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Volumn 14, Issue 1, 2013, Pages

Filling out the structural map of the NTF2-like superfamily

Author keywords

3D structure; JCSG; Ligand binding; NTF2 like superfamily; Protein family; Protein function prediction; Protein structure

Indexed keywords

3D STRUCTURE; JCSG; LIGAND BINDING; NTF2-LIKE SUPERFAMILY; PROTEIN FAMILY; PROTEIN FUNCTION PREDICTION; PROTEIN STRUCTURES;

EID: 84887684997     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-14-327     Document Type: Article
Times cited : (45)

References (51)
  • 1
    • 0030593377 scopus 로고    scopus 로고
    • The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2)
    • 10.1006/jmbi.1996.0411, 8757804
    • Bullock TL, Clarkson WD, Kent HM, Stewart M. The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2). J Mol Biol 1996, 260(3):422-431. 10.1006/jmbi.1996.0411, 8757804.
    • (1996) J Mol Biol , vol.260 , Issue.3 , pp. 422-431
    • Bullock, T.L.1    Clarkson, W.D.2    Kent, H.M.3    Stewart, M.4
  • 2
    • 3142559476 scopus 로고    scopus 로고
    • Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation
    • 10.1038/sj.emboj.7600201, 404321, 15071504
    • Sultana A, Kallio P, Jansson A, Wang JS, Niemi J, Mantsala P, Schneider G. Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation. EMBO J 2004, 23(9):1911-1921. 10.1038/sj.emboj.7600201, 404321, 15071504.
    • (2004) EMBO J , vol.23 , Issue.9 , pp. 1911-1921
    • Sultana, A.1    Kallio, P.2    Jansson, A.3    Wang, J.S.4    Niemi, J.5    Mantsala, P.6    Schneider, G.7
  • 3
    • 0032516487 scopus 로고    scopus 로고
    • Cryogenic X-ray crystal structure analysis for the complex of scytalone dehydratase of a rice blast fungus and its tight-binding inhibitor, carpropamid: the structural basis of tight-binding inhibition
    • 10.1021/bi980321b, 9665698
    • Nakasako M, Motoyama T, Kurahashi Y, Yamaguchi I. Cryogenic X-ray crystal structure analysis for the complex of scytalone dehydratase of a rice blast fungus and its tight-binding inhibitor, carpropamid: the structural basis of tight-binding inhibition. Biochemistry 1998, 37(28):9931-9939. 10.1021/bi980321b, 9665698.
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 9931-9939
    • Nakasako, M.1    Motoyama, T.2    Kurahashi, Y.3    Yamaguchi, I.4
  • 4
    • 0037863737 scopus 로고    scopus 로고
    • Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site
    • 10.1093/emboj/cdg275, 156771, 12773375
    • Arand M, Hallberg BM, Zou J, Bergfors T, Oesch F, van der Werf MJ, De Bont JA, Jones TA, Mowbray SL. Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site. EMBO J 2003, 22(11):2583-2592. 10.1093/emboj/cdg275, 156771, 12773375.
    • (2003) EMBO J , vol.22 , Issue.11 , pp. 2583-2592
    • Arand, M.1    Hallberg, B.M.2    Zou, J.3    Bergfors, T.4    Oesch, F.5    van der Werf, M.J.6    De Bont, J.A.7    Jones, T.A.8    Mowbray, S.L.9
  • 5
    • 0001305507 scopus 로고    scopus 로고
    • High-resolution crystal structures of delta5-3-ketosteroid isomerase with and without a reaction intermediate analogue
    • 10.1021/bi971546+, 9369474
    • Kim SW, Cha SS, Cho HS, Kim JS, Ha NC, Cho MJ, Joo S, Kim KK, Choi KY, Oh BH. High-resolution crystal structures of delta5-3-ketosteroid isomerase with and without a reaction intermediate analogue. Biochemistry 1997, 36(46):14030-14036. 10.1021/bi971546+, 9369474.
