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Volumn 37, Issue SUPPL. 3, 1999, Pages 126-132

Cooperative approach for the protein fold recognition

Author keywords

CASP; Compatibility function; Homology; Structure prediction; Threading

Indexed keywords

PROTEIN; BACTERIAL PROTEIN; CARRIER PROTEIN; CYANOVIRIN N; CYTOCHROME; LIGASE; RNA 3' TERMINAL PHOSPHATE CYCLASE; RNA 3'-TERMINAL PHOSPHATE CYCLASE;

EID: 0032613334     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(1999)37:3+<126::AID-PROT17>3.0.CO;2-8     Document Type: Article
Times cited : (14)

References (39)
  • 1
    • 0028818340 scopus 로고
    • Protein structure prediction by threading methods: Evaluation of current technologies
    • Lamer M-R, Rooman MJ, Wodak SJ. Protein structure prediction by threading methods: evaluation of current technologies. Proteins 1995;23:337-355.
    • (1995) Proteins , vol.23 , pp. 337-355
    • Lamer, M.-R.1    Rooman, M.J.2    Wodak, S.J.3
  • 2
    • 0031307020 scopus 로고    scopus 로고
    • Competitive assessment of protein fold recognition and alignment accuracy
    • Levitt M. Competitive assessment of protein fold recognition and alignment accuracy. Proteins Suppl 1997;1:92-104.
    • (1997) Proteins Suppl , vol.1 , pp. 92-104
    • Levitt, M.1
  • 3
    • 0031303337 scopus 로고    scopus 로고
    • A retrospective analysis of CASP2 threading predictions
    • Marchler-Bauer A, Levitt M, Bryant SH. A retrospective analysis of CASP2 threading predictions. Proteins Suppl 1997;1:83-91.
    • (1997) Proteins Suppl , vol.1 , pp. 83-91
    • Marchler-Bauer, A.1    Levitt, M.2    Bryant, S.H.3
  • 4
    • 0031302793 scopus 로고    scopus 로고
    • Distant homology recognition using structural classification of proteins
    • Murzin A, Bateman A. Distant homology recognition using structural classification of proteins. Proteins Suppl 1997;1:105-112.
    • (1997) Proteins Suppl , vol.1 , pp. 105-112
    • Murzin, A.1    Bateman, A.2
  • 5
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W, Lipman D. Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 1988;85:2444-2448.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.1    Lipman, D.2
  • 8
    • 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, Higgins D, Gibson T. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.1    Higgins, D.2    Gibson, T.3
  • 9
    • 0032893084 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999
    • Bairoch A, Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999. Nucleic Acids Res 1999;27:49-54.
    • (1999) Nucleic Acids Res , vol.27 , pp. 49-54
    • Bairoch, A.1    Apweiler, R.2
  • 10
    • 0345286739 scopus 로고    scopus 로고
    • http://www.ncbi.nlm.nih.gov/PubMed/
  • 11
    • 0030774720 scopus 로고    scopus 로고
    • Prediction of protein secondary structure using the 3D-1D compatibility algorithm
    • Ito M, Matsuo Y, Nishikawa K. Prediction of protein secondary structure using the 3D-1D compatibility algorithm. Comput Appl Biosci 1997;13:415-424.
    • (1997) Comput Appl Biosci , vol.13 , pp. 415-424
    • Ito, M.1    Matsuo, Y.2    Nishikawa, K.3
  • 12
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 1994;19:55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 13
    • 0026326273 scopus 로고
    • Predicting protein secondary structure based on amino acid sequence
    • Nishikawa K, Noguchi T. Predicting protein secondary structure based on amino acid sequence. Methods Enzymol 1991;202:31-44.
    • (1991) Methods Enzymol , vol.202 , pp. 31-44
    • Nishikawa, K.1    Noguchi, T.2
  • 14
    • 0031022743 scopus 로고    scopus 로고
    • Improvement of protein secondary structure prediction using binary word encoding
    • Kawabata T, Doi J. Improvement of protein secondary structure prediction using binary word encoding. Proteins 1997;27:36-46.
    • (1997) Proteins , vol.27 , pp. 36-46
    • Kawabata, T.1    Doi, J.2
  • 16
    • 0032214622 scopus 로고    scopus 로고
    • Protein Data Bank (PDB): Database of three-dimensional structural information of biological macromolecules
    • Sussman JL, Lin D, Jianag J, Manning NO, Prilusky J, Ritter O, Abola EE. Protein Data Bank (PDB): database of three-dimensional structural information of biological macromolecules. Acta Cryst D 1998;54:1078-1084.
