메뉴 건너뛰기




Volumn 134, Issue 2-3, 2001, Pages 167-185

Fold change in evolution of protein structures

Author keywords

Circular permutation; Conformational change; Deletion; Homology modeling; Insertion; Molecular evolution; Protein structure classification

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE RACEMASE; AMINO ACID; LACTATE DEHYDROGENASE; LIPOCALIN; LUCIFERASE; METHYLTRANSFERASE; ORNITHINE DECARBOXYLASE; PEROXIDASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SAPONIN; SERINE PROTEINASE INHIBITOR;

EID: 0035783063     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2001.4335     Document Type: Article
Times cited : (384)

References (134)
  • 2
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST - A tool for discovery in protein databases
    • Altschul, S. F., and Koonin, E. V. (1998) Iterated profile searches with PSI-BLAST - A tool for discovery in protein databases, Trends Biochem. Sci. 23, 444-447.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 4
    • 0033485460 scopus 로고    scopus 로고
    • DNA-binding proteins and evolution of transcription regulation in the archaea
    • Aravind, L., and Koonin, E. V. (1999a) DNA-binding proteins and evolution of transcription regulation in the archaea, Nucleic Acids Res. 27, 4658-4670.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4658-4670
    • Aravind, L.1    Koonin, E.V.2
  • 5
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches
    • Aravind, L., and Koonin, E. V. (1999b) Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches, J. Mol. Biol. 287, 1023-1040.
    • (1999) J. Mol. Biol. , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 6
    • 0032005329 scopus 로고    scopus 로고
    • Crystal structures and properties of de novo circularly permuted 1,3,4-β-glucanases
    • Ay, J., Hahn, M., Decanniere, K., Piotukh, K., Borriss, R., and Heinemann, U. (1998) Crystal structures and properties of de novo circularly permuted 1,3-1,4-β-glucanases, Proteins 30, 155-167.
    • (1998) Proteins , vol.30 , pp. 155-167
    • Ay, J.1    Hahn, M.2    Decanniere, K.3    Piotukh, K.4    Borriss, R.5    Heinemann, U.6
  • 7
    • 0033054043 scopus 로고    scopus 로고
    • High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor
    • Baber, J. L., Libutti, D., Levens, D., and Tjandra, N. (1999) High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor, J. Mol. Biol. 289, 949-962.
    • (1999) J. Mol. Biol. , vol.289 , pp. 949-962
    • Baber, J.L.1    Libutti, D.2    Levens, D.3    Tjandra, N.4
  • 10
    • 0027483434 scopus 로고
    • Empirical and structural models for insertions and deletions in the divergent evolution of proteins
    • Benner, S. A., Cohen, M. A., and Gonnet, G. H. (1993) Empirical and structural models for insertions and deletions in the divergent evolution of proteins, J. Mol. Biol. 229, 1065-1082.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1065-1082
    • Benner, S.A.1    Cohen, M.A.2    Gonnet, G.H.3
  • 11
    • 0033555717 scopus 로고    scopus 로고
    • Exploring the conformational properties of the sequence space between two proteins with different folds: An experimental study
    • Blanco, F. J., Angrand, I., and Serrano, L. (1999) Exploring the conformational properties of the sequence space between two proteins with different folds: An experimental study, J. Mol. Biol. 285, 741-753.
    • (1999) J. Mol. Biol. , vol.285 , pp. 741-753
    • Blanco, F.J.1    Angrand, I.2    Serrano, L.3
  • 12
    • 0034640125 scopus 로고    scopus 로고
    • The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families
    • Bordo, D., Deriu, D., Colnaghi, R., Carpen, A., Pagani, S., and Bolognesi, M. (2000) The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families, J. Mol. Biol. 298, 691-704.
    • (2000) J. Mol. Biol. , vol.298 , pp. 691-704
    • Bordo, D.1    Deriu, D.2    Colnaghi, R.3    Carpen, A.4    Pagani, S.5    Bolognesi, M.6
  • 14
    • 0032568596 scopus 로고    scopus 로고
    • Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships
    • Brenner, S. E., Chothia, C., and Hubbard, T. J. (1998) Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships, Proc. Natl. Acad. Sci. USA 95, 6073-6078.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6073-6078
    • Brenner, S.E.1    Chothia, C.2    Hubbard, T.J.3
  • 15
    • 0022001083 scopus 로고
    • Polypeptide ligation occurs during post-translational modification of concanavalin A
    • Carrington, D. M., Auffret, A., and Hanke, D. E. (1985) Polypeptide ligation occurs during post-translational modification of concanavalin A, Nature 313, 64-67.
