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Volumn 31, Issue 7, 2015, Pages 1138-1140

The Victor C++ library for protein representation and advanced manipulation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 84929143784     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btu773     Document Type: Article
Times cited : (5)

References (27)
  • 1
    • 77957803889 scopus 로고    scopus 로고
    • OpenStructure: A flexible software framework for computational structural biology
    • Biasini, M. et al. (2010) OpenStructure: a flexible software framework for computational structural biology. Bioinformatics, 26, 2626-2628.
    • (2010) Bioinformatics , vol.26 , pp. 2626-2628
    • Biasini, M.1
  • 2
    • 20844462588 scopus 로고    scopus 로고
    • MollDE: A homology modeling framework you can click with
    • Canutescu, A.A. and Dunbrack, R.L. (2005) MollDE: a homology modeling framework you can click with. Bioinformatics, 21, 2914-2916.
    • (2005) Bioinformatics , vol.21 , pp. 2914-2916
    • Canutescu, A.A.1    Dunbrack, R.L.2
  • 3
    • 34548118802 scopus 로고    scopus 로고
    • StrBioLib: A Java library for development of custom computational structural biology applications
    • Chandonia, J.-M. (2007) StrBioLib: a Java library for development of custom computational structural biology applications. Bioinformatics, 23, 2018-2020.
    • (2007) Bioinformatics , vol.23 , pp. 2018-2020
    • Chandonia, J.-M.1
  • 4
    • 13844292778 scopus 로고    scopus 로고
    • The SSEA server for protein secondary structure alignment
    • Fontana, P. et al. (2005) The SSEA server for protein secondary structure alignment. Bioinformatics, 21, 393-395.
    • (2005) Bioinformatics , vol.21 , pp. 393-395
    • Fontana, P.1
  • 6
    • 84925286085 scopus 로고    scopus 로고
    • NeEMO: A method using residue interaction networks to improve prediction of protein stability upon mutation
    • Giollo, M. et al. (2014) NeEMO: a method using residue interaction networks to improve prediction of protein stability upon mutation. BMC Genomics, 15 (Suppl 4), S7.
    • (2014) BMC Genomics , vol.15 , pp. S7
    • Giollo, M.1
  • 7
    • 34147192127 scopus 로고    scopus 로고
    • Biskit-A software platform for structural bioinformatics
    • Grünberg, R. et al. (2007) Biskit-a software platform for structural bioinformatics. Bioinformatics, 23, 769-770.
    • (2007) Bioinformatics , vol.23 , pp. 769-770
    • Grünberg, R.1
  • 8
    • 69249212321 scopus 로고    scopus 로고
    • Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: A historical perspective
    • Guex, N. et al. (2009) Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: a historical perspective. Electrophoresis, 30 (Suppl 1), S162-173.
    • (2009) Electrophoresis , vol.30 , pp. S162-173
    • Guex, N.1
  • 9
    • 77958140046 scopus 로고    scopus 로고
    • BALL-biochemical algorithms library 1.3
    • Hildebrandt, A. et al. (2010) BALL-biochemical algorithms library 1.3. BMC Bioinformatics, 11, 531.
    • (2010) BMC Bioinformatics , vol.11 , pp. 531
    • Hildebrandt, A.1
  • 10
    • 84904800658 scopus 로고    scopus 로고
    • Enhancing UCSF Chimera through web services
    • Huang, C.C. et al. (2014) Enhancing UCSF Chimera through web services. Nucleic Acids Res., 42, W478-W484.
    • (2014) Nucleic Acids Res. , vol.42 , pp. W478-W484
    • Huang, C.C.1
  • 11
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • 27-28
    • Humphrey, W. et al. (1996) VMD: visual molecular dynamics. J. Mol. Graph., 14, 33-38, 27-28.
    • (1996) J. Mol. Graph. , vol.14 , pp. 33-38
    • Humphrey, W.1
  • 12
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 13
    • 84906312795 scopus 로고    scopus 로고
    • WeFold: A coopetition for protein structure prediction
    • Khoury, G.A. et al. (2014) WeFold: a coopetition for protein structure prediction. Proteins, 82, 1850-1868.
    • (2014) Proteins , vol.82 , pp. 1850-1868
    • Khoury, G.A.1
  • 14
    • 84892968997 scopus 로고    scopus 로고
    • CASP10 results compared to those of previous CASP experiments
    • Kryshtafovych, A. et al. (2014) CASP10 results compared to those of previous CASP experiments. Proteins, 82 (Suppl 2), 164-174.
    • (2014) Proteins , vol.82 , pp. 164-174
    • Kryshtafovych, A.1
  • 15
    • 84862572941 scopus 로고    scopus 로고
    • Structural informatics, modeling, and design with an open-source molecular software Library (MSL)