    • (1998) Acta Cryst D , vol.54 , pp. 1078-1084
    • Sussman, J.L.1    Lin, D.2    Jianag, J.3    Manning, N.O.4    Prilusky, J.5    Ritter, O.6    Abola, E.E.7
  • 17
    • 0028579433 scopus 로고
    • Protein structural similarities predicted by a sequence-structure compatibility method
    • Matsuo Y, Nishikawa K. Protein structural similarities predicted by a sequence-structure compatibility method. Protein Sci 1994;3: 2055-2063.
    • (1994) Protein Sci , vol.3 , pp. 2055-2063
    • Matsuo, Y.1    Nishikawa, K.2
  • 18
    • 0032903975 scopus 로고    scopus 로고
    • Feasibility in the inverse protein folding protocol
    • Ota M, Nishikawa K. Feasibility in the inverse protein folding protocol. Protein Sci 1999;8:1001-1009.
    • (1999) Protein Sci , vol.8 , pp. 1001-1009
    • Ota, M.1    Nishikawa, K.2
  • 19
    • 0028874809 scopus 로고
    • Assessment of a protein fold recognition method that takes into account four physicochemical properties: Side-chain packing, solvation, hydrogen-bonding, and local conformation
    • Matsuo Y, Nishikawa K. Assessment of a protein fold recognition method that takes into account four physicochemical properties: side-chain packing, solvation, hydrogen-bonding, and local conformation. Proteins 1995;23:370-375.
    • (1995) Proteins , vol.23 , pp. 370-375
    • Matsuo, Y.1    Nishikawa, K.2
  • 20
    • 0029003770 scopus 로고
    • Desk-top analysis of the structural stability of various point mutations introduced into ribonuclease H
    • Ota M, Kanaya S, Nishikawa K. Desk-top analysis of the structural stability of various point mutations introduced into ribonuclease H. J Mol Biol 1995;248:733-738.
    • (1995) J Mol Biol , vol.248 , pp. 733-738
    • Ota, M.1    Kanaya, S.2    Nishikawa, K.3
  • 21
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • Dayhoff MO, editor. Washington, DC: National Biomedical Research Foundation
    • Dayhoff MO, Schwartz RM, Orcutt BC. A model of evolutionary change in proteins. In: Dayhoff MO, editor. Atlas of protein sequence and structure. 5 suppl. 3, Washington, DC: National Biomedical Research Foundation, 1978. p 345-352.
    • (1978) Atlas of Protein Sequence and Structure , vol.5 , Issue.SUPPL. 3 , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 22
    • 0028961335 scopus 로고
    • Scop: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. Scop: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 23
    • 0032605908 scopus 로고    scopus 로고
    • Structure classification-based assessment of CASP3 predictions for the fold recognition targets
    • Murzin AG. Structure classification-based assessment of CASP3 predictions for the fold recognition targets. Proteins Suppl 1999;3: 88-103.
    • (1999) Proteins Suppl , vol.3 , pp. 88-103
    • Murzin, A.G.1
  • 24
    • 0030995325 scopus 로고    scopus 로고
    • A role for Salmonella typhimurium cbiK in cobalamin (vitamin B12) and siroheme biosynthesis
    • Raux E, Thermes C, Heathcote P, Rambach A, Warren M. A role for Salmonella typhimurium cbiK in cobalamin (vitamin B12) and siroheme biosynthesis. J Biotechnol 1997;179:3202-3212.
    • (1997) J Biotechnol , vol.179 , pp. 3202-3212
    • Raux, E.1    Thermes, C.2    Heathcote, P.3    Rambach, A.4    Warren, M.5
  • 25
    • 0031940246 scopus 로고    scopus 로고
    • An atlas of protein topology cartoons available on the worldwide web
    • Westhead D, Hatton D, Thornton J. An atlas of protein topology cartoons available on the worldwide web. Trends Biochem Sci 1998;23:35-36.
    • (1998) Trends Biochem Sci , vol.23 , pp. 35-36
    • Westhead, D.1    Hatton, D.2    Thornton, J.3
  • 26
    • 0024961628 scopus 로고
    • Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution
    • Mondragon A, Subbiah S, Almo SC, Drottar M, Harrisori SC. Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution. J Mol Biol 1989;205:189-200.
    • (1989) J Mol Biol , vol.205 , pp. 189-200
    • Mondragon, A.1    Subbiah, S.2    Almo, S.C.3    Drottar, M.4    Harrisori, S.C.5
  • 27
    • 0029083544 scopus 로고
    • Detection of 3D-1D compatibility characterized by the evaluation of side-chain packing and electrostatic interactions