    • (1997) Biochemistry , vol.36 , Issue.46 , pp. 14030-14036
    • Kim, S.W.1    Cha, S.S.2    Cho, H.S.3    Kim, J.S.4    Ha, N.C.5    Cho, M.J.6    Joo, S.7    Kim, K.K.8    Choi, K.Y.9    Oh, B.H.10
  • 6
    • 2142648724 scopus 로고    scopus 로고
    • CaMKII, an enzyme on the move: regulation of temporospatial localization
    • 10.1124/mi.3.7.386, 14993460
    • Griffith LC, Lu CS, Sun XX. CaMKII, an enzyme on the move: regulation of temporospatial localization. Mol Interv 2003, 3(7):386-403. 10.1124/mi.3.7.386, 14993460.
    • (2003) Mol Interv , vol.3 , Issue.7 , pp. 386-403
    • Griffith, L.C.1    Lu, C.S.2    Sun, X.X.3
  • 7
    • 33646138730 scopus 로고    scopus 로고
    • Mba1, a membrane-associated ribosome receptor in mitochondria
    • 10.1038/sj.emboj.7601070, 1440829, 16601683
    • Ott M, Prestele M, Bauerschmitt H, Funes S, Bonnefoy N, Herrmann JM. Mba1, a membrane-associated ribosome receptor in mitochondria. EMBO J 2006, 25(8):1603-1610. 10.1038/sj.emboj.7601070, 1440829, 16601683.
    • (2006) EMBO J , vol.25 , Issue.8 , pp. 1603-1610
    • Ott, M.1    Prestele, M.2    Bauerschmitt, H.3    Funes, S.4    Bonnefoy, N.5    Herrmann, J.M.6
  • 9
    • 84855804851 scopus 로고    scopus 로고
    • The conjugation protein TcpC from Clostridium perfringens is structurally related to the type IV secretion system protein VirB8 from Gram-negative bacteria
    • 10.1111/j.1365-2958.2011.07930.x, 22150951
    • Porter CJ, Bantwal R, Bannam TL, Rosado CJ, Pearce MC, Adams V, Lyras D, Whisstock JC, Rood JI. The conjugation protein TcpC from Clostridium perfringens is structurally related to the type IV secretion system protein VirB8 from Gram-negative bacteria. Mol Microbiol 2012, 83(2):275-288. 10.1111/j.1365-2958.2011.07930.x, 22150951.
    • (2012) Mol Microbiol , vol.83 , Issue.2 , pp. 275-288
    • Porter, C.J.1    Bantwal, R.2    Bannam, T.L.3    Rosado, C.J.4    Pearce, M.C.5    Adams, V.6    Lyras, D.7    Whisstock, J.C.8    Rood, J.I.9
  • 10
    • 15444380769 scopus 로고    scopus 로고
    • Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori
    • 10.1073/pnas.0408927102, 555499, 15764702
    • Terradot L, Bayliss R, Oomen C, Leonard GA, Baron C, Waksman G. Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori. Proc Natl Acad Sci U S A 2005, 102(12):4596-4601. 10.1073/pnas.0408927102, 555499, 15764702.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.12 , pp. 4596-4601
    • Terradot, L.1    Bayliss, R.2    Oomen, C.3    Leonard, G.A.4    Baron, C.5    Waksman, G.6
  • 11
    • 84862602464 scopus 로고    scopus 로고
    • Polymorphic toxin systems: Comprehensive characterization of trafficking modes, processing, mechanisms of action, immunity and ecology using comparative genomics
    • 10.1186/1745-6150-7-18, 3482391, 22731697
    • Zhang D, De Souza RF, Anantharaman V, Iyer LM, Aravind L. Polymorphic toxin systems: Comprehensive characterization of trafficking modes, processing, mechanisms of action, immunity and ecology using comparative genomics. Biol Direct 2012, 7:18. 10.1186/1745-6150-7-18, 3482391, 22731697.
    • (2012) Biol Direct , vol.7 , pp. 18
    • Zhang, D.1    De Souza, R.F.2    Anantharaman, V.3    Iyer, L.M.4    Aravind, L.5
  • 13
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • 10.1093/nar/gkg556, 168963, 12824317
    • Gouet P, Robert X, Courcelle E. ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res 2003, 31(13):3320-3323. 10.1093/nar/gkg556, 168963, 12824317.
