메뉴 건너뛰기




Volumn 77, Issue 1, 2010, Pages 183-199

The molecular basis of glycogen breakdown and transport in Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; BINDING PROTEIN; GLYCOGEN; PROTEIN MALX; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARRIER PROTEIN; MALTOOLIGOSACCHARIDES; MALX PROTEIN, STREPTOCOCCUS PNEUMONIAE; OLIGOSACCHARIDE;

EID: 77953990905     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07199.x     Document Type: Article
Times cited : (56)

References (58)
  • 1
    • 34248173904 scopus 로고    scopus 로고
    • Specific recognition of saturated and 4,5-unsaturated hexuronate sugars by a periplasmic binding protein involved in pectin catabolism
    • Abbott, D.W. Boraston, A.B. (2007) Specific recognition of saturated and 4,5-unsaturated hexuronate sugars by a periplasmic binding protein involved in pectin catabolism. J Mol Biol 369 : 759 770.
    • (2007) J Mol Biol , vol.369 , pp. 759-770
    • Abbott, D.W.1    Boraston, A.B.2
  • 2
    • 33750033526 scopus 로고    scopus 로고
    • Serotype-specific invasiveness and colonization prevalence in Streptococcus pneumoniae correlate with the lag phase during in vitro growth
    • Battig, P., Hathaway, L.J., Hofer, S. Muhlemann, K. (2006) Serotype-specific invasiveness and colonization prevalence in Streptococcus pneumoniae correlate with the lag phase during in vitro growth. Microbes Infect 8 : 2612 2617.
    • (2006) Microbes Infect , vol.8 , pp. 2612-2617
    • Battig, P.1    Hathaway, L.J.2    Hofer, S.3    Muhlemann, K.4
  • 3
    • 0034442654 scopus 로고    scopus 로고
    • Antigenicity, expression, and molecular characterization of surface-located pullulanase of Streptococcus pneumoniae
    • Bongaerts, R.J., Heinz, H.P., Hadding, U. Zysk, G. (2000) Antigenicity, expression, and molecular characterization of surface-located pullulanase of Streptococcus pneumoniae. Infect Immun 68 : 7141 7143.
    • (2000) Infect Immun , vol.68 , pp. 7141-7143
    • Bongaerts, R.J.1    Heinz, H.P.2    Hadding, U.3    Zysk, G.4
  • 4
    • 0035807792 scopus 로고    scopus 로고
    • Beta-1,3-Glucan binding by a thermostable carbohydrate-binding module from Thermotoga maritima
    • Boraston, A.B., Warren, R.A. Kilburn, D.G. (2001) beta-1,3-Glucan binding by a thermostable carbohydrate-binding module from Thermotoga maritima. Biochemistry 40 : 14679 14685.
    • (2001) Biochemistry , vol.40 , pp. 14679-14685
    • Boraston, A.B.1    Warren, R.A.2    Kilburn, D.G.3
  • 5
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine tuning polysaccharide recognition
    • Boraston, A.B., Bolam, D.N., Gilbert, H.J. Davies, G.J. (2004) Carbohydrate-binding modules: fine tuning polysaccharide recognition. Biochem J 382 : 769 782.
    • (2004) Biochem J , vol.382 , pp. 769-782
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 6
    • 33644855732 scopus 로고    scopus 로고
    • A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition
    • Boraston, A.B., Healey, M., Klassen, J., Ficko-Blean, E., Lammerts van Bueren, A. Law, V. (2006) A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition. J Biol Chem 281 : 587 598.
    • (2006) J Biol Chem , vol.281 , pp. 587-598
    • Boraston, A.B.1    Healey, M.2    Klassen, J.3    Ficko-Blean, E.4    Lammerts Van Bueren, A.5    Law, V.6
  • 7
    • 0033005813 scopus 로고    scopus 로고
    • Transformation of a type 4 encapsulated strain of Streptococcus pneumoniae
    • Bricker, A.L. Camilli, A. (1999) Transformation of a type 4 encapsulated strain of Streptococcus pneumoniae. FEMS Microbiol Lett 172 : 131 135.
    • (1999) FEMS Microbiol Lett , vol.172 , pp. 131-135
    • Bricker, A.L.1    Camilli, A.2
  • 8
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, A.T. (1992) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 : 472 475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 10
    • 0037336363 scopus 로고    scopus 로고
    • Characterization of a novel fucose-regulated promoter (PfcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae
    • Chan, P.F., O'Dwyer, K.M., Palmer, L.M., Ambrad, J.D., Ingraham, K.A., So, C., et al. (2003) Characterization of a novel fucose-regulated promoter (PfcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae. J Bacteriol 185 : 2051 2058.