    • (1985) Nature , vol.313 , pp. 64-67
    • Carrington, D.M.1    Auffret, A.2    Hanke, D.E.3
  • 16
    • 0021118508 scopus 로고
    • Principles that determine the structure of proteins
    • Chothia, C. (1984) Principles that determine the structure of proteins, Annu. Rev. Biochem. 53, 537-572.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 537-572
    • Chothia, C.1
  • 17
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C., and Lesk, A. M. (1986) The relation between the divergence of sequence and structure in proteins, EMBO J. 5, 823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 18
    • 0343063933 scopus 로고
    • Structure of proteins: Packing of alpha-helices and pleated sheets
    • Chothia, C., Levitt, M., and Richardson, D. (1977) Structure of proteins: Packing of alpha-helices and pleated sheets, Proc. Natl. Acad. Sci. USA 74, 4130-4134.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4130-4134
    • Chothia, C.1    Levitt, M.2    Richardson, D.3
  • 21
    • 0030986375 scopus 로고    scopus 로고
    • Protein alchemy: Changing beta-sheet into alpha-helix
    • Dalal, S., Balasubramanian, S., and Regan, L. (1997a) Protein alchemy: Changing beta-sheet into alpha-helix, Nat. Struct. Biol. 4, 548-552.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 548-552
    • Dalal, S.1    Balasubramanian, S.2    Regan, L.3
  • 22
    • 0030631518 scopus 로고    scopus 로고
    • Transmuting alpha helices and beta sheets
    • Dalal, S., Balasubramanian, S., and Regan, L. (1997b) Transmuting alpha helices and beta sheets, Fold Des. 2, R71-R79.
    • (1997) Fold Des. , vol.2
    • Dalal, S.1    Balasubramanian, S.2    Regan, L.3
  • 23
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • Dayhoff, M. O. (Ed.). National Biomedical Research Foundation, Washington, DC
    • Dayhoff, M. O., Schwartz, R. M., and Orcutt, B. C. (1978) A model of evolutionary change in proteins, in Atlas of Protein Sequences and Structures Dayhoff, M. O. (Ed.), Vol. 5, Suppl. 3, pp. 345-352. National Biomedical Research Foundation, Washington, DC.
    • (1978) Atlas of Protein Sequences and Structures , vol.5 , Issue.SUPPL. 3 , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 24
    • 0026079373 scopus 로고
    • The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution
    • Diederichs, K., and Schulz, G. E. (1991) The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution, J. Mol. Biol. 217, 541-549.
    • (1991) J. Mol. Biol. , vol.217 , pp. 541-549
    • Diederichs, K.1    Schulz, G.E.2
  • 25
    • 0019858614 scopus 로고
    • Similar amino acid sequences: Chance or common ancestry?
    • Doolittle, R. F. (1981) Similar amino acid sequences: Chance or common ancestry? Science 214, 149-159.
    • (1981) Science , vol.214 , pp. 149-159
    • Doolittle, R.F.1
  • 26
    • 0027983037 scopus 로고
    • Convergent evolution: The need to be explicit
    • Doolittle, R. F. (1994) Convergent evolution: The need to be explicit, Trends Biochem. Sci. 19, 15-18.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 15-18
    • Doolittle, R.F.1
  • 27
    • 0031568330 scopus 로고    scopus 로고
    • A new function for a common fold: The crystal structure of quinolinic acid phosphoribosyltransferase
    • Eads, J. C., Ozturk, D., Wexler, T. B., Grubmeyer, C., and Sacchettini, J. C. (1997) A new function for a common fold: The crystal structure of quinolinic acid phosphoribosyltransferase, Structure 5, 47-58.
    • (1997) Structure , vol.5 , pp. 47-58
    • Eads, J.C.1    Ozturk, D.2    Wexler, T.B.3    Grubmeyer, C.4    Sacchettini, J.C.5
  • 28
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy, S. R. (1998) Profile hidden Markov models, Bioinformatics 14, 755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 29
    • 0034623993 scopus 로고    scopus 로고
    • The saposin-like domain of the plant aspartic proteinase precursor is a potent inducer of vesicle leakage
    • Egas, C., Lavoura, N., Resende, R., Brito, R. M., Pires, E., Pedroso De Lima, M. C., and Faro, C. (2000) The saposin-like domain of the plant aspartic proteinase precursor is a potent inducer of vesicle leakage, J. Biol. Chem. 275, 38190-38196.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38190-38196
    • Egas, C.1    Lavoura, N.2    Resende, R.3    Brito, R.M.4    Pires, E.5    Pedroso De Lima, M.C.6    Faro, C.7
  • 30
    • 0025120714 scopus 로고
    • Modeling the intact form of the alpha 1-proteinase inhibitor
    • Engh, R. A., Wright, H. T., and Huber, R. (1990) Modeling the intact form of the alpha 1-proteinase inhibitor, Protein Eng. 3, 469-477.
