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Volumn 82, Issue 8, 2014, Pages 1553-1562

Second Antibody Modeling Assessment (AMA-II)

Author keywords

Antigen binding site; Canonical structures; Homology modeling; Immunoglobulin; X ray structure

Indexed keywords

ANTIBODY COMBINING SITE; ANTIBODY STRUCTURE; CONFORMATION; CRYSTAL STRUCTURE; EDITORIAL; MOLECULAR MODEL; PRIORITY JOURNAL; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; MOLECULAR GENETICS; MOUSE; PROTEIN CONFORMATION; RABBIT; X RAY CRYSTALLOGRAPHY;

EID: 84904420055     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24567     Document Type: Editorial
Times cited : (119)

References (21)
  • 1
    • 84856483987 scopus 로고    scopus 로고
    • Leveraging SBDD in protein therapeutic development: antibody engineering
    • Gilliland G, Luo J, Vafa O, Almagro J. Leveraging SBDD in protein therapeutic development: antibody engineering. Methods Mol Biol 2012;841:321-349.
    • (2012) Methods Mol Biol , vol.841 , pp. 321-349
    • Gilliland, G.1    Luo, J.2    Vafa, O.3    Almagro, J.4
  • 2
    • 50549090182 scopus 로고    scopus 로고
    • PIGS: automatic prediction of antibody structures
    • Marcatili P, Rosi A, Tramontano A. PIGS: automatic prediction of antibody structures. Bioinformatics 2008;24:1953-1954.
    • (2008) Bioinformatics , vol.24 , pp. 1953-1954
    • Marcatili, P.1    Rosi, A.2    Tramontano, A.3
  • 3
    • 67849111558 scopus 로고    scopus 로고
    • RosettaAntibody: antibody variable region homology modeling server
    • Sircar A, Kim E, Gray J. RosettaAntibody: antibody variable region homology modeling server. Nucleic Acids Res 2009;37:W474-W479.
    • (2009) Nucleic Acids Res , vol.37
    • Sircar, A.1    Kim, E.2    Gray, J.3
  • 8
    • 84904470524 scopus 로고    scopus 로고
    • Structural evidence for a constrained conformation of short CDR-L3 in antibodies
    • Teplyakov A, Obmolova G, Malia TJ, Luo J, Gilliland GL. Structural evidence for a constrained conformation of short CDR-L3 in antibodies. Proteins 2014;82:1679-1683.
    • (2014) Proteins , vol.82 , pp. 1679-1683
    • Teplyakov, A.1    Obmolova, G.2    Malia, T.J.3    Luo, J.4    Gilliland, G.L.5
  • 11
    • 84904498280 scopus 로고    scopus 로고
    • Crystal structure determination of anti-DNA Fab A52
    • Stanfield RL, Eilat D. Crystal structure determination of anti-DNA Fab A52. Proteins 2014;82:1674-1678.
    • (2014) Proteins , vol.82 , pp. 1674-1678
    • Stanfield, R.L.1    Eilat, D.2
  • 12
    • 84904461597 scopus 로고    scopus 로고
    • Automated antibody structure prediction using accelrys tools: results and best practices
    • Fasnacht M, Butenhof K, Goupil A, Hernandez-Guzman F, Huang H, Yan L. Automated antibody structure prediction using accelrys tools: results and best practices. Proteins 2014;82:1636-1645.
    • (2014) Proteins , vol.82 , pp. 1636-1645
    • Fasnacht, M.1    Butenhof, K.2    Goupil, A.3    Hernandez-Guzman, F.4    Huang, H.5    Yan, L.6
  • 13
    • 84904509953 scopus 로고    scopus 로고
    • Assessment of fully automated antibody modeling protocols
    • Maier J, Labute P. Assessment of fully automated antibody modeling protocols. Proteins 2014;82:1599-1610.
    • (2014) Proteins , vol.82 , pp. 1599-1610
    • Maier, J.1    Labute, P.2
  • 15
    • 84904468725 scopus 로고    scopus 로고
    • Blind prediction performance of RosettaAntibody 3.0: grafting, relaxation, kinematic loop modeling, and full CDR optimization
    • Weitzner B, Kuroda D, Marze N, Xu J, Gray J. Blind prediction performance of RosettaAntibody 3.0: grafting, relaxation, kinematic loop modeling, and full CDR optimization. Proteins 2014;82:1611-1623.
    • (2014) Proteins , vol.82 , pp. 1611-1623
    • Weitzner, B.1    Kuroda, D.2    Marze, N.3    Xu, J.4    Gray, J.5
  • 16
    • 84904460487 scopus 로고    scopus 로고
    • Antibody structure determination using a combination of homology modeling and energy-based refinement and loop prediction
    • Zhu K, Pearlman D, Day T, Warshaviak D, Murrett C, Friesner R. Antibody structure determination using a combination of homology modeling and energy-based refinement and loop prediction. Proteins. 2014;82:1646-1655.
    • (2014) Proteins , vol.82 , pp. 1646-1655
    • Zhu, K.1    Pearlman, D.2    Day, T.3    Warshaviak, D.4    Murrett, C.5    Friesner, R.6
  • 17
    • 84904504150 scopus 로고    scopus 로고
    • Automated aufbau of antibody structures from given sequences using macromoltek's SmrtMolAntibody
    • Berrondo M, Kaufmann S, Berrondo M. Automated aufbau of antibody structures from given sequences using macromoltek's SmrtMolAntibody. Proteins 2014;82:1636-1645.
    • (2014) Proteins , vol.82 , pp. 1636-1645
    • Berrondo, M.1    Kaufmann, S.2    Berrondo, M.3
  • 19
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia C, Lesk AM. Canonical structures for the hypervariable regions of immunoglobulins. J Mol Biol 1987;196:901-917.
    • (1987) J Mol Biol , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 20
    • 57349097173 scopus 로고    scopus 로고
    • Structural classification of CDR-H3 revisited: a lesson in antibody modeling
    • Kuroda D, Shirai H, Kobori M, Nakamura H. Structural classification of CDR-H3 revisited: a lesson in antibody modeling. Proteins 2008;73:608-620.
    • (2008) Proteins , vol.73 , pp. 608-620
    • Kuroda, D.1    Shirai, H.2    Kobori, M.3    Nakamura, H.4
  • 21
    • 83455220717 scopus 로고    scopus 로고
    • A protocol for computer-based protein structure and function prediction
    • Roy A1, Xu D, Poisson J, Zhang Y. A protocol for computer-based protein structure and function prediction. J Vis Exp 2011;3:e3259.
    • (2011) J Vis Exp , vol.3
    • Roy, A.1    Xu, D.2    Poisson, J.3    Zhang, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.