    • (2003) J Bacteriol , vol.185 , pp. 2051-2058
    • Chan, P.F.1    O'Dwyer, K.M.2    Palmer, L.M.3    Ambrad, J.D.4    Ingraham, K.A.5    So, C.6
  • 12
    • 0028609712 scopus 로고
    • Receptor specificity of adherence of Streptococcus pneumoniae to human type-II pneumocytes and vascular endothelial cells in vitro
    • Cundell, D.R. Tuomanen, E.I. (1994) Receptor specificity of adherence of Streptococcus pneumoniae to human type-II pneumocytes and vascular endothelial cells in vitro. Microb Pathog 17 : 361 374.
    • (1994) Microb Pathog , vol.17 , pp. 361-374
    • Cundell, D.R.1    Tuomanen, E.I.2
  • 13
    • 33748798733 scopus 로고    scopus 로고
    • The crystal structure of a thermophilic glucose binding protein reveals adaptations that interconvert mono and di-saccharide binding sites
    • Cuneo, M.J., Changela, A., Warren, J.J., Beese, L.S. Hellinga, H.W. (2006) The crystal structure of a thermophilic glucose binding protein reveals adaptations that interconvert mono and di-saccharide binding sites. J Mol Biol 362 : 259 270.
    • (2006) J Mol Biol , vol.362 , pp. 259-270
    • Cuneo, M.J.1    Changela, A.2    Warren, J.J.3    Beese, L.S.4    Hellinga, H.W.5
  • 14
    • 65449123447 scopus 로고    scopus 로고
    • Structural adaptations that modulate monosaccharide, disaccharide, and trisaccharide specificities in periplasmic maltose-binding proteins
    • Cuneo, M.J., Changela, A., Beese, L.S. Hellinga, H.W. (2009) Structural adaptations that modulate monosaccharide, disaccharide, and trisaccharide specificities in periplasmic maltose-binding proteins. J Mol Biol 389 : 157 166.
    • (2009) J Mol Biol , vol.389 , pp. 157-166
    • Cuneo, M.J.1    Changela, A.2    Beese, L.S.3    Hellinga, H.W.4
  • 15
    • 0035951304 scopus 로고    scopus 로고
    • The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic Archaeon Thermococcus litoralis at 1.85 A
    • Diez, J., Diederichs, K., Greller, G., Horlacher, R., Boos, W. Welte, W. (2001) The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic Archaeon Thermococcus litoralis at 1.85 A. J Mol Biol 305 : 905 915.
    • (2001) J Mol Biol , vol.305 , pp. 905-915
    • Diez, J.1    Diederichs, K.2    Greller, G.3    Horlacher, R.4    Boos, W.5    Welte, W.6
  • 16
    • 0035830955 scopus 로고    scopus 로고
    • Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: Flexibility of tertiary structure and ligand binding
    • Duan, X., Hall, J.A., Nikaido, H. Quiocho, F.A. (2001) Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding. J Mol Biol 306 : 1115 1126.
    • (2001) J Mol Biol , vol.306 , pp. 1115-1126
    • Duan, X.1    Hall, J.A.2    Nikaido, H.3    Quiocho, F.A.4
  • 17
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60 : 2126 2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 18
    • 33845968854 scopus 로고    scopus 로고
    • The interaction of carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor
    • Ficko-Blean, E. Boraston, A.B. (2006) The interaction of carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta- hexosaminidase with its carbohydrate receptor. J Biol Chem 281 : 37748 37757.
    • (2006) J Biol Chem , vol.281 , pp. 37748-37757
    • Ficko-Blean, E.1    Boraston, A.B.2
  • 19
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v.2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy, J.L., Laird, M.R., Chen, F., Rey, S., Walsh, C.J., Ester, M. Brinkman, F.S. (2005) PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 21 : 617 623.
    • (2005) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3    Rey, S.4    Walsh, C.J.5    Ester, M.6    Brinkman, F.S.7
  • 21
    • 33748867079 scopus 로고    scopus 로고
    • Analysis of the transcriptome of group A Streptococcus in mouse soft tissue infection
    • Graham, M.R., Virtaneva, K., Porcella, S.F., Gardner, D.J., Long, R.D., Welty, D.M., et al. (2006) Analysis of the transcriptome of group A Streptococcus in mouse soft tissue infection. Am J Pathol 169 : 927 942.