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 14
    • 84864462812 scopus 로고    scopus 로고
    • EvolView, an online tool for visualizing, annotating and managing phylogenetic trees
    • 10.1093/nar/gks576, 3394307, 22695796
    • Zhang H, Gao S, Lercher MJ, Hu S, Chen WH. EvolView, an online tool for visualizing, annotating and managing phylogenetic trees. Nucleic Acids Res 2012, 40:W569-W572. 10.1093/nar/gks576, 3394307, 22695796.
    • (2012) Nucleic Acids Res , vol.40
    • Zhang, H.1    Gao, S.2    Lercher, M.J.3    Hu, S.4    Chen, W.H.5
  • 15
    • 79955684513 scopus 로고    scopus 로고
    • Representative proteomes: a stable, scalable and unbiased proteome set for sequence analysis and functional annotation
    • 10.1371/journal.pone.0018910, 3083393, 21556138
    • Chen C, Natale DA, Finn RD, Huang H, Zhang J, Wu CH, Mazumder R. Representative proteomes: a stable, scalable and unbiased proteome set for sequence analysis and functional annotation. PloS one 2011, 6(4):e18910. 10.1371/journal.pone.0018910, 3083393, 21556138.
    • (2011) PloS one , vol.6 , Issue.4
    • Chen, C.1    Natale, D.A.2    Finn, R.D.3    Huang, H.4    Zhang, J.5    Wu, C.H.6    Mazumder, R.7
  • 16
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • 10.1016/j.jmb.2004.03.016, 15111065
    • Kall L, Krogh A, Sonnhammer EL. A combined transmembrane topology and signal peptide prediction method. J Mol Biol 2004, 338(5):1027-1036. 10.1016/j.jmb.2004.03.016, 15111065.
    • (2004) J Mol Biol , vol.338 , Issue.5 , pp. 1027-1036
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 17
    • 18244415313 scopus 로고    scopus 로고
    • Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes
    • 10.1186/gb-2003-4-2-r11, 151301, 12620121
    • Anantharaman V, Aravind L. Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes. Genome Biol 2003, 4(2):R11. 10.1186/gb-2003-4-2-r11, 151301, 12620121.
    • (2003) Genome Biol , vol.4 , Issue.2
    • Anantharaman, V.1    Aravind, L.2
  • 19
    • 3042581007 scopus 로고    scopus 로고
    • Flexible structure alignment by chaining aligned fragment pairs allowing twists
    • Ye Y, Godzik A. Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics 2003, 19(Suppl 2):ii246-ii255.
    • (2003) Bioinformatics , vol.19 , Issue.SUPPL 2
    • Ye, Y.1    Godzik, A.2
  • 20
    • 0035575802 scopus 로고    scopus 로고
    • Identification of protein fold and catalytic residues of gamma-hexachlorocyclohexane dehydrochlorinase LinA
    • 10.1002/prot.10007, 11746694
    • Nagata Y, Mori K, Takagi M, Murzin AG, Damborsky J. Identification of protein fold and catalytic residues of gamma-hexachlorocyclohexane dehydrochlorinase LinA. Proteins 2001, 45(4):471-477. 10.1002/prot.10007, 11746694.
    • (2001) Proteins , vol.45 , Issue.4 , pp. 471-477
    • Nagata, Y.1    Mori, K.2    Takagi, M.3    Murzin, A.G.4    Damborsky, J.5
  • 21
    • 70350465128 scopus 로고    scopus 로고
    • Structural relationships among proteins with different global topologies and their implications for function annotation strategies
    • 10.1073/pnas.0907971106, 2765090, 19805138
    • Petrey D, Fischer M, Honig B. Structural relationships among proteins with different global topologies and their implications for function annotation strategies. Proc Natl Acad Sci USA 2009, 106(41):17377-17382. 10.1073/pnas.0907971106, 2765090, 19805138.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.41 , pp. 17377-17382
    • Petrey, D.1    Fischer, M.2    Honig, B.3
  • 22
    • 19544388989 scopus 로고    scopus 로고
    • Multiple flexible structure alignment using partial order graphs
    • 10.1093/bioinformatics/bti353, 15746292
    • Ye Y, Godzik A. Multiple flexible structure alignment using partial order graphs. Bioinformatics 2005, 21(10):2362-2369. 10.1093/bioinformatics/bti353, 15746292.