    • (1990) Protein Eng. , vol.3 , pp. 469-477
    • Engh, R.A.1    Wright, H.T.2    Huber, R.3
  • 31
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R. M. (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities, J. Mol. Graph. Model. 15, 133-138.
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 32
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • Essen, L. O., Perisic, O., Cheung, R., Katan, M., and Williams, R. L. (1996) Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta, Nature 380, 595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 34
    • 0028151598 scopus 로고
    • Vancomycin resistance: Structure of D-alanine:D-alanine ligase at 2.3 Å resolution
    • Fan, C., Moews, P. C., Walsh, C. T., and Knox, J. R. (1994) Vancomycin resistance: Structure of D-alanine:D-alanine ligase at 2.3 Å resolution, Science 266, 439-443.
    • (1994) Science , vol.266 , pp. 439-443
    • Fan, C.1    Moews, P.C.2    Walsh, C.T.3    Knox, J.R.4
  • 36
    • 0028118764 scopus 로고
    • Hin recombinase bound to DNA: The origin of specificity in major and minor groove interactions
    • Feng, J. A., Johnson, R. C., and Dickerson, R. E. (1994) Hin recombinase bound to DNA: The origin of specificity in major and minor groove interactions, Science 263, 348-355.
    • (1994) Science , vol.263 , pp. 348-355
    • Feng, J.A.1    Johnson, R.C.2    Dickerson, R.E.3
  • 37
    • 0031626899 scopus 로고    scopus 로고
    • Function driven protein evolution. A possible proto-protein for the RNA-binding proteins
    • Fetrow, J. S., and Godzik, A. (1998) Function driven protein evolution. A possible proto-protein for the RNA-binding proteins, Pac. Symp. Biocomput. 3, 485-496.
    • (1998) Pac. Symp. Biocomput. , vol.3 , pp. 485-496
    • Fetrow, J.S.1    Godzik, A.2
  • 38
    • 0029027663 scopus 로고
    • Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution
    • Fisher, A. J., Raushel, F. M., Baldwin, T. O., and Rayment, I. (1995) Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution, Biochemistry 34, 6581-6586.
    • (1995) Biochemistry , vol.34 , pp. 6581-6586
    • Fisher, A.J.1    Raushel, F.M.2    Baldwin, T.O.3    Rayment, I.4
  • 39
    • 0027485083 scopus 로고
    • Comparison of conformational characteristics in structurally similar protein pairs
    • Flores, T. P., Orengo, C. A., Moss, D. S., and Thornton, J. M. (1993) Comparison of conformational characteristics in structurally similar protein pairs, Protein Sci. 2, 1811-1826.
    • (1993) Protein Sci. , vol.2 , pp. 1811-1826
    • Flores, T.P.1    Orengo, C.A.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 0030666566 scopus 로고    scopus 로고
    • Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug
    • Fuentes-Prior, P., Noeske-Jungblut, C., Donner, P., Schleuning, W. D., Huber, R., and Bode, W. (1997) Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug, Proc. Natl. Acad. Sci. USA 94, 11845-11850.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11845-11850
    • Fuentes-Prior, P.1    Noeske-Jungblut, C.2    Donner, P.3    Schleuning, W.D.4    Huber, R.5    Bode, W.6
  • 41
    • 0031467818 scopus 로고    scopus 로고
    • A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity
    • Galperin, M. Y., and Koonin, E. V. (1997) A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity, Protein Sci. 6, 2639-2643.
    • (1997) Protein Sci. , vol.6 , pp. 2639-2643
    • Galperin, M.Y.1    Koonin, E.V.2
  • 42
    • 85059706238 scopus 로고
    • Circularly permuted proteins
    • Goldenberg, D. P. (1989) Circularly permuted proteins, Protein Eng. 2, 493-495.