    • (2006) Am J Pathol , vol.169 , pp. 927-942
    • Graham, M.R.1    Virtaneva, K.2    Porcella, S.F.3    Gardner, D.J.4    Long, R.D.5    Welty, D.M.6
  • 22
    • 0036047758 scopus 로고    scopus 로고
    • Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors
    • Hava, D.L. Camilli, A. (2002) Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors. Mol Microbiol 45 : 1389 1406.
    • (2002) Mol Microbiol , vol.45 , pp. 1389-1406
    • Hava, D.L.1    Camilli, A.2
  • 23
    • 0036716927 scopus 로고    scopus 로고
    • Glycogen metabolism loss: A common marker of parasitic behaviour in bacteria?
    • Henrissat, B., Deleury, E. Coutinho, P.M. (2002) Glycogen metabolism loss: a common marker of parasitic behaviour in bacteria? Trends Genet 18 : 437 440.
    • (2002) Trends Genet , vol.18 , pp. 437-440
    • Henrissat, B.1    Deleury, E.2    Coutinho, P.M.3
  • 24
    • 0027503489 scopus 로고
    • Fluorophore-assisted carbohydrate electrophoresis: A new technology for the analysis of glycans
    • Jackson, P. (1993) Fluorophore-assisted carbohydrate electrophoresis: a new technology for the analysis of glycans. Biochem Soc Trans 21 : 121 125.
    • (1993) Biochem Soc Trans , vol.21 , pp. 121-125
    • Jackson, P.1
  • 25
    • 38549174180 scopus 로고    scopus 로고
    • Unveiling molecular mechanisms of bacterial surface proteins: Streptococcus pneumoniae as a model organism for structural studies
    • Jedrzejas, M.J. (2007) Unveiling molecular mechanisms of bacterial surface proteins: Streptococcus pneumoniae as a model organism for structural studies. Cell Mol Life Sci 64 : 2799 2822.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2799-2822
    • Jedrzejas, M.J.1
  • 26
    • 1342281657 scopus 로고    scopus 로고
    • The innate immune response to pneumococcal lung infection: The untold story
    • Kadioglu, A. Andrew, P.W. (2004) The innate immune response to pneumococcal lung infection: the untold story. Trends Immunol 25 : 143 149.
    • (2004) Trends Immunol , vol.25 , pp. 143-149
    • Kadioglu, A.1    Andrew, P.W.2
  • 27
  • 28
    • 46049115447 scopus 로고    scopus 로고
    • Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices
    • Koropatkin, N.M., Martens, E.C., Gordon, J.I. Smith, T.J. (2008) Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices. Structure 16 : 1105 1115.
    • (2008) Structure , vol.16 , pp. 1105-1115
    • Koropatkin, N.M.1    Martens, E.C.2    Gordon, J.I.3    Smith, T.J.4
  • 29
    • 0013861147 scopus 로고
    • Integration efficiency and genetic recombination in pneumococcal transformation
    • Lacks, S. (1966) Integration efficiency and genetic recombination in pneumococcal transformation. Genetics 53 : 207 235.
    • (1966) Genetics , vol.53 , pp. 207-235
    • Lacks, S.1
  • 30
    • 10644283902 scopus 로고    scopus 로고
    • Alpha-glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens
    • Lammerts van Bueren, A., Finn, R., Ausio, J. Boraston, A.B. (2004) Alpha-glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens. Biochemistry 43 : 15633 15642.
    • (2004) Biochemistry , vol.43 , pp. 15633-15642
    • Lammerts Van Bueren, A.1    Finn, R.2    Ausio, J.3    Boraston, A.B.4
  • 31
    • 33846096051 scopus 로고    scopus 로고
    • Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors
    • Lammerts van Bueren, A., Higgins, M., Wang, D., Burke, R.D. Boraston, A.B. (2007) Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors. Nat Struct Mol Biol 14 : 76 84.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 76-84
    • Lammerts Van Bueren, A.1    Higgins, M.2    Wang, D.3    Burke, R.D.4    Boraston, A.B.5
  • 32
    • 0000243829 scopus 로고
    • Procheck - A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., Macarthur, M.W., Moss, D.S. Thornton, J.M. (1993) Procheck - a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26 : 283 291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 33
    • 0034999527 scopus 로고    scopus 로고
    • A functional genomic analysis of type 3 Streptococcus pneumoniae virulence
    • Lau, G.W., Haataja, S., Lonetto, M., Kensit, S.E., Marra, A., Bryant, A.P., et al. (2001) A functional genomic analysis of type 3 Streptococcus pneumoniae virulence. Mol Microbiol 40 : 555 571.
