메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Structure and Function of Cyanobacterial DHDPS and DHDPR

Author keywords

[No Author keywords available]

Indexed keywords

4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE; BACTERIAL PROTEIN; DIHYDRODIPICOLINATE REDUCTASE; HYDROLYASE;

EID: 84995543175     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep37111     Document Type: Article
Times cited : (22)

References (62)
  • 1
    • 77951219030 scopus 로고    scopus 로고
    • eds Doelle, H. W. & Rokem, S. EOLSS Publishers
    • Dogovski, C. et al. In Encyclopedia of Life Support Systems (eds. Doelle, H. W. & Rokem, S.) 116-136 (EOLSS Publishers, 2009).
    • (2009) Encyclopedia of Life Support Systems , pp. 116-136
    • Dogovski, C.1
  • 2
    • 84865655739 scopus 로고    scopus 로고
    • ed Ekinci, D Open Access Publisher
    • Dogovski, C. et al. In Biochemistry (ed. Ekinci, D.) 225-262 (Open Access Publisher, 2012).
    • (2012) Biochemistry , pp. 225-262
    • Dogovski, C.1
  • 3
    • 84948582981 scopus 로고    scopus 로고
    • Quaternary Structure Analyses of an Essential Oligomeric Enzyme
    • Soares da Costa, T. P. et al. Quaternary Structure Analyses of an Essential Oligomeric Enzyme. Methods Enzymol. 562, 205-223 (2015).
    • (2015) Methods Enzymol. , vol.562 , pp. 205-223
    • Soares Da Costa, T.P.1
  • 4
  • 5
    • 34250692637 scopus 로고    scopus 로고
    • Inhibition of lysine biosynthesis: An evolving antibiotic strategy
    • Hutton, C. A., Perugini, M. A. & Gerrard, J. A. Inhibition of lysine biosynthesis: an evolving antibiotic strategy. Mol. Biosyst. 3, 458-465 (2007).
    • (2007) Mol. Biosyst. , vol.3 , pp. 458-465
    • Hutton, C.A.1    Perugini, M.A.2    Gerrard, J.A.3
  • 6
    • 0031012162 scopus 로고    scopus 로고
    • Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy
    • Blickling, S. et al. Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry 36, 24-33 (1997).
    • (1997) Biochemistry , vol.36 , pp. 24-33
    • Blickling, S.1
  • 7
    • 45549122274 scopus 로고    scopus 로고
    • Evolution of quaternary structure in a homotetrameric enzyme
    • Griffin, M. D. et al. Evolution of quaternary structure in a homotetrameric enzyme. J. Mol. Biol. 380, 691-703 (2008).
    • (2008) J. Mol. Biol. , vol.380 , pp. 691-703
    • Griffin, M.D.1
  • 8
    • 0345668475 scopus 로고    scopus 로고
    • Essential Bacillus subtilis genes
    • Kobayashi, K. et al. Essential Bacillus subtilis genes. Proc. Natl. Acad. Sci. USA 100, 4678-4683 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4678-4683
    • Kobayashi, K.1
  • 9
    • 84892534088 scopus 로고    scopus 로고
    • From knock-out phenotype to three-dimensional structure of a promising antibiotic target from Streptococcus pneumoniae
    • Dogovski, C. et al. From knock-out phenotype to three-dimensional structure of a promising antibiotic target from Streptococcus pneumoniae. PLoS One 8, e83419 (2013).
    • (2013) PLoS One , vol.8 , pp. e83419
    • Dogovski, C.1
  • 10
    • 75149118182 scopus 로고    scopus 로고
    • Cloning, expression and crystallization of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus
    • Dommaraju, S. R. et al. Cloning, expression and crystallization of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus. Acta Crystallogr. Sect. F: Struct. Biol. Commun. 66, 55-60 (2010).
    • (2010) Acta Crystallogr. Sect. F: Struct. Biol. Commun. , vol.66 , pp. 55-60
    • Dommaraju, S.R.1
  • 11
    • 79960450056 scopus 로고    scopus 로고
    • Catalytic mechanism and cofactor preference of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus
    • Dommaraju, S. R. et al. Catalytic mechanism and cofactor preference of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus. Arch. Biochem. Biophys. 512, 167-174 (2011).