    • (1989) Protein Eng. , vol.2 , pp. 493-495
    • Goldenberg, D.P.1
  • 43
    • 0030612472 scopus 로고    scopus 로고
    • Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment
    • Gong, W., O'Gara, M., Blumenthal, R. M., and Cheng, X. (1997) Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment, Nucleic Acids Res. 25, 2702-2715.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2702-2715
    • Gong, W.1    O'Gara, M.2    Blumenthal, R.M.3    Cheng, X.4
  • 44
    • 0029859408 scopus 로고    scopus 로고
    • Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase
    • Graf, R., and Schachman, H. K. (1996) Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase, Proc. Natl. Acad. Sci. USA 93, 11591-11596.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11591-11596
    • Graf, R.1    Schachman, H.K.2
  • 45
    • 0030763376 scopus 로고    scopus 로고
    • Estimation of evolutionary distances from protein spatial structures
    • Grishin, N. V. (1997) Estimation of evolutionary distances from protein spatial structures, J. Mol. Evol. 45, 359-369.
    • (1997) J. Mol. Evol. , vol.45 , pp. 359-369
    • Grishin, N.V.1
  • 46
    • 0035253621 scopus 로고    scopus 로고
    • KH domain: One motif, two folds
    • Grishin, N. V. (2001) KH domain: One motif, two folds, Nucleic Acids Res. 29, 638-643.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 638-643
    • Grishin, N.V.1
  • 47
    • 0033576286 scopus 로고    scopus 로고
    • X-ray structure of ornithine decarboxylase from Trypanosoma brucei: The native structure and the structure in complex with alpha-difluoromethylornithine
    • Grishin, N. V., Osterman, A. L., Brooks, H. B., Phillips, M. A., and Goldsmith, E. J. (1999) X-ray structure of ornithine decarboxylase from Trypanosoma brucei: The native structure and the structure in complex with alpha-difluoromethylornithine, Biochemistry 38, 15174-15184.
    • (1999) Biochemistry , vol.38 , pp. 15174-15184
    • Grishin, N.V.1    Osterman, A.L.2    Brooks, H.B.3    Phillips, M.A.4    Goldsmith, E.J.5
  • 48
    • 0029046782 scopus 로고
    • Modeling of the spatial structure of eukaryotic ornithine decarboxylases
    • Grishin, N. V., Phillips, M. A., and Goldsmith, E. J. (1995) Modeling of the spatial structure of eukaryotic ornithine decarboxylases, Protein Sci. 4, 1291-1304.
    • (1995) Protein Sci. , vol.4 , pp. 1291-1304
    • Grishin, N.V.1    Phillips, M.A.2    Goldsmith, E.J.3
  • 49
    • 0033200307 scopus 로고    scopus 로고
    • A systematic comparison of protein structure classifications: SCOP, CATH and FSSP
    • Hadley, C., and Jones, D. T. (1999) A systematic comparison of protein structure classifications: SCOP, CATH and FSSP, Structure Fold Des. 7, 1099-1112.
    • (1999) Structure Fold Des. , vol.7 , pp. 1099-1112
    • Hadley, C.1    Jones, D.T.2
  • 50
    • 0028841677 scopus 로고
    • A potential catalytic site revealed by the 1.7-Å crystal structure of the amino-terminal signalling domain of Sonic hedgehog
    • Hall, T. M., Porter, J. A., Beachy, P. A., and Leahy, D. J. (1995) A potential catalytic site revealed by the 1.7-Å crystal structure of the amino-terminal signalling domain of Sonic hedgehog, Nature 378, 212-216.
    • (1995) Nature , vol.378 , pp. 212-216
    • Hall, T.M.1    Porter, J.A.2    Beachy, P.A.3    Leahy, D.J.4
  • 51
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff, S., and Henikoff, J. G. (1992) Amino acid substitution matrices from protein blocks, Proc. Natl. Acad. Sci. USA 89, 10915-10919.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 52
    • 0032104511 scopus 로고    scopus 로고
    • Unification of protein families
    • Holm, L. (1998) Unification of protein families, Curr. Opin. Struct. Biol. 8, 372-379.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 372-379
    • Holm, L.1
  • 53
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm, L., and Sander, C. (1996) Mapping the protein universe, Science 273, 595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 54
    • 0030765455 scopus 로고    scopus 로고
    • Dali/FSSP classification of three-dimensional protein folds
    • Holm, L., and Sander, C. (1997a) Dali/FSSP classification of three-dimensional protein folds, Nucleic Acids Res. 25, 231-234.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 231-234
    • Holm, L.1    Sander, C.2
  • 55
    • 0030623880 scopus 로고    scopus 로고
    • Decision support system for the evolutionary classification of protein structures
    • Holm, L., and Sander, C. (1997b) Decision support system for the evolutionary classification of protein structures, Ismb 5, 140-146.
    • (1997) Ismb , vol.5 , pp. 140-146
    • Holm, L.1    Sander, C.2
  • 56
    • 0030935327 scopus 로고    scopus 로고
    • New structure - Novel fold?
    • Holm, L., and Sander, C. (1997c) New structure - Novel fold? Structure 5, 165-171.