    • (2001) Mol Microbiol , vol.40 , pp. 555-571
    • Lau, G.W.1    Haataja, S.2    Lonetto, M.3    Kensit, S.E.4    Marra, A.5    Bryant, A.P.6
  • 34
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum likelihood method
    • Murshudov, G.N., Vagin, A.A. Dodson, E.J. (1997) Refinement of macromolecular structures by the maximum likelihood method. Acta Cryst D 53 : 240 255.
    • (1997) Acta Cryst D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 35
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham, M.L., Khare, D., Quiocho, F.A., Davidson, A.L. Chen, J. (2007) Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450 : 515 521.
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 37
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R. Lamzin, V.S. (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6 : 458 463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 38
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Part 10
    • Pflugrath, J.W. (1999) The finer things in X-ray diffraction data collection. Acta Crystallogr D Biol Crystallogr 55 (Part 10 1718 1725.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 41
    • 70349333637 scopus 로고    scopus 로고
    • The mechanism of ABC transporters: General lessons from structural and functional studies of an antigenic peptide transporter
    • Procko, E., O'Mara, M.L., Bennett, W.F., Tieleman, D.P. Gaudet, R. (2009) The mechanism of ABC transporters: general lessons from structural and functional studies of an antigenic peptide transporter. FASEB J 23 : 1287 1302.
    • (2009) FASEB J , vol.23 , pp. 1287-1302
    • Procko, E.1    O'Mara, M.L.2    Bennett, W.F.3    Tieleman, D.P.4    Gaudet, R.5
  • 42
    • 0027159810 scopus 로고
    • Structure of the maltodextrin-uptake locus of Streptococcus pneumoniae. Correlation to the Escherichia coli maltose regulon
    • Puyet, A. Espinosa, M. (1993) Structure of the maltodextrin-uptake locus of Streptococcus pneumoniae. Correlation to the Escherichia coli maltose regulon. J Mol Biol 230 : 800 811.
    • (1993) J Mol Biol , vol.230 , pp. 800-811
    • Puyet, A.1    Espinosa, M.2
  • 43
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho, F.A., Spurlino, J.C. Rodseth, L.E. (1997) Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure 5 : 997 1015.
    • (1997) Structure , vol.5 , pp. 997-1015
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 44
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Cryst A 42 : 140 149.
    • (1986) Acta Cryst A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 45
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R.J. (2001) Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr D Biol Crystallogr 57 : 1373 1382.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 46
    • 4544239607 scopus 로고    scopus 로고
    • Surfactant lipid synthesis and lamellar body formation in glycogen-laden type II cells
    • Ridsdale, R. Post, M. (2004) Surfactant lipid synthesis and lamellar body formation in glycogen-laden type II cells. Am J Physiol Lung Cell Mol Physiol 287 : L743 L751.
    • (2004) Am J Physiol Lung Cell Mol Physiol , vol.287
    • Ridsdale, R.1    Post, M.2
  • 47
    • 56849124577 scopus 로고    scopus 로고
    • Functional characterization of a newly identified group B Streptococcus pullulanase eliciting antibodies able to prevent alpha-glucans degradation
    • Santi, I., Pezzicoli, A., Bosello, M., Berti, F., Mariani, M., Telford, J.L., et al. (2008) Functional characterization of a newly identified group B Streptococcus pullulanase eliciting antibodies able to prevent alpha-glucans degradation. PLoS One 3 : e3787.
    • (2008) PLoS One , vol.3 , pp. 3787
    • Santi, I.1    Pezzicoli, A.2    Bosello, M.3    Berti, F.4    Mariani, M.5    Telford, J.L.6
  • 48
    • 0037195083 scopus 로고    scopus 로고
    • The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract
    • Schell, M.A., Karmirantzou, M., Snel, B., Vilanova, D., Berger, B., Pessi, G., et al. (2002) The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract. Proc Natl Acad Sci USA 99 : 14422 14427.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14422-14427
    • Schell, M.A.1    Karmirantzou, M.2    Snel, B.3    Vilanova, D.4    Berger, B.5    Pessi, G.6
  • 50
    • 33746583568 scopus 로고    scopus 로고
    • Maltodextrin utilization plays a key role in the ability of group A Streptococcus to colonize the oropharynx
    • Shelburne, S.A., 3rd., Sumby, P., Sitkiewicz, I., Okorafor, N., Granville, C., Patel, P., et al. (2006) Maltodextrin utilization plays a key role in the ability of group A Streptococcus to colonize the oropharynx. Infect Immun 74 : 4605 4614.
