메뉴 건너뛰기




Volumn 366, Issue 1, 2007, Pages 117-131

New Insights on the Role of the γ-Herpesvirus Uracil-DNA Glycosylase Leucine Loop Revealed by the Structure of the Epstein-Barr Virus Enzyme in Complex with an Inhibitor Protein

Author keywords

crystal structure; DNA repair; Epstein Barr virus; lytic protein; uracil DNA glycosylase

Indexed keywords

DOUBLE STRANDED DNA; ENZYME INHIBITOR; HYDROLASE; LEUCINE; UNCLASSIFIED DRUG; URACIL; URACIL DNA GLYCOSIDASE; URACIL DNA GLYCOSYLASE INHIBITOR; URACIL TRIPHOSPHATE HYDROLASE;

EID: 33846285662     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.007     Document Type: Article
Times cited : (27)

References (57)
  • 5
    • 85047694072 scopus 로고    scopus 로고
    • Epstein-Barr virus-associated lymphomas
    • Gandhi M.K. Epstein-Barr virus-associated lymphomas. Expert Rev. Anti Infect. Ther. 4 (2006) 77-89
    • (2006) Expert Rev. Anti Infect. Ther. , vol.4 , pp. 77-89
    • Gandhi, M.K.1
  • 6
    • 21844464297 scopus 로고    scopus 로고
    • C → T mutagenesis and gamma-radiation sensitivity due to deficiency in the Smug1 and Ung DNA glycosylases
    • An Q., Robins P., Lindahl T., and Barnes D.E. C → T mutagenesis and gamma-radiation sensitivity due to deficiency in the Smug1 and Ung DNA glycosylases. EMBO J. 24 (2005) 2205-2213
    • (2005) EMBO J. , vol.24 , pp. 2205-2213
    • An, Q.1    Robins, P.2    Lindahl, T.3    Barnes, D.E.4
  • 7
    • 0000476915 scopus 로고
    • An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues
    • Lindahl T. An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues. Proc. Natl Acad. Sci. USA 71 (1974) 3649-3653
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 3649-3653
    • Lindahl, T.1
  • 8
    • 24044460415 scopus 로고    scopus 로고
    • DNA base damage recognition and removal: new twists and grooves
    • Huffman J.L., Sundheim O., and Tainer J.A. DNA base damage recognition and removal: new twists and grooves. Mutat. Res. 577 (2005) 55-76
    • (2005) Mutat. Res. , vol.577 , pp. 55-76
    • Huffman, J.L.1    Sundheim, O.2    Tainer, J.A.3
  • 9
    • 13944277344 scopus 로고    scopus 로고
    • HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle
    • Priet S., Gros N., Navarro J.M., Boretto J., Canard B., Querat G., and Sire J. HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle. Mol. Cell 17 (2005) 479-490
    • (2005) Mol. Cell , vol.17 , pp. 479-490
    • Priet, S.1    Gros, N.2    Navarro, J.M.3    Boretto, J.4    Canard, B.5    Querat, G.6    Sire, J.7
  • 10
    • 0028291733 scopus 로고
    • Evidence that the herpes simplex virus type 1 uracil DNA glycosylase is required for efficient viral replication and latency in the murine nervous system
    • Pyles R.B., and Thompson R.L. Evidence that the herpes simplex virus type 1 uracil DNA glycosylase is required for efficient viral replication and latency in the murine nervous system. J. Virol. 68 (1994) 4963-4972
    • (1994) J. Virol. , vol.68 , pp. 4963-4972
    • Pyles, R.B.1    Thompson, R.L.2
  • 11
    • 0029968637 scopus 로고    scopus 로고
    • Human cytomegalovirus uracil DNA glycosylase is required for the normal temporal regulation of both DNA synthesis and viral replication
    • Prichard M.N., Duke G.M., and Mocarski E.S. Human cytomegalovirus uracil DNA glycosylase is required for the normal temporal regulation of both DNA synthesis and viral replication. J. Virol. 70 (1996) 3018-3025
    • (1996) J. Virol. , vol.70 , pp. 3018-3025
    • Prichard, M.N.1    Duke, G.M.2    Mocarski, E.S.3
  • 12
    • 0029845801 scopus 로고    scopus 로고
