메뉴 건너뛰기




Volumn 5, Issue 10, 2010, Pages

Of bits and bugs - on the use of bioinformatics and a bacterial crystal structure to solve a eukaryotic repeat- protein structure

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DROSOPHILA PROTEIN;

EID: 78149492329     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0013402     Document Type: Article
Times cited : (20)

References (50)
  • 1
    • 38749149916 scopus 로고    scopus 로고
    • Protein crystallization: From purified protein to diffraction-quality crystal
    • Chayen NE, Saridakis E (2008) Protein crystallization: from purified protein to diffraction-quality crystal. Nat Methods 5: 147-153.
    • (2008) Nat Methods , vol.5 , pp. 147-153
    • Chayen, N.E.1    Saridakis, E.2
  • 2
    • 59349103076 scopus 로고    scopus 로고
    • Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data
    • Price WN, 2nd, Chen Y, Handelman SK, Neely H, Manor P, et al. (2009) Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data. Nat Biotechnol 27: 51-57.
    • (2009) Nat Biotechnol , vol.27 , pp. 51-57
    • Price II, W.N.1    Chen, Y.2    Handelman, S.K.3    Neely, H.4    Manor, P.5
  • 3
    • 26444615377 scopus 로고    scopus 로고
    • Highthroughput limited proteolysis/mass spectrometry for protein domain elucidation
    • Gao X, Bain K, Bonanno JB, Buchanan M, Henderson D, et al. (2005) Highthroughput limited proteolysis/mass spectrometry for protein domain elucidation. J Struct Funct Genomics 6: 129-134.
    • (2005) J Struct Funct Genomics , vol.6 , pp. 129-134
    • Gao, X.1    Bain, K.2    Bonanno, J.B.3    Buchanan, M.4    Henderson, D.5
  • 4
    • 13844311014 scopus 로고    scopus 로고
    • NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline
    • Page R, Peti W, Wilson IA, Stevens RC, Wüthrich K (2005) NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline. Proc Natl Acad Sci U S A 102: 1901-1905.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1901-1905
    • Page, R.1    Peti, W.2    Wilson, I.A.3    Stevens, R.C.4    Wüthrich, K.5
  • 5
    • 68349097394 scopus 로고    scopus 로고
    • Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)
    • Hura GL, Menon AL, Hammel M, Rambo RP, Poole FL, 2nd, et al. (2009) Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS). Nat Methods 6: 606-612.
    • (2009) Nat Methods , vol.6 , pp. 606-612
    • Hura, G.L.1    Menon, A.L.2    Hammel, M.3    Rambo, R.P.4    Poole II, F.L.5
  • 6
    • 0037441549 scopus 로고    scopus 로고
    • Strategies for structural proteomics of prokaryotes: Quantifying the advantages of studying orthologous proteins and of using both NMR and X-ray crystallography approaches
    • Savchenko A, Yee A, Khachatryan A, Skarina T, Evdokimova E, et al. (2003) Strategies for structural proteomics of prokaryotes: Quantifying the advantages of studying orthologous proteins and of using both NMR and X-ray crystallography approaches. Proteins 50: 392-399.
    • (2003) Proteins , vol.50 , pp. 392-399
    • Savchenko, A.1    Yee, A.2    Khachatryan, A.3    Skarina, T.4    Evdokimova, E.5
  • 7
  • 8
    • 33645972948 scopus 로고    scopus 로고
    • Servers for protein structure prediction
    • Fischer D (2006) Servers for protein structure prediction. Curr Opin Struct Biol 16: 178-182.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 178-182
    • Fischer, D.1
  • 9
    • 73249115808 scopus 로고    scopus 로고
    • X-ray structure of Pur-alpha reveals a Whirly-like fold and an unusual nucleic-acid binding surface
    • Graebsch A, Roche S, Niessing D (2009) X-ray structure of Pur-alpha reveals a Whirly-like fold and an unusual nucleic-acid binding surface. Proc Natl Acad Sci U S A 106: 18521-18526.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 18521-18526
    • Graebsch, A.1    Roche, S.2    Niessing, D.3
  • 10
    • 0141557777 scopus 로고    scopus 로고
    • Pur-alpha is essential for postnatal brain development and developmentally coupled cellular proliferation as revealed by genetic inactivation in the mouse
    • Khalili K, Del Valle L, Muralidharan V, Gault WJ, Darbinian N, et al. (2003) Pur-alpha is essential for postnatal brain development and developmentally coupled cellular proliferation as revealed by genetic inactivation in the mouse. Mol Cell Biol 23: 6857-6875.
    • (2003) Mol Cell Biol , vol.23 , pp. 6857-6875
    • Khalili, K.1    Del Valle, L.2    Muralidharan, V.3    Gault, W.J.4    Darbinian, N.5
  • 11
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule
    • Kanai Y, Dohmae N, Hirokawa N (2004) Kinesin transports RNA: isolation and characterization of an RNA-transporting granule. Neuron 43: 513-525.
    • (2004) Neuron , vol.43 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 12
    • 59449092121 scopus 로고    scopus 로고
    • Multiple roles for Puralpha in cellular and viral regulation
    • White MK, Johnson EM, Khalili K (2009) Multiple roles for Puralpha in cellular and viral regulation. Cell Cycle 8: 1-7.
    • (2009) Cell Cycle , vol.8 , pp. 1-7
    • White, M.K.1    Johnson, E.M.2    Khalili, K.3
  • 13
    • 0026453350 scopus 로고
    • Sequence of cDNA comprising the human pur gene and sequence-specific single-stranded-DNA-binding properties of the encoded protein
    • Bergemann AD, Ma ZW, Johnson EM (1992) Sequence of cDNA comprising the human pur gene and sequence-specific single-stranded-DNA-binding properties of the encoded protein. Mol Cell Biol 12: 5673-5682.
    • (1992) Mol Cell Biol , vol.12 , pp. 5673-5682
    • Bergemann, A.D.1    Ma, Z.W.2    Johnson, E.M.3
  • 14
    • 40749144066 scopus 로고    scopus 로고
    • De novo identification of highly diverged protein repeats by probabilistic consistency
    • Biegert A, Söding J (2008) De novo identification of highly diverged protein repeats by probabilistic consistency. Bioinformatics 24: 807-814.
    • (2008) Bioinformatics , vol.24 , pp. 807-814
    • Biegert, A.1    Söding, J.2
  • 15