    • (1997) Structure , vol.5 , pp. 165-171
    • Holm, L.1    Sander, C.2
  • 57
    • 0000338489 scopus 로고
    • Comparison of solvent-inaccessible cores of homologous proteins: Definitions useful for protein modelling
    • Hubbard, T. J., and Blundell, T. L. (1987) Comparison of solvent-inaccessible cores of homologous proteins: Definitions useful for protein modelling, Protein Eng. 1, 159-171.
    • (1987) Protein Eng. , vol.1 , pp. 159-171
    • Hubbard, T.J.1    Blundell, T.L.2
  • 58
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J. A., Read, R. J., and Carrell, R. W. (2000) Structure of a serpin-protease complex shows inhibition by deformation, Nature 407, 923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 59
    • 0033013317 scopus 로고    scopus 로고
    • Circular permutations in the molecular evolution of DNA methyltransferases
    • Jeltsch, A. (1999) Circular permutations in the molecular evolution of DNA methyltransferases, J. Mol. Evol. 49, 161-164.
    • (1999) J. Mol. Evol. , vol.49 , pp. 161-164
    • Jeltsch, A.1
  • 60
    • 0029881326 scopus 로고    scopus 로고
    • Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of paracelsin-43, an alpha-helical protein with over 50% sequence identity to an all-beta protein
    • Jones, D. T., Moody, C. M., Uppenbrink, J., Viles, J. H., Doyle, P. M., Harris, C. J., Pearl, L. H., Sadler, P. J., and Thornton, J. M. (1996) Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of paracelsin-43, an alpha-helical protein with over 50% sequence identity to an all-beta protein, Proteins 24, 502-513.
    • (1996) Proteins , vol.24 , pp. 502-513
    • Jones, D.T.1    Moody, C.M.2    Uppenbrink, J.3    Viles, J.H.4    Doyle, P.M.5    Harris, C.J.6    Pearl, L.H.7    Sadler, P.J.8    Thornton, J.M.9
  • 61
    • 0033135202 scopus 로고    scopus 로고
    • Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: Stereochemical implications if PLP-dependent amino acid decarboxylases
    • Kern, A. D., Oliveira, M. A., Coffino, P., and Hackert, M. L. (1999) Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: Stereochemical implications if PLP-dependent amino acid decarboxylases, Structure Fold Des. 7, 567-581
    • (1999) Structure Fold Des. , vol.7 , pp. 567-581
    • Kern, A.D.1    Oliveira, M.A.2    Coffino, P.3    Hackert, M.L.4
  • 62
    • 0033565640 scopus 로고    scopus 로고
    • Crystal structure of plant aspartic proteinase prophytepsin: Inactivation and vacuolar targeting
    • Kervinen, J., Tobin, G. J., Costa, J., Waugh, D. S., Wlodawer, A., and Zdanov, A. (1999) Crystal structure of plant aspartic proteinase prophytepsin: Inactivation and vacuolar targeting, EMBO J. 18, 3947-3955.
    • (1999) EMBO J. , vol.18 , pp. 3947-3955
    • Kervinen, J.1    Tobin, G.J.2    Costa, J.3    Waugh, D.S.4    Wlodawer, A.5    Zdanov, A.6
  • 63
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • Kleywegt, G. J., Bergfors, T., Senn, H., Le Motte, P., Gsell, B., Shudo, K., and Jones, T. A. (1994) Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid, Structure 2, 1241-1258.
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Bergfors, T.2    Senn, H.3    Le Motte, P.4    Gsell, B.5    Shudo, K.6    Jones, T.A.7
  • 64
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • Koebnik, R., Locher, K. P., and Van Gelder, P. (2000) Structure and function of bacterial outer membrane proteins: Barrels in a nutshell, Mol. Microbiol. 37, 239-253.