    • Mutations in active-site residues of the uracil-DNA glycosylase encoded by vaccinia virus are incompatible with virus viability
    • Ellison K.S., Peng W., and McFadden G. Mutations in active-site residues of the uracil-DNA glycosylase encoded by vaccinia virus are incompatible with virus viability. J. Virol. 70 (1996) 7965-7973
    • (1996) J. Virol. , vol.70 , pp. 7965-7973
    • Ellison, K.S.1    Peng, W.2    McFadden, G.3
  • 13
    • 0032567095 scopus 로고    scopus 로고
    • Expression of a uracil DNA glycosylase (UNG) inhibitor in mammalian cells: varicella-zoster virus can replicate in vitro in the absence of detectable UNG activity
    • Reddy S.M., Williams M., and Cohen J.I. Expression of a uracil DNA glycosylase (UNG) inhibitor in mammalian cells: varicella-zoster virus can replicate in vitro in the absence of detectable UNG activity. Virology 251 (1998) 393-401
    • (1998) Virology , vol.251 , pp. 393-401
    • Reddy, S.M.1    Williams, M.2    Cohen, J.I.3
  • 14
    • 0036788148 scopus 로고    scopus 로고
    • Roles of uracil-DNA glycosylase and dUTPase in virus replication
    • Chen R., Wang H., and Mansky L.M. Roles of uracil-DNA glycosylase and dUTPase in virus replication. J. Gen. Virol. 83 (2002) 2339-2345
    • (2002) J. Gen. Virol. , vol.83 , pp. 2339-2345
    • Chen, R.1    Wang, H.2    Mansky, L.M.3
  • 15
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan H.E., Standal R., and Slupphaug G. DNA glycosylases in the base excision repair of DNA. Biochem. J. 325 (1997) 1-16
    • (1997) Biochem. J. , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 16
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • Savva R., McAuley-Hecht K., Brown T., and Pearl L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 373 (1995) 487-493
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 17
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis
    • Mol C.D., Arvai A.S., Slupphaug G., Kavli B., Alseth I., Krokan H.E., and Tainer J.A. Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell 80 (1995) 478-869
    • (1995) Cell , vol.80 , pp. 478-869
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 18
    • 3643055084 scopus 로고    scopus 로고
    • X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG
    • Ravishankar R., Bidya Sagar M., Roy S., Purnapatre K., Handa P., Varshney U., and Vijayan M. X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG. Nucl. Acids Res. 26 (1998) 4880-4887
    • (1998) Nucl. Acids Res. , vol.26 , pp. 4880-4887
    • Ravishankar, R.1    Bidya Sagar, M.2    Roy, S.3    Purnapatre, K.4    Handa, P.5    Varshney, U.6    Vijayan, M.7
  • 19
    • 0042568932 scopus 로고    scopus 로고
    • The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features
    • Leiros I., Moe E., Lanes O., Smalas A.O., and Willassen N.P. The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features. Acta Crystallog. sect. D 59 (2003) 1357-1365
    • (2003) Acta Crystallog. sect. D , vol.59 , pp. 1357-1365
    • Leiros, I.1    Moe, E.2    Lanes, O.3    Smalas, A.O.4    Willassen, N.P.5
  • 20
    • 25144524607 scopus 로고    scopus 로고
    • Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans
    • Leiros I., Moe E., Smalas A.O., and McSweeney S. Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans. Acta Crystallog. sect. D 61 (2005) 1049-1056
    • (2005) Acta Crystallog. sect. D , vol.61 , pp. 1049-1056
    • Leiros, I.1    Moe, E.2    Smalas, A.O.3    McSweeney, S.4
  • 21
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions
    • Barrett T.E., Savva R., Panayotou G., Barlow T., Brown T., Jiricny J., and Pearl L.H. Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92 (1998) 117-129
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1    Savva, R.2    Panayotou, G.3    Barlow, T.4    Brown, T.5    Jiricny, J.6    Pearl, L.H.7
  • 22
    • 0038771139 scopus 로고    scopus 로고
    • Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1
    • Wibley J.E., Waters T.R., Haushalter K., Verdine G.L., and Pearl L.H. Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1. Mol. Cell 11 (2003) 1647-1659
    • (2003) Mol. Cell , vol.11 , pp. 1647-1659
    • Wibley, J.E.1    Waters, T.R.2    Haushalter, K.3    Verdine, G.L.4    Pearl, L.H.5
  • 23
    • 0037799511 scopus 로고    scopus 로고
    • A novel uracil-DNA glycosylase family related to the helix-hairpin-helix DNA glycosylase superfamily
    • Chung J.H., Im E.K., Park H.Y., Kwon J.H., Lee S., Oh J., et al. A novel uracil-DNA glycosylase family related to the helix-hairpin-helix DNA glycosylase superfamily. Nucl. Acids Res. 31 (2003) 2045-2055
    • (2003) Nucl. Acids Res. , vol.31 , pp. 2045-2055
    • Chung, J.H.1    Im, E.K.2    Park, H.Y.3    Kwon, J.H.4    Lee, S.5    Oh, J.6
  • 25
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • Parikh S.S., Mol C.D., Slupphaug G., Bharati S., Krokan H.E., and Tainer J.A. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J. 17 (1998) 5214-5226
    • (1998) EMBO J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 26
    • 0029084487 scopus 로고
    • Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA
    • Mol C.D., Arvai A.S., Sanderson R.J., Slupphaug G., Kavli B., Krokan H.E., et al. Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA. Cell 82 (1995) 701-708
    • (1995) Cell , vol.82 , pp. 701-708
    • Mol, C.D.1    Arvai, A.S.2    Sanderson, R.J.3    Slupphaug, G.4    Kavli, B.5    Krokan, H.E.6
  • 27
    • 0029115366 scopus 로고
    • Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex
    • Savva R., and Pearl L.H. Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex. Nature Struct. Biol. 2 (1995) 752-757
    • (1995) Nature Struct. Biol. , vol.2 , pp. 752-757
    • Savva, R.1    Pearl, L.H.2
  • 28
    • 0033605817 scopus 로고    scopus 로고
    • Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase
    • Putnam C.D., Shroyer M.J., Lundquist A.J., Mol C.D., Arvai A.S., Mosbaugh D.W., and Tainer J.A. Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase. J. Mol. Biol. 287 (1999) 331-346
    • (1999) J. Mol. Biol. , vol.287 , pp. 331-346
    • Putnam, C.D.1    Shroyer, M.J.2    Lundquist, A.J.3    Mol, C.D.4    Arvai, A.S.5    Mosbaugh, D.W.6    Tainer, J.A.7
  • 29
    • 0016782046 scopus 로고
    • N-Glycosidase activity in extracts of Bacillus subtilis and its inhibition after infection with bacteriophage PBS2
    • Friedberg E.C., Ganesan A.K., and Minton K. N-Glycosidase activity in extracts of Bacillus subtilis and its inhibition after infection with bacteriophage PBS2. J. Virol. 16 (1975) 315-321
    • (1975) J. Virol. , vol.16 , pp. 315-321
    • Friedberg, E.C.1    Ganesan, A.K.2    Minton, K.3
  • 30
    • 0000933459 scopus 로고
    • Replacement of thymidylic acid by deoxyuridylic acid in the deoxyribonucleic acid of a transducing phage for Bacillus subtilis
    • Takahashi I., and Marmur J. Replacement of thymidylic acid by deoxyuridylic acid in the deoxyribonucleic acid of a transducing phage for Bacillus subtilis. Nature 197 (1963) 794-795
    • (1963) Nature , vol.197 , pp. 794-795
    • Takahashi, I.1    Marmur, J.2
  • 31
    • 0019864721 scopus 로고