    • (2006) Infect Immun , vol.74 , pp. 4605-4614
    • Shelburne III, S.A.1    Sumby, P.2    Sitkiewicz, I.3    Okorafor, N.4    Granville, C.5    Patel, P.6
  • 51
    • 34147118421 scopus 로고    scopus 로고
    • MalE of group A Streptococcus participates in the rapid transport of maltotriose and longer maltodextrins
    • Shelburne, S.A., 3rd., Fang, H., Okorafor, N., Sumby, P., Sitkiewicz, I., Keith, D., et al. (2007) MalE of group A Streptococcus participates in the rapid transport of maltotriose and longer maltodextrins. J Bacteriol 189 : 2610 2617.
    • (2007) J Bacteriol , vol.189 , pp. 2610-2617
    • Shelburne III, S.A.1    Fang, H.2    Okorafor, N.3    Sumby, P.4    Sitkiewicz, I.5    Keith, D.6
  • 52
    • 47249150528 scopus 로고    scopus 로고
    • Molecular characterization of group A Streptococcus maltodextrin catabolism and its role in pharyngitis
    • Shelburne, S.A., 3rd., Keith, D.B., Davenport, M.T., Horstmann, N., Brennan, R.G. Musser, J.M. (2008) Molecular characterization of group A Streptococcus maltodextrin catabolism and its role in pharyngitis. Mol Microbiol 69 : 436 452.
    • (2008) Mol Microbiol , vol.69 , pp. 436-452
    • Shelburne III, S.A.1    Keith, D.B.2    Davenport, M.T.3    Horstmann, N.4    Brennan, R.G.5    Musser, J.M.6
  • 53
    • 70350148680 scopus 로고    scopus 로고
    • Contribution of AmyA, an extracellular alpha-glucan degrading enzyme, to group A streptococcal host-pathogen interaction
    • Shelburne, S.A., 3rd., Keith, D.B., Davenport, M.T., Beres, S.B., Carroll, R.K. Musser, J.M. (2009) Contribution of AmyA, an extracellular alpha-glucan degrading enzyme, to group A streptococcal host-pathogen interaction. Mol Microbiol 74 : 159 174.
    • (2009) Mol Microbiol , vol.74 , pp. 159-174
    • Shelburne III, S.A.1    Keith, D.B.2    Davenport, M.T.3    Beres, S.B.4    Carroll, R.K.5    Musser, J.M.6
  • 54
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: Towards improved functional annotations of alpha-amylase-related proteins
    • Stam, M.R., Danchin, E.G., Rancurel, C., Coutinho, P.M. Henrissat, B. (2006) Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of alpha-amylase-related proteins. Protein Eng Des Sel 19 : 555 562.
    • (2006) Protein Eng des Sel , vol.19 , pp. 555-562
    • Stam, M.R.1    Danchin, E.G.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 55
    • 0032536508 scopus 로고    scopus 로고
    • A thermodynamic study of the binding of linear and cyclic oligosaccharides to the maltodextrin-binding protein of Escherichia coli
    • Thomson, J., Liu, Y., Sturtevant, J.M. Quiocho, F.A. (1998) A thermodynamic study of the binding of linear and cyclic oligosaccharides to the maltodextrin-binding protein of Escherichia coli. Biophys Chem 70 : 101 108.
    • (1998) Biophys Chem , vol.70 , pp. 101-108
    • Thomson, J.1    Liu, Y.2    Sturtevant, J.M.3    Quiocho, F.A.4
  • 56
    • 34247115617 scopus 로고    scopus 로고
    • Structural basis for cyclodextrin recognition by Thermoactinomyces vulgaris cyclo/maltodextrin-binding protein
    • Tonozuka, T., Sogawa, A., Yamada, M., Matsumoto, N., Yoshida, H., Kamitori, S., et al. (2007) Structural basis for cyclodextrin recognition by Thermoactinomyces vulgaris cyclo/maltodextrin-binding protein. FEBS J 274 : 2109 2120.
    • (2007) FEBS J , vol.274 , pp. 2109-2120
    • Tonozuka, T.1    Sogawa, A.2    Yamada, M.3    Matsumoto, N.4    Yoshida, H.5    Kamitori, S.6
  • 57
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A.A., Richelle, J. Wodak, S.J. (1999) SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D Biol Crystallogr 55 : 191 205.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 58
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J.F. Lin, L.N. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 179 : 131 137.
    • (1989) Anal Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.