    • (2011) Arch. Biochem. Biophys. , vol.512 , pp. 167-174
    • Dommaraju, S.R.1
  • 12
    • 77954379663 scopus 로고    scopus 로고
    • Methanococci use the diaminopimelate aminotransferase (DapL) pathway for lysine biosynthesis
    • Liu, Y., White, R. H. & Whitman, W. B. Methanococci use the diaminopimelate aminotransferase (DapL) pathway for lysine biosynthesis. J. Bacteriol. 192, 3304-3310 (2010).
    • (2010) J. Bacteriol. , vol.192 , pp. 3304-3310
    • Liu, Y.1    White, R.H.2    Whitman, W.B.3
  • 13
    • 33645808723 scopus 로고    scopus 로고
    • An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants
    • Hudson, A. O., Singh, B. K., Leustek, T. & Gilvarg, C. An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants. Plant Physiol. 140, 292-301 (2006).
    • (2006) Plant Physiol. , vol.140 , pp. 292-301
    • Hudson, A.O.1    Singh, B.K.2    Leustek, T.3    Gilvarg, C.4
  • 14
    • 84906310372 scopus 로고    scopus 로고
    • Identification of the bona fide DHDPS from a common plant pathogen
    • Atkinson, S. C., Hor, L., Dogovski, C., Dobson, R. C. J. & Perugini, M. A. Identification of the bona fide DHDPS from a common plant pathogen. Proteins 82, 1869-1883 (2014).
    • (2014) Proteins , vol.82 , pp. 1869-1883
    • Atkinson, S.C.1    Hor, L.2    Dogovski, C.3    Dobson, R.C.J.4    Perugini, M.A.5
  • 15
    • 30344464699 scopus 로고    scopus 로고
    • Crystal structure of dihydrodipicolinate synthase (BA3935) from Bacillus anthracis at 1. 94 A resolution
    • Blagova, E. et al. Crystal structure of dihydrodipicolinate synthase (BA3935) from Bacillus anthracis at 1. 94 A resolution. Proteins 62, 297-301 (2006).
    • (2006) Proteins , vol.62 , pp. 297-301
    • Blagova, E.1
  • 16
    • 77949314517 scopus 로고    scopus 로고
    • Substrate-mediated stabilization of a tetrameric drug target reveals Achilles heel in anthrax
    • Voss, J. E. et al. Substrate-mediated stabilization of a tetrameric drug target reveals Achilles heel in anthrax. J. Biol. Chem. 285, 5188-5195 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 5188-5195
    • Voss, J.E.1
  • 17
    • 0028907826 scopus 로고
    • The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2. 5 A resolution
    • Mirwaldt, C., Korndorfer, I. & Huber, R. The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2. 5 A resolution. J. Mol. Biol. 246, 227-239 (1995).
    • (1995) J. Mol. Biol. , vol.246 , pp. 227-239
    • Mirwaldt, C.1    Korndorfer, I.2    Huber, R.3
  • 18
    • 25144446271 scopus 로고    scopus 로고
    • The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance
    • Dobson, R. C. J., Griffin, M. D., Jameson, G. B. & Gerrard, J. A. The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance. Acta. Crystallogr. D. Biol. Crystallogr. 61, 1116-1124 (2005).
    • (2005) Acta. Crystallogr. D. Biol. Crystallogr. , vol.61 , pp. 1116-1124
    • Dobson, R.C.J.1    Griffin, M.D.2    Jameson, G.B.3    Gerrard, J.A.4
  • 19
    • 84978966687 scopus 로고    scopus 로고
    • Structural determinants defining the allosteric inhibition of an essential antibiotic target
    • Soares da Costa, T. P. et al. Structural determinants defining the allosteric inhibition of an essential antibiotic target. Structure 8, 1282-1291 (2016).
    • (2016) Structure , vol.8 , pp. 1282-1291
    • Soares Da Costa, T.P.1
  • 20
    • 42449110007 scopus 로고    scopus 로고
    • Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis
    • Kefala, G. et al. Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis. Biochem. J. 411, 351-360 (2008).
    • (2008) Biochem. J. , vol.411 , pp. 351-360
    • Kefala, G.1
  • 21
    • 79955835071 scopus 로고    scopus 로고
    • Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa
    • Kaur, N. et al. Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa. Int. J. Biol. Macromol. 48, 779-787 (2011).
    • (2011) Int. J. Biol. Macromol. , vol.48 , pp. 779-787
    • Kaur, N.1
  • 22
    • 55549137411 scopus 로고    scopus 로고
    • Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen
    • Burgess, B. R. et al. Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen. J. Biol. Chem. 283, 27598-27603 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 27598-27603
    • Burgess, B.R.1
  • 23
    • 48749085398 scopus 로고    scopus 로고
    • Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase
    • Girish, T. S., Sharma, E. & Gopal, B. Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase. FEBS Lett. 582, 2923-2930 (2008).