    • Matsuo Y, Nakamura H, Nishikawa K. Detection of 3D-1D compatibility characterized by the evaluation of side-chain packing and electrostatic interactions. J Biochem (Tokyo) 1995;118:137-148.
    • (1995) J Biochem (Tokyo) , vol.118 , pp. 137-148
    • Matsuo, Y.1    Nakamura, H.2    Nishikawa, K.3
  • 28
    • 0030611275 scopus 로고    scopus 로고
    • The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea
    • Igarashi N, Moriyama H, Fujiwara T, Fukumori Y, Tanaka N. The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. Nature Struct Biol 1997;4:276-284.
    • (1997) Nature Struct Biol , vol.4 , pp. 276-284
    • Igarashi, N.1    Moriyama, H.2    Fujiwara, T.3    Fukumori, Y.4    Tanaka, N.5
  • 29
    • 0031734953 scopus 로고    scopus 로고
    • Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea
    • Iverson T, Arciero D, Hsu B, Logan M, Hooper A, Rees D. Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea. Nature Struct Biol 1998;5:1005-1012.
    • (1998) Nature Struct Biol , vol.5 , pp. 1005-1012
    • Iverson, T.1    Arciero, D.2    Hsu, B.3    Logan, M.4    Hooper, A.5    Rees, D.6
  • 30
    • 0031559765 scopus 로고    scopus 로고
    • Isolation, primary sequence determination, and disulfide bond structure of cyanovirin-N, an anti-HIV (human immunodeficiency virus) protein from the cyano-bacterium nostoc ellipsosporum
    • Gustafson K, Sowder RI, Henderson L, Cardellina JI, McMahon J, Rajamani U, Pannell L, Boyd M. Isolation, primary sequence determination, and disulfide bond structure of cyanovirin-N, an anti-HIV (human immunodeficiency virus) protein from the cyano-bacterium Nostoc ellipsosporum. Biochem Biophys Res Commun 1997;238:223-228.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 223-228
    • Gustafson, K.1    Sowder, R.I.2    Henderson, L.3    Cardellina, J.I.4    McMahon, J.5    Rajamani, U.6    Pannell, L.7    Boyd, M.8
  • 32
    • 0032612579 scopus 로고    scopus 로고
    • Ab initio protein structure prediction of CASP III targets using ROSETTA
    • Simons KT, Bonneau R, Ruczinski I, Baker D. Ab initio protein structure prediction of CASP III targets using ROSETTA. Proteins Suppl 1999;3:171-176.
    • (1999) Proteins Suppl , vol.3 , pp. 171-176
    • Simons, K.T.1    Bonneau, R.2    Ruczinski, I.3    Baker, D.4
  • 33
    • 0031307341 scopus 로고    scopus 로고
    • Fold assignments for amino acid sequences of the CASP2 experiment
    • Rice D, Fischer D, Weiss R, Eisenberg D. Fold assignments for amino acid sequences of the CASP2 experiment. Proteins Suppl 1997;1:113-122.
    • (1997) Proteins Suppl , vol.1 , pp. 113-122
    • Rice, D.1    Fischer, D.2    Weiss, R.3    Eisenberg, D.4
  • 34
    • 0032111312 scopus 로고    scopus 로고
    • The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance
    • Bussiere DE, Pratt SD, Katz L, Severin JM, Holzman T, Park CH. The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance. Mol Cell 1998;2:75-84.
    • (1998) Mol Cell , vol.2 , pp. 75-84
    • Bussiere, D.E.1    Pratt, S.D.2    Katz, L.3    Severin, J.M.4    Holzman, T.5    Park, C.H.6
  • 35
    • 0030779872 scopus 로고    scopus 로고
    • Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX
    • McCafferty D, Lessard I, Walsh C. Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX. Biochemistry 1997;36:10498-10505.
    • (1997) Biochemistry , vol.36 , pp. 10498-10505
    • McCafferty, D.1    Lessard, I.2    Walsh, C.3
  • 37
    • 0030724017 scopus 로고    scopus 로고
    • Assigning folds to the proteins encoded by the genome of Mycoplasma genitalium
    • Fischer D, Eisenberg D. Assigning folds to the proteins encoded by the genome of Mycoplasma genitalium. Proc Natl Acad Sci USA 1997;94:11929-11934.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11929-11934
    • Fischer, D.1    Eisenberg, D.2
  • 38
    • 0031296896 scopus 로고    scopus 로고
    • Measures of threading specificity and accuracy
    • Marchler-Bauer A, Bryant SH. Measures of threading specificity and accuracy. Proteins Suppl 1997;1:74-82.
    • (1997) Proteins Suppl , vol.1 , pp. 74-82
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24: 946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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