    • Kulp, D.W. et al. (2012) Structural informatics, modeling, and design with an open-source molecular software Library (MSL). J. Comput. Chem., 33, 1645-1661.
    • (2012) J. Comput. Chem. , vol.33 , pp. 1645-1661
    • Kulp, D.W.1
  • 16
    • 77951946532 scopus 로고    scopus 로고
    • ESBTL: Efficient PDB parser and data structure for the structural and geometric analysis of biological macromolecules
    • Loriot, S. et al. (2010) ESBTL: efficient PDB parser and data structure for the structural and geometric analysis of biological macromolecules. Bioinformatics, 26, 1127-1128.
    • (2010) Bioinformatics , vol.26 , pp. 1127-1128
    • Loriot, S.1
  • 17
    • 33644971388 scopus 로고    scopus 로고
    • Variable gap penalty for protein sequencestructure alignment
    • Madhusudhan, M.S. et al. (2006) Variable gap penalty for protein sequencestructure alignment. Protein Eng. Des. Sel., 19, 129-133.
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 129-133
    • Madhusudhan, M.S.1
  • 18
    • 79960149420 scopus 로고    scopus 로고
    • RING: Networking interacting residues, evolutionary information and energetics in protein structures
    • Martin, A.J.M. et al. (2011) RING: networking interacting residues, evolutionary information and energetics in protein structures. Bioinformatics, 27, 2003-2005.
    • (2011) Bioinformatics , vol.27 , pp. 2003-2005
    • Martin, A.J.M.1
  • 19
    • 84893021599 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP)-round x
    • Moult, J. et al. (2014) Critical assessment of methods of protein structure prediction (CASP)-round x. Proteins, 82 (Suppl 2), 1-6.
    • (2014) Proteins , vol.82 , pp. 1-6
    • Moult, J.1
  • 20
    • 66149165880 scopus 로고    scopus 로고
    • PTools: An opensource molecular docking library
    • Saladin, A. et al. (2009) PTools: an opensource molecular docking library. BMC Struct. Biol., 9, 27.
    • (2009) BMC Struct. Biol. , vol.9 , pp. 27
    • Saladin, A.1
  • 21
    • 84884194561 scopus 로고    scopus 로고
    • The polarizable atomic multipole-based AMOEBA force field for proteins
    • Shi, Y. et al. (2013) The polarizable atomic multipole-based AMOEBA force field for proteins. J. Chem. Theory Comput., 9, 4046-4063.
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 4046-4063
    • Shi, Y.1
  • 22
    • 0033028454 scopus 로고    scopus 로고
    • PSIC: Profile extraction from sequence alignments with position-specific counts of independent observations
    • Sunyaev, S.R. et al. (1999) PSIC: profile extraction from sequence alignments with position-specific counts of independent observations. Protein Eng., 12, 387-394.
    • (1999) Protein Eng. , vol.12 , pp. 387-394
    • Sunyaev, S.R.1
  • 23
    • 0036096608 scopus 로고    scopus 로고
    • A divide and conquer approach to fast loop modeling
    • Tosatto, S.C.E. et al. (2002) A divide and conquer approach to fast loop modeling. Protein Eng., 15, 279-286.
    • (2002) Protein Eng. , vol.15 , pp. 279-286
    • Tosatto, S.C.E.1
  • 24
    • 33947324043 scopus 로고    scopus 로고
    • Align: A C++ class library and web server for rapid sequence alignment prototyping
    • Tosatto, S.C.E. et al. (2006) Align: a C++ class library and web server for rapid sequence alignment prototyping. Curr. Drug Discov. Technol., 3, 167-173.
    • (2006) Curr. Drug Discov. Technol. , vol.3 , pp. 167-173
    • Tosatto, S.C.E.1
  • 25
    • 28144448406 scopus 로고    scopus 로고
    • The victor/FRST function for model quality estimation
    • Tosatto, S.C.E. (2005) The victor/FRST function for model quality estimation. J. Comput. Biol., 12, 1316-1327.
    • (2005) J. Comput. Biol. , vol.12 , pp. 1316-1327
    • Tosatto, S.C.E.1
  • 26
    • 34249778085 scopus 로고    scopus 로고
    • TAP score: Torsion angle propensity normalization applied to local protein structure evaluation
    • Tosatto, S.C.E. and Battistutta, R. (2007) TAP score: torsion angle propensity normalization applied to local protein structure evaluation. BMC Bioinformatics, 8, 155.
    • (2007) BMC Bioinformatics , vol.8 , pp. 155
    • Tosatto, S.C.E.1    Battistutta, R.2
  • 27
    • 2442663920 scopus 로고    scopus 로고
    • Scoring profile-to-profile sequence alignments
    • Wang, G. and Dunbrack, R.L. (2004) Scoring profile-to-profile sequence alignments. Protein Sci., 13, 1612-1626.
    • (2004) Protein Sci. , vol.13 , pp. 1612-1626
    • Wang, G.1    Dunbrack, R.L.2


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