    • (2008) FEBS Lett. , vol.582 , pp. 2923-2930
    • Girish, T.S.1    Sharma, E.2    Gopal, B.3
  • 25
    • 74149094662 scopus 로고    scopus 로고
    • Exploring the dihydrodipicolinate synthase tetramer: How resilient is the dimer-dimer interface Arch
    • Griffin, M. D. W., Dobson, R. C. J., Gerrard, J. A. & Perugini, M. A. Exploring the dihydrodipicolinate synthase tetramer: how resilient is the dimer-dimer interface Arch. Biochem. Biophys. 494, 58-63 (2010).
    • (2010) Biochem. Biophys. , vol.494 , pp. 58-63
    • Griffin, M.D.W.1    Dobson, R.C.J.2    Gerrard, J.A.3    Perugini, M.A.4
  • 26
    • 0031566028 scopus 로고    scopus 로고
    • Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure
    • Blickling, S. et al. Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure. J. Mol. Biol. 274, 608-621 (1997).
    • (1997) J. Mol. Biol. , vol.274 , pp. 608-621
    • Blickling, S.1
  • 27
    • 84862637299 scopus 로고    scopus 로고
    • Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine
    • Atkinson, S. C. et al. Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine. PLoS ONE 7 e38318 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e38318
    • Atkinson, S.C.1
  • 28
    • 84863615811 scopus 로고    scopus 로고
    • Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana
    • Griffin, M. D. et al. Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana. PLoS One 7, e40318 (2012).
    • (2012) PLoS One , vol.7 , pp. e40318
    • Griffin, M.D.1
  • 29
    • 84874301737 scopus 로고    scopus 로고
    • Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition
    • Atkinson. S. C. et al. Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition. Plant Mol. Biol. 81, 431-446 (2013).
    • (2013) Plant Mol. Biol. , vol.81 , pp. 431-446
    • Atkinson, S.C.1
  • 30
    • 78149346456 scopus 로고    scopus 로고
    • Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from the psychrophile Shewanella benthica
    • Wubben, J. M. et al. Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from the psychrophile Shewanella benthica. Acta Crystallogr. Sect. F Struct. Biol. Commun. 66, 1511-1516 (2010).
    • (2010) Acta Crystallogr. Sect. F Struct. Biol. Commun. , vol.66 , pp. 1511-1516
    • Wubben, J.M.1
  • 31
    • 84975778601 scopus 로고    scopus 로고
    • Structural insight into dihydrodipicolinate reductase from Corybebacterium glutamicum for lysine biosynthesis
    • Sagong, H. Y. & Kim, K. J. Structural insight into dihydrodipicolinate reductase from Corybebacterium glutamicum for lysine biosynthesis. J. Microbiol. Biotechnol. 2, 226-232 (2016).
    • (2016) J. Microbiol. Biotechnol. , vol.2 , pp. 226-232
    • Sagong, H.Y.1    Kim, K.J.2
  • 32
    • 0028937651 scopus 로고
    • Three-dimensional structure of Escherichia coli sihydrodipicolinate reductase
    • Scapin, G., Blanchard, J. S. & Sacchettini, J. C. Three-dimensional structure of Escherichia coli sihydrodipicolinate reductase. Biochemistry 34, 3502-3512 (1995).
    • (1995) Biochemistry , vol.34 , pp. 3502-3512
    • Scapin, G.1    Blanchard, J.S.2    Sacchettini, J.C.3
  • 33
    • 0029820832 scopus 로고    scopus 로고
    • Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: Thermodynamic and structural analysis of binary complexes
    • Reddy, S. G., Scapin, G. & Blanchard, J. S. Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Biochemistry 35, 13294-13302 (1996).
    • (1996) Biochemistry , vol.35 , pp. 13294-13302
    • Reddy, S.G.1    Scapin, G.2    Blanchard, J.S.3
  • 34
    • 0041317450 scopus 로고    scopus 로고
    • The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2, 6-PDC and-NADPH-2, 6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity
    • Cirilli, M., Zheng, R., Scapin, G. & Blanchard, J. S. The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2, 6-PDC and-NADPH-2, 6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity. Biochemistry 42, 10644-10650 (2003).