    • (2005) Bioinformatics , vol.21 , Issue.10 , pp. 2362-2369
    • Ye, Y.1    Godzik, A.2
  • 24
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • 10.1093/nar/gkq366, 2896194, 20457744
    • Holm L, Rosenstrom P. Dali server: conservation mapping in 3D. Nucleic Acids Res 2010, 38:W545-W549. 10.1093/nar/gkq366, 2896194, 20457744.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 25
    • 77955039883 scopus 로고    scopus 로고
    • Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation
    • 10.1371/journal.pbio.1000426, 2910593, 20668654
    • Rellos P, Pike AC, Niesen FH, Salah E, Lee WH, Von Delft F, Knapp S. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010, 8(7):e1000426. 10.1371/journal.pbio.1000426, 2910593, 20668654.
    • (2010) PLoS biology , vol.8 , Issue.7
    • Rellos, P.1    Pike, A.C.2    Niesen, F.H.3    Salah, E.4    Lee, W.H.5    Von Delft, F.6    Knapp, S.7
  • 26
    • 0035342617 scopus 로고    scopus 로고
    • Coupling mechanism of the oxaloacetate decarboxylase Na(+) pump
    • 10.1016/S0005-2728(00)00272-3, 11248184
    • Dimroth P, Jockel P, Schmid M. Coupling mechanism of the oxaloacetate decarboxylase Na(+) pump. Biochim Biophys Acta 2001, 1505(1):1-14. 10.1016/S0005-2728(00)00272-3, 11248184.
    • (2001) Biochim Biophys Acta , vol.1505 , Issue.1 , pp. 1-14
    • Dimroth, P.1    Jockel, P.2    Schmid, M.3
  • 28
    • 0038438514 scopus 로고    scopus 로고
    • IMPALA: matching a protein sequence against a collection of PSI-BLAST-constructed position-specific score matrices
    • 10.1093/bioinformatics/15.12.1000, 10745990
    • Schaffer AA, Wolf YI, Ponting CP, Koonin EV, Aravind L, Altschul SF. IMPALA: matching a protein sequence against a collection of PSI-BLAST-constructed position-specific score matrices. Bioinformatics 1999, 15(12):1000-1011. 10.1093/bioinformatics/15.12.1000, 10745990.
    • (1999) Bioinformatics , vol.15 , Issue.12 , pp. 1000-1011
    • Schaffer, A.A.1    Wolf, Y.I.2    Ponting, C.P.3    Koonin, E.V.4    Aravind, L.5    Altschul, S.F.6
  • 29
    • 41149148236 scopus 로고    scopus 로고
    • Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts
    • 10.1002/prot.21786, 18004753
    • Klock HE, Koesema EJ, Knuth MW, Lesley SA. Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts. Proteins 2008, 71(2):982-994. 10.1002/prot.21786, 18004753.
    • (2008) Proteins , vol.71 , Issue.2 , pp. 982-994
    • Klock, H.E.1    Koesema, E.J.2    Knuth, M.W.3    Lesley, S.A.4
  • 30
    • 0037015054 scopus 로고    scopus 로고
    • Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline
    • 10.1073/pnas.142413399, 129326, 12193646
    • Lesley SA, Kuhn P, Godzik A, Deacon AM, Mathews I, Kreusch A, Spraggon G, Klock HE, McMullan D, Shin T, et al. Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. Proc Natl Acad Sci U S A 2002, 99(18):11664-11669. 10.1073/pnas.142413399, 129326, 12193646.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.18 , pp. 11664-11669
    • Lesley, S.A.1    Kuhn, P.2    Godzik, A.3    Deacon, A.M.4    Mathews, I.5    Kreusch, A.6    Spraggon, G.7    Klock, H.E.8    McMullan, D.9    Shin, T.10
  • 32
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 1993, 26:795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 33
    • 76449099287 scopus 로고    scopus 로고
    • Xds
    • 10.1107/S0907444909047337, 2815665, 20124692
    • Kabsch W. Xds. Acta Crystallogr D Biol Crystallogr 2010, 66(2):125-132. 10.1107/S0907444909047337, 2815665, 20124692.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.2 , pp. 125-132
    • Kabsch, W.1
  • 34
    • 71649092785 scopus 로고    scopus 로고
    • Processing diffraction data with MOSFLM
    • Dordrech, The Netherlands: Springer, Read RJ, Sussman JL, volume 245. ISBN 978-1-4020-6314-5
    • Leslie AGW, Powell HR. Processing diffraction data with MOSFLM. Evolving Methods for Macromolecular Crystallography 2007, 41-51. Dordrech, The Netherlands: Springer, Read RJ, Sussman JL, volume 245. ISBN 978-1-4020-6314-5.