    • Specificity of the bacteriophage PBS2 induced inhibitor of uracil-DNA glycosylase
    • Karran P., Cone R., and Friedberg E.C. Specificity of the bacteriophage PBS2 induced inhibitor of uracil-DNA glycosylase. Biochemistry 20 (1981) 6092-6096
    • (1981) Biochemistry , vol.20 , pp. 6092-6096
    • Karran, P.1    Cone, R.2    Friedberg, E.C.3
  • 32
    • 33646193797 scopus 로고    scopus 로고
    • A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1
    • Krusong K., Carpenter E.P., Bellamy S.R., Savva R., and Baldwin G.S. A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1. J. Biol. Chem. 281 (2006) 4983-4992
    • (2006) J. Biol. Chem. , vol.281 , pp. 4983-4992
    • Krusong, K.1    Carpenter, E.P.2    Bellamy, S.R.3    Savva, R.4    Baldwin, G.S.5
  • 33
    • 0036024512 scopus 로고    scopus 로고
    • Domain closure and action of uracil DNA glycosylase (UDG): structures of new crystal forms containing the Escherichia coli enzyme and a comparative study of the known structures involving UDG
    • Saikrishnan K., Bidya Sagar M., Ravishankar R., Roy S., Purnapatre K., Handa P., et al. Domain closure and action of uracil DNA glycosylase (UDG): structures of new crystal forms containing the Escherichia coli enzyme and a comparative study of the known structures involving UDG. Acta Crystallog. sect. D 58 (2002) 1269-1276
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 1269-1276
    • Saikrishnan, K.1    Bidya Sagar, M.2    Ravishankar, R.3    Roy, S.4    Purnapatre, K.5    Handa, P.6
  • 34
    • 0026574664 scopus 로고
    • Characterization of the Escherichia coli uracil-DNA glycosylase-inhibitor protein complex
    • Bennett S.E., and Mosbaugh D.W. Characterization of the Escherichia coli uracil-DNA glycosylase-inhibitor protein complex. J. Biol. Chem. 267 (1992) 22512-22521
    • (1992) J. Biol. Chem. , vol.267 , pp. 22512-22521
    • Bennett, S.E.1    Mosbaugh, D.W.2
  • 35
    • 0035883852 scopus 로고    scopus 로고
    • A kinetic analysis of substrate recognition by uracil-DNA glycosylase from herpes simplex virus type 1
    • Bellamy S.R., and Baldwin G.S. A kinetic analysis of substrate recognition by uracil-DNA glycosylase from herpes simplex virus type 1. Nucl. Acids Res. 29 (2001) 3857-3863
    • (2001) Nucl. Acids Res. , vol.29 , pp. 3857-3863
    • Bellamy, S.R.1    Baldwin, G.S.2
  • 36
    • 0019878052 scopus 로고
    • Uracil DNa-glycosylase from HeLa cells: general properties, substrate specificity and effect of uracil analogs
    • Krokan H., and Wittwer C.U. Uracil DNa-glycosylase from HeLa cells: general properties, substrate specificity and effect of uracil analogs. Nucl. Acids Res. 9 (1981) 2599-2613
    • (1981) Nucl. Acids Res. , vol.9 , pp. 2599-2613
    • Krokan, H.1    Wittwer, C.U.2
  • 37
    • 0032531934 scopus 로고    scopus 로고
    • Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively
    • Otterlei M., Haug T., Nagelhus T.A., Slupphaug G., Lindmo T., and Krokan H.E. Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively. Nucl. Acids Res. 26 (1998) 4611-4617
    • (1998) Nucl. Acids Res. , vol.26 , pp. 4611-4617
    • Otterlei, M.1    Haug, T.2    Nagelhus, T.A.3    Slupphaug, G.4    Lindmo, T.5    Krokan, H.E.6
  • 38
    • 9144238218 scopus 로고    scopus 로고
    • Mutational analysis of arginine 276 in the leucine-loop of human uracil-DNA glycosylase
    • Chen C.Y., Mosbaugh D.W., and Bennett S.E. Mutational analysis of arginine 276 in the leucine-loop of human uracil-DNA glycosylase. J. Biol. Chem. 279 (2004) 48177-48188
    • (2004) J. Biol. Chem. , vol.279 , pp. 48177-48188