    • (2003) Biochemistry , vol.42 , pp. 10644-10650
    • Cirilli, M.1    Zheng, R.2    Scapin, G.3    Blanchard, J.S.4
  • 35
    • 74549158341 scopus 로고    scopus 로고
    • The structure of dihydrodipicolinate reductase (DapB) from Mycobacterium tuberculosis in three crystal forms
    • Janowski. R., Kefala, G. & Weiss, M. S. The structure of dihydrodipicolinate reductase (DapB) from Mycobacterium tuberculosis in three crystal forms. Acta Crystallogr. Sect. D Struct. Biol. Cryst. Commun. 66, 61-72 (2010).
    • (2010) Acta Crystallogr. Sect. D Struct. Biol. Cryst. Commun. , vol.66 , pp. 61-72
    • Janowski, R.1    Kefala, G.2    Weiss, M.S.3
  • 36
    • 80051779531 scopus 로고    scopus 로고
    • Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB)
    • Girish, T. S., Navratna, V. & Gopal, B. Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB). FEBS Lett. 585, 2561-2567 (2011).
    • (2011) FEBS Lett. , vol.585 , pp. 2561-2567
    • Girish, T.S.1    Navratna, V.2    Gopal, B.3
  • 37
    • 0002815512 scopus 로고
    • D-glyceraldehyde-3-phosphate dehydrogenase: Three-dimensional structure and evolutionary significance
    • Buehner M., Ford G. C., Moras D., Olsen K. W. & Rossman M. G. D-glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance. Proc. Natl. Acad. Sci. USA 70, 3052-3054 (1973)
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3052-3054
    • Buehner, M.1    Ford, G.C.2    Moras, D.3    Olsen, K.W.4    Rossman, M.G.5
  • 39
    • 84893411166 scopus 로고    scopus 로고
    • Complete genome sequence of Anabaena variabilis ATCC 29413
    • Thiel, T. et al. Complete genome sequence of Anabaena variabilis ATCC 29413. Stand. Genomic Sci. 9, 562-573 (2014).
    • (2014) Stand. Genomic Sci. , vol.9 , pp. 562-573
    • Thiel, T.1
  • 40
    • 59749098709 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Bacillus anthracis in the presence of pyruvate
    • Voss, J. E. et al. Expression, purification, crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Bacillus anthracis in the presence of pyruvate. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65, 188-191 (2009).
    • (2009) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.65 , pp. 188-191
    • Voss, J.E.1
  • 41
    • 84864127998 scopus 로고    scopus 로고
    • Comparative structure and function analyses of native and histagged forms of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus
    • Dogovski, C., Dommaraju, S. R., Small, L. C. & Perugini, M. A. Comparative structure and function analyses of native and histagged forms of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus. Prot. Expr. Purif. 85, 66-76 (2012).
    • (2012) Prot. Expr. Purif. , vol.85 , pp. 66-76
    • Dogovski, C.1    Dommaraju, S.R.2    Small, L.C.3    Perugini, M.A.4
  • 42
    • 84855254333 scopus 로고    scopus 로고
    • Protein-binding assays in biological liquids using microscale thermophoresis
    • Wienken, C. J., Baaske, P., Rothbauer, U., Braun, D. & Duhr, S. Protein-binding assays in biological liquids using microscale thermophoresis. Nat. Commun. 1, 100 (2010).
    • (2010) Nat. Commun. , vol.1 , pp. 100
    • Wienken, C.J.1    Baaske, P.2    Rothbauer, U.3    Braun, D.4    Duhr, S.5
  • 43
    • 22844439302 scopus 로고    scopus 로고
    • Insight into the self-association of key enzymes from pathogenic species
    • Perugini, M. A. et al. Insight into the self-association of key enzymes from pathogenic species. Eur. Biophys. J. 34, 469-476 (2005).
    • (2005) Eur. Biophys. J. , vol.34 , pp. 469-476
    • Perugini, M.A.1
  • 44
    • 84947567875 scopus 로고    scopus 로고
    • Extracellular peptidases of the cereal pathogen Fusarium graminearum
    • Lowe, R. G. T. et al. Extracellular peptidases of the cereal pathogen Fusarium graminearum. Front. Plant. Sci. 6, doi: 10. 3389/ fpls. 2015. 00962 (2015).
    • (2015) Front. Plant. Sci. , vol.6
    • Lowe, R.G.T.1
  • 45
    • 84925852266 scopus 로고    scopus 로고
    • The recently identified modifier of murine metastable epialleles, Rearranged L-Myc Fusion, is involved in maintaining epigenetic marks at CpG island shores and enhancers
    • Harten, S. K. et al. The recently identified modifier of murine metastable epialleles, Rearranged L-Myc Fusion, is involved in maintaining epigenetic marks at CpG island shores and enhancers. BMC. Biol. 13, doi: 10. 1186/s12915-015-0128-2 (2015).