    • (2000) Mol. Microbiol. , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 65
    • 0027267908 scopus 로고
    • A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication
    • Koonin, E. V. (1993) A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication, Nucleic Acids Res. 21, 2541-2547.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2541-2547
    • Koonin, E.V.1
  • 66
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 67
    • 0024961746 scopus 로고
    • The structure of yeast enolase at 2.25-Å resolution. An 8-fold beta + alpha-barrel with a novel beta beta alpha alpha (beta alpha) 6 topology
    • Lebioda, L., Stec, B., and Brewer, J. M. (1989) The structure of yeast enolase at 2.25-Å resolution. An 8-fold beta + alpha-barrel with a novel beta beta alpha alpha (beta alpha) 6 topology, J. Biol. Chem. 264, 3685-3693.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3685-3693
    • Lebioda, L.1    Stec, B.2    Brewer, J.M.3
  • 68
    • 0032006084 scopus 로고    scopus 로고
    • The Flavobacterium okeanokoites adenine-N6-specific DNA-methyltransferase M.FokI is a tandem enzyme of two independent domains with very different kinetic properties
    • Leismann, O., Roth, M., Friedrich, T., Wende, W., and Jeltsch, A. (1998) The Flavobacterium okeanokoites adenine-N6-specific DNA-methyltransferase M.FokI is a tandem enzyme of two independent domains with very different kinetic properties, Eur. J. Biochem. 251, 899-906.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 899-906
    • Leismann, O.1    Roth, M.2    Friedrich, T.3    Wende, W.4    Jeltsch, A.5
  • 69
    • 0017309766 scopus 로고
    • Structural patterns in globular proteins
    • Levitt, M., and Chothia, C. (1976) Structural patterns in globular proteins, Nature 261, 552-558.
    • (1976) Nature , vol.261 , pp. 552-558
    • Levitt, M.1    Chothia, C.2
  • 71
    • 0030979555 scopus 로고    scopus 로고
    • Circular permutations of natural protein sequences: Structural evidence
    • Lindqvist, Y., and Schneider, G. (1997) Circular permutations of natural protein sequences: Structural evidence, Curr. Opin. Struct. Biol. 7, 422-427.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 422-427
    • Lindqvist, Y.1    Schneider, G.2
  • 73
    • 0021747157 scopus 로고
    • Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • Loebermann, H., Tokuoka, R., Deisenhofer, J., and Huber, R. (1984) Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function, J. Mol. Biol. 177, 531-557.
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-557
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 74
    • 0024490818 scopus 로고
    • Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo
    • Luger, K., Hommel, U., Herold, M., Hofsteenge, J., and Kirschner, K. (1989) Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo, Science 243, 206-210.
    • (1989) Science , vol.243 , pp. 206-210
    • Luger, K.1    Hommel, U.2    Herold, M.3    Hofsteenge, J.4    Kirschner, K.5
  • 75
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 Å resolution
    • Machius, M., Wiegand, G., and Huber, R. (1995) Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 Å resolution, J. Mol. Biol. 246, 545-559.
    • (1995) J. Mol. Biol. , vol.246 , pp. 545-559
    • Machius, M.1    Wiegand, G.2    Huber, R.3
  • 76
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes
    • Malone, T., Blumenthal, R. M., and Cheng, X. (1995) Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes, J. Mol. Biol. 253, 618-632.
    • (1995) J. Mol. Biol. , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3
  • 77
    • 0029864575 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: A new structural family with the P-loop nucleoside triphosphate hydrolase fold
    • Matte, A., Goldie, H., Sweet, R. M., and Delbaere, L. T. (1996) Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: A new structural family with the P-loop nucleoside triphosphate hydrolase fold, J. Mol. Biol. 256, 126-143.
    • (1996) J. Mol. Biol. , vol.256 , pp. 126-143
    • Matte, A.1    Goldie, H.2    Sweet, R.M.3    Delbaere, L.T.4
  • 78
    • 0033214429 scopus 로고    scopus 로고
    • Toward more meaningful hierarchical classification of protein three-dimensional structures
    • May, A. C. (1999) Toward more meaningful hierarchical classification of protein three-dimensional structures, Proteins 37, 20-29.
    • (1999) Proteins , vol.37 , pp. 20-29
    • May, A.C.1
  • 79
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • Minor, D. L., Jr., and Kim, P. S. (1996) Context-dependent secondary structure formation of a designed protein sequence, Nature 380, 730-734
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor D.L., Jr.1    Kim, P.S.2
  • 80
    • 0028579712 scopus 로고
    • Common structural features of the luxF protein and the subunits of bacterial luciferase: Evidence for a (beta alpha) 8 fold in luciferase
    • Moore, S. A., and James, M. N. (1994) Common structural features of the luxF protein and the subunits of bacterial luciferase: Evidence for a (beta alpha) 8 fold in luciferase, Protein Sci. 3, 1914-1926.
    • (1994) Protein Sci. , vol.3 , pp. 1914-1926
    • Moore, S.A.1    James, M.N.2
  • 81
    • 0027310218 scopus 로고
    • Crystal structure of a flavoprotein related to the subunits of bacterial luciferase
    • Moore, S. A., James, M. N., O'Kane, D. J., and Lee, J. (1993) Crystal structure of a flavoprotein related to the subunits of bacterial luciferase, EMBO J. 12, 1767-1774.
