메뉴 건너뛰기




Volumn 34, Issue WEB. SERV. ISS., 2006, Pages

PreBI: Prediction of biological interfaces of proteins in crystals

Author keywords

[No Author keywords available]

Indexed keywords

TELOMERIC REPEAT BINDING FACTOR 2; MULTIPROTEIN COMPLEX; PROTEIN;

EID: 33747863302     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkl267     Document Type: Article
Times cited : (13)

References (14)
  • 1
    • 18044397545 scopus 로고    scopus 로고
    • Progress of structural genomics initiatives: An analysis of solved target structures
    • Todd,A.E., Marsden,R.L., Thornton,J.M. and Orengo,C.A. (2005) Progress of structural genomics initiatives: an analysis of solved target structures. J. Mol. Biol., 348, 1235-1260.
    • (2005) J. Mol. Biol. , vol.348 , pp. 1235-1260
    • Todd, A.E.1    Marsden, R.L.2    Thornton, J.M.3    Orengo, C.A.4
  • 2
    • 0037305974 scopus 로고    scopus 로고
    • Overview of structural genomics: From structure to function
    • Zhang,C. and Kim,S.H. (2003) Overview of structural genomics: from structure to function. Curr. Opin. Chem. Biol., 7, 28-32.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 28-32
    • Zhang, C.1    Kim, S.H.2
  • 3
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick,K. and Thornton,J.M. (1998) PQS: a protein quaternary structure file server. Trends Biochem. Sci., 23, 358-361.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 4
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • Ponstingl,H., Henrick,K. and Thornton,J.M. (2000) Discriminating between homodimeric and monomeric proteins in the crystalline state. Proteins, 41, 47-57.
    • (2000) Proteins , vol.41 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 5
    • 0035914476 scopus 로고    scopus 로고
    • Conservation helps to identify biologically relevant crystal contacts
    • Valdar,W.S. and Thornton,J.M. (2001) Conservation helps to identify biologically relevant crystal contacts. J. Mol. Biol., 313, 399-416.
    • (2001) J. Mol. Biol. , vol.313 , pp. 399-416
    • Valdar, W.S.1    Thornton, J.M.2
  • 6
    • 0034847376 scopus 로고    scopus 로고
    • Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2
    • Fairall,L., Chapman,L., Moss,H., de Lange,T. and Rhodes,D. (2001) Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. Mol. Cell, 8, 351-361.
    • (2001) Mol. Cell , vol.8 , pp. 351-361
    • Fairall, L.1    Chapman, L.2    Moss, H.3    de Lange, T.4    Rhodes, D.5
  • 8
    • 0000758624 scopus 로고
    • Numerical calculations of electrostatic potentials of protein-solvent systems by the self consistent boundary method
    • Nakamura,H. and Nishida,S. (1987) Numerical calculations of electrostatic potentials of protein-solvent systems by the self consistent boundary method. J. Phys. Soc. Jpn., 56, 1609-1622.
    • (1987) J. Phys. Soc. Jpn. , vol.56 , pp. 1609-1622
    • Nakamura, H.1    Nishida, S.2
  • 9
    • 0023338543 scopus 로고
    • Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides
    • Ooi,T., Oobatake,M., Nemethy,G. and Scheraga,H.A. (1987) Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides. Proc. Natl Acad. Sci. USA, 84, 3086-3090.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 3086-3090
    • Ooi, T.1    Oobatake, M.2    Nemethy, G.3    Scheraga, H.A.4
  • 10
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly,M.L. (1983) Solvent-accessible surfaces of proteins and nucleic acids. Science, 221, 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 11
    • 2542557409 scopus 로고    scopus 로고
    • Structure-based prediction of DNA-binding sites on proteins using the empirical preference of electrostatic potential and the shape of molecular surfaces
    • Tsuchiya,Y., Kinoshita,K. and Nakamura,H. (2004) Structure-based prediction of DNA-binding sites on proteins using the empirical preference of electrostatic potential and the shape of molecular surfaces. Proteins, 55, 885-894.
    • (2004) Proteins , vol.55 , pp. 885-894
    • Tsuchiya, Y.1    Kinoshita, K.2    Nakamura, H.3
  • 13
    • 3042683893 scopus 로고    scopus 로고
    • eF-site and PDBjViewer: Database and viewer for protein functional sites
    • Kinoshita,K. and Nakamura,H. (2004) eF-site and PDBjViewer: database and viewer for protein functional sites. Bioinformatics, 20, 1329-1330.
    • (2004) Bioinformatics , vol.20 , pp. 1329-1330
    • Kinoshita, K.1    Nakamura, H.2
  • 14
    • 0028186046 scopus 로고
    • Using the FASTA program to search protein and DNA sequence databases
    • Pearson,W.R. (1994) Using the FASTA program to search protein and DNA sequence databases. Met. Mol. Biol., 24, 307-331.
    • (1994) Met. Mol. Biol. , vol.24 , pp. 307-331
    • Pearson, W.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.