Research, vol. 35, no. 2, pp. W473-W476, 2007.
    • (2007) Nucleic Acids Research , vol.35 , Issue.2 , pp. W473-W476
    • Tina, K.G.1    Bhadra, R.2    Srinivasan, N.3
  • 82
    • 0037212102 scopus 로고    scopus 로고
    • Ligand Fit: A novel method for the shape-directed rapid docking of ligands to protein active sites
    • C. M. Venkatachalam, X. Jiang, T. Oldfield, and M. Waldman, "Ligand Fit: a novel method for the shape-directed rapid docking of ligands to protein active sites, " Journal of Molecular Graphics and Modelling, vol. 21, no. 4, pp. 289-307, 2003.
    • (2003) Journal of Molecular Graphics and Modelling , vol.21 , Issue.4 , pp. 289-307
    • Venkatachalam, C.M.1    Jiang, X.2    Oldfield, T.3    Waldman, M.4
  • 83
    • 79960395595 scopus 로고    scopus 로고
    • Identification of cavities on protein surface usingmultiple computational approaches for drug binding site prediction
    • Article ID btr331
    • Z. Zhang, Y. Li, B. Lin, M. Schroeder, and B. Huang, "Identification of cavities on protein surface usingmultiple computational approaches for drug binding site prediction, " Bioinformatics, vol. 27, no. 15, Article ID btr331, pp. 2083-2088, 2011.
    • (2011) Bioinformatics , vol.27 , Issue.15 , pp. 2083-2088
    • Zhang, Z.1    Li, Y.2    Lin, B.3    Schroeder, M.4    Huang, B.5
  • 84
    • 73249124001 scopus 로고    scopus 로고
    • Probing allosteric binding sites of the maize endosperm ADPglucose pyrophosphorylase
    • S. K. Boehlein, J. R. Shaw, L. C. Hannah, and J. D. Stewart, "Probing allosteric binding sites of the maize endosperm ADPglucose pyrophosphorylase, " Plant Physiology, vol. 152, no. 1, pp. 85-95, 2010.
    • (2010) Plant Physiology , vol.152 , Issue.1 , pp. 85-95
    • Boehlein, S.K.1    Shaw, J.R.2    Hannah, L.C.3    Stewart, J.D.4
  • 85
    • 0041781898 scopus 로고    scopus 로고
    • Detailed analysis of grid-basedmolecular docking: A case study of CDOCKER-a CHARMm-based MD docking algorithm
    • G. Wu, D. H. Robertson, C. L. Brooks, and M. Vieth, "Detailed analysis of grid-basedmolecular docking: a case study of CDOCKER-a CHARMm-based MD docking algorithm, " Journal of Computational Chemistry, vol. 24, no. 13, pp. 1549-1562, 2003.
    • (2003) Journal of Computational Chemistry , vol.24 , Issue.13 , pp. 1549-1562
    • Wu, G.1    Robertson, D.H.2    Brooks, C.L.3    Vieth, M.4
  • 86
    • 0025612425 scopus 로고
    • Correlation between stability of a protein and its dipeptide composition: A novel approach for predicting in vivo stability of a protein from its primary sequence
    • K. Guruprasad, B. V. B. Reddy, and M. W. Pandit, "Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence, " Protein Engineering, vol. 4, no. 2, pp. 155-161, 1990.
    • (1990) Protein Engineering , vol.4 , Issue.2 , pp. 155-161
    • Guruprasad, K.1    Reddy, B.V.B.2    Pandit, M.W.3
  • 87
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H. J. Dyson and P. E. Wright, "Intrinsically unstructured proteins and their functions, " Nature Reviews Molecular Cell Biology, vol. 6, no. 3, pp. 197-208, 2005.
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 88
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • V. N. Uversky, C. J. Oldfield, and A. K. Dunker, "Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling, " Journal of Molecular Recognition, vol. 18, no. 5, pp. 343-384, 2005.
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.5 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 90
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte and R. F. Doolittle, "A simple method for displaying the hydropathic character of a protein, " Journal of Molecular Biology, vol. 157, no. 1, pp. 105-132, 1982.
    • (1982) Journal of Molecular Biology , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 91
    • 0037113956 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+
    • J. Sivaraman, V. Sauve, A. Matte, and M. Cygler, "Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+, " The Journal of Biological Chemistry, vol. 277, no. 46, pp. 44214-44219, 2002.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 44214-44219
    • Sivaraman, J.1    Sauve, V.2    Matte, A.3    Cygler, M.4
  • 92
    • 0001395823 scopus 로고
    • Bacterial glycogen and plant starch biosynthesis
    • A. A. Iglesias and J. Preiss, "Bacterial glycogen and plant starch biosynthesis, " Biochemical Education, vol. 20, no. 4, pp. 196-203, 1992.
    • (1992) Biochemical Education , vol.20 , Issue.4 , pp. 196-203
    • Iglesias, A.A.1    Preiss, J.2
  • 94
    • 0001172247 scopus 로고
    • The rb mutation of peas causes structural and regulatory changes in ADP glucose pyrophosphorylase from developing embryos
    • C. Hylton and A. M. Smith, "The rb mutation of peas causes structural and regulatory changes in ADP glucose pyrophosphorylase from developing embryos, " Plant Physiology, vol. 99, no. 4, pp. 1626-1634, 1992.
    • (1992) Plant Physiology , vol.99 , Issue.4 , pp. 1626-1634
    • Hylton, C.1    Smith, A.M.2
  • 95
    • 0001608011 scopus 로고
    • Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm
    • M. Olive, R. J. Ellis, and W. W. Schuch, "Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm, " Plant Molecular Biology, vol. 12, no. 5, pp. 525-538, 1989.
    • (1989) Plant Molecular Biology , vol.12 , Issue.5 , pp. 525-538
    • Olive, M.1    Ellis, R.J.2    Schuch, W.W.3
  • 96
    • 0029108075 scopus 로고
    • Cell-type specific, coordinate expression of two ADP-glucose pyrophosphorylase genes in relation to starch biosynthesis during seed development of Vicia faba L
    • H. Weber, U. Heim, L. Borisjuk, and U. Wobus, "Cell-type specific, coordinate expression of two ADP-glucose pyrophosphorylase genes in relation to starch biosynthesis during seed development of Vicia faba L., " Planta, vol. 195, no. 3, pp. 352-361, 1995.
    • (1995) Planta , vol.195 , Issue.3 , pp. 352-361
    • Weber, H.1    Heim, U.2    Borisjuk, L.3    Wobus, U.4
  • 97
    • 0032711802 scopus 로고    scopus 로고
    • The allosterically unregulated isof orm of ADP-glucose pyrophosphorylase from barley endosperm is the most likely source of ADP-glucose incorporated into endosperm starch
    • D. N. P. Doan, H. Rudi, and O. A. Olsen, "The allosterically unregulated isof orm of ADP-glucose pyrophosphorylase from barley endosperm is the most likely source of ADP-glucose incorporated into endosperm starch, " Plant Physiology, vol. 121, no. 3, pp. 965-975, 1999.
    • (1999) Plant Physiology , vol.121 , Issue.3 , pp. 965-975
    • Doan, D.N.P.1    Rudi, H.2    Olsen, O.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.