    • (1993) EMBO J. , vol.12 , pp. 1767-1774
    • Moore, S.A.1    James, M.N.2    O'Kane, D.J.3    Lee, J.4
  • 82
    • 0031552349 scopus 로고    scopus 로고
    • Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri
    • Morishita, Y., Hasegawa, K., Matsuura, Y., Katsube, Y., Kubota, M., and Sakai, S. (1997) Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri, J. Mol. Biol. 267, 661-672.
    • (1997) J. Mol. Biol. , vol.267 , pp. 661-672
    • Morishita, Y.1    Hasegawa, K.2    Matsuura, Y.3    Katsube, Y.4    Kubota, M.5    Sakai, S.6
  • 84
    • 0032104477 scopus 로고    scopus 로고
    • How far divergent evolution goes in proteins
    • Murzin, A. G. (1998) How far divergent evolution goes in proteins, Curr. Opin. Struct. Biol. 8, 380-387.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 380-387
    • Murzin, A.G.1
  • 85
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., Brenner, S. E., Hubbard, T., and Chothia, C. (1995) SCOP: A structural classification of proteins database for the investigation of sequences and structures, J. Mol. Biol. 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
  • 86
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski, E. A., and Falke, J. J. (1996) The C2 domain calcium-binding motif: Structural and functional diversity, Protein Sci. 5, 2375-2390.
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 87
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L., and Koonin, E. V. (1999) AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes, Genome Res. 9, 27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 89
    • 0032474460 scopus 로고    scopus 로고
    • Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus
    • Otzen, D. E., and Fersht, A. R. (1998) Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus, Biochemistry 37, 8139-8146.
    • (1998) Biochemistry , vol.37 , pp. 8139-8146
    • Otzen, D.E.1    Fersht, A.R.2
  • 90
    • 0029644732 scopus 로고
    • Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase complexed with substrate analogue and product
    • Owen, D. J., Noble, M. E., Garman, E. F., Papageorgiou, A. C., and Johnson, L. N. (1995) Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase complexed with substrate analogue and product, Structure 3, 467-482.
    • (1995) Structure , vol.3 , pp. 467-482
    • Owen, D.J.1    Noble, M.E.2    Garman, E.F.3    Papageorgiou, A.C.4    Johnson, L.N.5
  • 91
    • 0027467740 scopus 로고
    • Circularly permuted DNA, RNA and proteins - A review
    • Pan, T., and Uhlenbeck, O. C. (1993) Circularly permuted DNA, RNA and proteins - A review, Gene 125, 111-114.
    • (1993) Gene , vol.125 , pp. 111-114
    • Pan, T.1    Uhlenbeck, O.C.2
  • 93
    • 0026566796 scopus 로고
    • Analysis of insertions/deletions in protein structures
    • Pascarella, S., and Argos, P. (1992) Analysis of insertions/deletions in protein structures, J. Mol. Biol. 224, 461-471.
    • (1992) J. Mol. Biol. , vol.224 , pp. 461-471
    • Pascarella, S.1    Argos, P.2
  • 95
    • 0029000740 scopus 로고
    • Swaposins: Circular permutations within genes encoding saposin homologues
    • Ponting, C. P., and Russell, R. B. (1995) Swaposins: Circular permutations within genes encoding saposin homologues, Trends Biochem. Sci. 20, 179-180.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 179-180
    • Ponting, C.P.1    Russell, R.B.2
  • 96
    • 0019053499 scopus 로고
    • Similarities in protein topologies: Evolutionary divergence, functional convergence or principles of folding
    • Ptitsyn, O. B., and Finkelstein, A. V. (1981) Similarities in protein topologies: Evolutionary divergence, functional convergence or principles of folding, Q. Rev. Biophys. 13, 339-386.
    • (1981) Q. Rev. Biophys. , vol.13 , pp. 339-386
    • Ptitsyn, O.B.1    Finkelstein, A.V.2
  • 97
    • 0021095532 scopus 로고
    • Refined crystal structure of carboxypeptidase A at 1.54 Å resolution
    • Rees, D. C., Lewis, M., and Lipscomb, W. N. (1983) Refined crystal structure of carboxypeptidase A at 1.54 Å resolution, J. Mol. Biol. 168, 367-387.
    • (1983) J. Mol. Biol. , vol.168 , pp. 367-387
    • Rees, D.C.1    Lewis, M.2    Lipscomb, W.N.3
  • 98
    • 0017387723 scopus 로고
    • b-Sheet topology and the relatedness of proteins
    • Richardson, J. S. (1977) b-Sheet topology and the relatedness of proteins, Nature 268, 495-500.