    • (2007) Evolving Methods for Macromolecular Crystallography , pp. 41-51
    • Leslie, A.G.W.1    Powell, H.R.2
  • 35
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P. Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 2006, 62(Pt 1):72-82.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , Issue.PART 1 , pp. 72-82
    • Evans, P.1
  • 38
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • 2745878, 12499537
    • Terwilliger TC. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr D Biol Crystallogr 2003, 59(Pt 1):38-44. 2745878, 12499537.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , Issue.PART 1 , pp. 38-44
    • Terwilliger, T.C.1
  • 39
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • 10.1038/nprot.2008.91, 2582149, 18600222
    • Langer G, Cohen SX, Lamzin VS, Perrakis A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nature protocols 2008, 3(7):1171-1179. 10.1038/nprot.2008.91, 2582149, 18600222.
    • (2008) Nature protocols , vol.3 , Issue.7 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 40
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • 10.1107/S0907444906022116, 16929101
    • Cowtan K. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr D Biol Crystallogr 2006, 62(9):1002-1011. 10.1107/S0907444906022116, 16929101.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , Issue.9 , pp. 1002-1011
    • Cowtan, K.1
  • 41
    • 84860285553 scopus 로고    scopus 로고
    • Completion of autobuilt protein models using a database of protein fragments
    • 3322592, 22505253
    • Cowtan K. Completion of autobuilt protein models using a database of protein fragments. Acta Crystallogr D Biol Crystallogr 2012, 68(Pt 4):328-335. 3322592, 22505253.
    • (2012) Acta Crystallogr D Biol Crystallogr , vol.68 , Issue.PART 4 , pp. 328-335
    • Cowtan, K.1
  • 42
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004, 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 43
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn MD, Isupov MN, Murshudov GN. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr D Biol Crystallogr 2001, 57(Pt 1):122-133.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , Issue.PART 1 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 45
    • 80051978793 scopus 로고    scopus 로고
    • Network-based prediction for sources of transcriptional dysregulation using latent pathway identification analysis
    • 10.1073/pnas.1100891108, 3156179, 21788508
    • Pham L, Christadore L, Schaus S, Kolaczyk ED. Network-based prediction for sources of transcriptional dysregulation using latent pathway identification analysis. Proc Natl Acad Sci U S A 2011, 108(32):13347-13352. 10.1073/pnas.1100891108, 3156179, 21788508.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.32 , pp. 13347-13352
    • Pham, L.1    Christadore, L.2    Schaus, S.3    Kolaczyk, E.D.4
  • 47
    • 0025398721 scopus 로고
    • WHAT IF: a molecular modeling and drug design program
    • 10.1016/0263-7855(90)80070-V, 2268628
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph 1990, 8(1):52-56. 10.1016/0263-7855(90)80070-V, 2268628.
    • (1990) J Mol Graph , vol.8 , Issue.1 , pp. 52-56
    • Vriend, G.1
  • 48
    • 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. 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 1999, 55(Pt 1):191-205.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , Issue.PART 1 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 49
  • 50
    • 0030831667 scopus 로고    scopus 로고
    • Validation of protein models from Calpha coordinates alone
    • 10.1006/jmbi.1997.1309, 9344745
    • Kleywegt GJ. Validation of protein models from Calpha coordinates alone. J Mol Biol 1997, 273(2):371-376. 10.1006/jmbi.1997.1309, 9344745.
    • (1997) J Mol Biol , vol.273 , Issue.2 , pp. 371-376
    • Kleywegt, G.J.1
  • 51
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • 10.1016/j.jmb.2007.05.022, 17681537
    • Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007, 372(3):774-797. 10.1016/j.jmb.2007.05.022, 17681537.
    • (2007) J Mol Biol , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.