    • (2015) BMC. Biol. , vol.13
    • Harten, S.K.1
  • 46
    • 1842425027 scopus 로고    scopus 로고
    • Properties of GDP-mannose pyrophosphorylase, a critical enzyme and drug target in Leishmania mexicana
    • Davis, A. J., Perugini, M. A., Smith, B. J., Stewart, J., Ilg, T., Hodder, A. & Handman, E. Properties of GDP-mannose pyrophosphorylase, a critical enzyme and drug target in Leishmania mexicana. J. Biol. Chem. 279, 12462-12468 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 12462-12468
    • Davis, A.J.1    Perugini, M.A.2    Smith, B.J.3    Stewart, J.4    Ilg, T.5    Hodder, A.6    Handman, E.7
  • 47
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • Sreerama, N., Venyaminov, S. W. & Woody, R. W. Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 287, 243-251 (2000).
    • (2000) Anal. Biochem. , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.W.2    Woody, R.W.3
  • 48
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. & Woody, R. W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260 (2000).
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 50
    • 84994291710 scopus 로고    scopus 로고
    • Dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis
    • Peverelli, M. G., Soares da Costa, T. P., Kirby, N. & Perugini, M. A. Dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis. J. Biol. Chem. 291, 9785-9795 (2016).
    • (2016) J. Biol. Chem. , vol.291 , pp. 9785-9795
    • Peverelli, M.G.1    Soares Da Costa, T.P.2    Kirby, N.3    Perugini, M.A.4
  • 52
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606-1619 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 53
    • 0034711265 scopus 로고    scopus 로고
    • Self-association of human apolipoprotein E3 and E4 in the presence and absence of phospholipid
    • Perugini, M. A., Schuck, P. & Howlett, G. J. Self-association of human apolipoprotein E3 and E4 in the presence and absence of phospholipid. J. Biol. Chem. 275, 36758-36765 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 36758-36765
    • Perugini, M.A.1    Schuck, P.2    Howlett, G.J.3
  • 54
    • 18744407250 scopus 로고    scopus 로고
    • Differences in the binding capacity of human apolipoprotein E3 and E4 to sizefractionated lipid emulsions
    • Perugini, M. A., Schuck, P. & Howlett, G. J. Differences in the binding capacity of human apolipoprotein E3 and E4 to sizefractionated lipid emulsions. Eur. J. Biochem. 269, 5939-5949 (2002).
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5939-5949
    • Perugini, M.A.1    Schuck, P.2    Howlett, G.J.3
  • 55
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck, P., Perugini, M. A., Gonzales, N. R., Howlett, G. J. & Schubert, D. Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys. J. 82, 1096-1111 (2002).
    • (2002) Biophys. J. , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 59
    • 23844492576 scopus 로고    scopus 로고
    • Auto-Rickshaw: An automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment
    • Panjikar, S., Parthasarathy V., Lamzin, V. S., Weiss, M. S. & Tucker, P. A. Auto-Rickshaw: an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment. Acta Crystallogr. Sect. D Struct. Biol. Cryst. Commun. 61, 449-457 (2005).
    • (2005) Acta Crystallogr. Sect. D Struct. Biol. Cryst. Commun. , vol.61 , pp. 449-457
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 60
    • 16644364842 scopus 로고    scopus 로고
    • REFMAC5 dictionary: Organization of prior chemical knowledge and guidelines for its use
    • Vagin, A. A. et al. REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use. Acta Crystallogr. Sect. D Struct. Biol. Cryst. Commun. 60, 2284-2295 (2004).
    • (2004) Acta Crystallogr. Sect. D Struct. Biol. Cryst. Commun. , vol.60 , pp. 2284-2295
    • Vagin, A.A.1
  • 62
    • 56749132990 scopus 로고    scopus 로고
    • Conserved main-chain peptide distortions: A proposed role for Ile203 in catalysis by dihydrodipicolinate synthase
    • Dobson, R. C. J. et al. Conserved main-chain peptide distortions: a proposed role for Ile203 in catalysis by dihydrodipicolinate synthase. Protein Sci. 17, 2080-2090 (2008).
    • (2008) Protein Sci. , vol.17 , pp. 2080-2090
    • Dobson, R.C.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.