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding J, Biegert A, Lupas AN (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Research 33: W374-378.
    • (2005) Nucleic Acids Research , vol.33
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 16
    • 0034257920 scopus 로고    scopus 로고
    • Puralpha: A multifunctional singlestranded DNA- and RNA-binding protein
    • Gallia GL, Johnson EM, Khalili K (2000) Puralpha: a multifunctional singlestranded DNA- and RNA-binding protein. Nucleic Acids Res 28: 3197-3205.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3197-3205
    • Gallia, G.L.1    Johnson, E.M.2    Khalili, K.3
  • 17
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search progams
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search progams. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 22
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77: 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 23
    • 42449161827 scopus 로고    scopus 로고
    • The interface of protein-protein complexes: Analysis of contacts and prediction of interactions
    • Bahadur RP, Zacharias M (2008) The interface of protein-protein complexes: analysis of contacts and prediction of interactions. Cell Mol Life Sci 65: 1059-1072.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1059-1072
    • Bahadur, R.P.1    Zacharias, M.2
  • 24
    • 74249104499 scopus 로고    scopus 로고
    • Fast and accurate automatic structure prediction with HHpred
    • Hildebrand A, Remmert M, Biegert A, Söding J (2009) Fast and accurate automatic structure prediction with HHpred. Proteins 77(Suppl 9): 128-132.
    • (2009) Proteins , vol.77 , Issue.SUPPL 9 , pp. 128-132
    • Hildebrand, A.1    Remmert, M.2    Biegert, A.3    Söding, J.4
  • 25
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C, Lesk AM (1986) The relation between the divergence of sequence and structure in proteins. EMBO J 5: 823-826.
    • (1986) EMBO J , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 26
    • 0036408311 scopus 로고    scopus 로고
    • Sequence variations within protein families are linearly related to structural variations
    • Koehl P, Levitt M (2002) Sequence variations within protein families are linearly related to structural variations. J Mol Biol 323: 551-562.
    • (2002) J Mol Biol , vol.323 , pp. 551-562
    • Koehl, P.1    Levitt, M.2
  • 27
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost B (1999) Twilight zone of protein sequence alignments. Protein Eng 12: 85-94.
    • (1999) Protein Eng , vol.12 , pp. 85-94
    • Rost, B.1
  • 32
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: Modular design for efficient function
    • Lunde BM, Moore C, Varani G (2007) RNA-binding proteins: modular design for efficient function. Nat Rev Mol Cell Biol 8: 479-490.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 33
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of Selenomethionyl Proteins for Phase Determination
    • In: Charles W, Carter J, Sweet RM, eds
    • Doublie S (1997) Preparation of Selenomethionyl Proteins for Phase Determination. In: Charles W, Carter J, Sweet RM, eds. Meth Enzymol. pp 523-537.
    • (1997) Meth Enzymol , pp. 523-537
    • Doublie, S.1
  • 36
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM (2008) A short history of SHELX. Acta Crystallogr A 64: 112-122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 37
    • 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 60: 2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 39
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53: 240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 40
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger TC (2002) Automated structure solution, density modification and model building. Acta Crystallogr D 58: 1937-1940.
    • (2002) Acta Crystallogr D , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 41
    • 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 AA, Richelle J, Wodak SJ (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 55: 191-205.
    • (1999) Acta Crystallogr D , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 42
    • 0028103275 scopus 로고
    • The CCP4 Suite:Programs for Protein Crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project N (1994) The CCP4 Suite:Programs for Protein Crystallography. Acta Crystallogr D 50: 760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 43
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on positionspecific scoring matrices
    • Jones DT (1999) Protein secondary structure prediction based on positionspecific scoring matrices. J Mol Biol 292: 195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 44
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Söding J (2005) Protein homology detection by HMM-HMM comparison. Bioinformatics 21: 951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Söding, J.1
  • 45
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 46
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R, Bowie JU, Eisenberg D (1992) Assessment of protein models with three-dimensional profiles. Nature 356: 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 47
    • 0032540222 scopus 로고    scopus 로고
    • Assessing protein structures with a non-local atomic interaction energy
    • Melo F, Feytmans E (1998) Assessing protein structures with a non-local atomic interaction energy. J Mol Biol 277: 1141-1152.
    • (1998) J Mol Biol , vol.277 , pp. 1141-1152
    • Melo, F.1    Feytmans, E.2
  • 49
    • 0027172789 scopus 로고
    • A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions
    • Wong I, Lohman TM (1993) A double-filter method for nitrocellulose-filter binding: application to protein-nucleic acid interactions. Proc Natl Acad SciUS A 90: 5428-5432.
    • (1993) Proc Natl Acad SciUS A , vol.90 , pp. 5428-5432
    • Wong, I.1    Lohman, T.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.