    • Chen, C.Y.1    Mosbaugh, D.W.2    Bennett, S.E.3
  • 39
    • 0027761910 scopus 로고
    • Kinetics of the uracil-DNA glycosylase/inhibitor protein association. Ung interaction with Ugi, nucleic acids, and uracil compounds
    • Bennett S.E., Schimerlik M.I., and Mosbaugh D.W. Kinetics of the uracil-DNA glycosylase/inhibitor protein association. Ung interaction with Ugi, nucleic acids, and uracil compounds. J. Biol. Chem. 268 (1993) 26879-26885
    • (1993) J. Biol. Chem. , vol.268 , pp. 26879-26885
    • Bennett, S.E.1    Schimerlik, M.I.2    Mosbaugh, D.W.3
  • 40
    • 0025726472 scopus 로고
    • Overproduction and characterization of the uracil-DNA glycosylase inhibitor of bacteriophage PBS2
    • Wang Z.G., Smith D.G., and Mosbaugh D.W. Overproduction and characterization of the uracil-DNA glycosylase inhibitor of bacteriophage PBS2. Gene 99 (1991) 31-37
    • (1991) Gene , vol.99 , pp. 31-37
    • Wang, Z.G.1    Smith, D.G.2    Mosbaugh, D.W.3
  • 42
    • 0029086874 scopus 로고
    • Cloning and expression of the uracil-DNA glycosylase inhibitor (UGI) from bacteriophage PBS-1 and crystallization of a uracil-DNA glycosylase-UGI complex
    • Savva R., and Pearl L.H. Cloning and expression of the uracil-DNA glycosylase inhibitor (UGI) from bacteriophage PBS-1 and crystallization of a uracil-DNA glycosylase-UGI complex. Proteins: Struct. Funct. Genet. 22 (1995) 287-289
    • (1995) Proteins: Struct. Funct. Genet. , vol.22 , pp. 287-289
    • Savva, R.1    Pearl, L.H.2
  • 43
    • 0032529485 scopus 로고    scopus 로고
    • 2-Aminopurine fluorescence studies of base stacking interactions at abasic sites in DNA: metal-ion and base sequence effects
    • Stivers J.T. 2-Aminopurine fluorescence studies of base stacking interactions at abasic sites in DNA: metal-ion and base sequence effects. Nucl. Acids Res. 26 (1998) 3837-3844
    • (1998) Nucl. Acids Res. , vol.26 , pp. 3837-3844
    • Stivers, J.T.1
  • 44
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., and Burk D. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56 (1934) 658-666
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 45
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallog. sect. D 62 (2006) 48-57
    • (2006) Acta Crystallog. sect. D , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 46
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 47
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin A., and Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallog. sect. D 56 (2000) 1622-1624
    • (2000) Acta Crystallog. sect. D , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 48
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 49
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 51
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 52
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., F., and M. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    F.,, M.4
  • 53
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., and Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8 (1995) 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 54
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., and Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93 (1996) 13-20
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 56
    • 13544251502 scopus 로고    scopus 로고
    • The case for open-source software in drug discovery
    • DeLano W.L. The case for open-source software in drug discovery. Drug Discov. Today 10 (2005) 213-217
    • (2005) Drug Discov. Today , vol.10 , pp. 213-217
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.