    • (1977) Nature , vol.268 , pp. 495-500
    • Richardson, J.S.1
  • 99
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S. (1981) The anatomy and taxonomy of protein structure, Adv. Protein Chem. 34, 167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 100
    • 0032568859 scopus 로고    scopus 로고
    • Detection of protein three-dimensional side-chain patterns: New examples of convergent evolution
    • Russell, R. B. (1998) Detection of protein three-dimensional side-chain patterns: New examples of convergent evolution, J. Mol. Biol. 279, 1211-1227.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1211-1227
    • Russell, R.B.1
  • 101
    • 0032103855 scopus 로고    scopus 로고
    • Protein fold irregularities that hinder sequence analysis
    • Russell, R. B., and Ponting, C. P. (1998) Protein fold irregularities that hinder sequence analysis, Curr. Opin. Struct. Biol. 8, 364-371.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 364-371
    • Russell, R.B.1    Ponting, C.P.2
  • 102
    • 0031909873 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds - Assessment of prediction success and associated alignment accuracy using empirical substitution matrices
    • Russell, R. B., Saqi, M. A., Bates, P. A., Sayle, R. A., and Sternberg, M. J. (1998) Recognition of analogous and homologous protein folds - Assessment of prediction success and associated alignment accuracy using empirical substitution matrices, Protein Eng. 11, 1-9.
    • (1998) Protein Eng. , vol.11 , pp. 1-9
    • Russell, R.B.1    Saqi, M.A.2    Bates, P.A.3    Sayle, R.A.4    Sternberg, M.J.5
  • 103
    • 0031566432 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds: Analysis of sequence and structure conservation
    • Russell, R. B., Saqi, M. A., Sayle, R. A., Bates, P. A., and Sternberg, M. J. (1997) Recognition of analogous and homologous protein folds: Analysis of sequence and structure conservation, J. Mol. Biol. 269, 423-439.
    • (1997) J. Mol. Biol. , vol.269 , pp. 423-439
    • Russell, R.B.1    Saqi, M.A.2    Sayle, R.A.3    Bates, P.A.4    Sternberg, M.J.5
  • 104
    • 0031787022 scopus 로고    scopus 로고
    • 100,000 Protein structures for the biologist
    • Sali, A. (1998) 100,000 Protein structures for the biologist, Nat. Struct. Biol. 5, 1029-1032.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1029-1032
    • Sali, A.1
  • 105
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P. R., and Wittinghofer, A. (1990) The P-loop - A common motif in ATP- and GTP-binding proteins, Trends Biochem. Sci. 15, 430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 106
    • 0031561804 scopus 로고    scopus 로고
    • Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M, TaqI
    • Schluckebier, G., Kozak, M., Bleimling, N., Weinhold, E., and Saenger, W. (1997) Differential binding of S-adenosylmethi-onine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M. TaqI, J. Mol. Biol. 265, 56-67.
    • (1997) J. Mol. Biol. , vol.265 , pp. 56-67
    • Schluckebier, G.1    Kozak, M.2    Bleimling, N.3    Weinhold, E.4    Saenger, W.5
  • 107
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90 degrees
    • Schultz, S. C., Shields, G. C., and Steitz, T. A. (1991) Crystal structure of a CAP-DNA complex: The DNA is bent by 90 degrees, Science 253, 1001-1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 108
    • 0034730293 scopus 로고    scopus 로고
    • Genomics. Structural biology gets a $150 million boost
    • News
    • Service, R. F. (2000) Genomics. Structural biology gets a $150 million boost, Science 289, 2254-2255. [News]
    • (2000) Science , vol.289 , pp. 2254-2255
    • Service, R.F.1
  • 109
    • 0031032448 scopus 로고    scopus 로고
    • Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution
    • Shaw, J. P., Petsko, G. A., and Ringe, D. (1997) Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution, Biochemistry 36, 1329-1342.
    • (1997) Biochemistry , vol.36 , pp. 1329-1342
    • Shaw, J.P.1    Petsko, G.A.2    Ringe, D.3
  • 110
    • 0027273728 scopus 로고
    • The pre-mRNA binding K protein contains a novel evolutionarily conserved motif
    • Siomi, H., Matunis, M. J., Michael, W. M., and Dreyfuss, G. (1993) The pre-mRNA binding K protein contains a novel evolutionarily conserved motif, Nucleic Acids Res. 21, 1193-1198.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1193-1198
    • Siomi, H.1    Matunis, M.J.2    Michael, W.M.3    Dreyfuss, G.4
  • 111
    • 0029614803 scopus 로고
    • Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop
    • Song, H. K., Lee, K. N., Kwon, K. S., Yu, M. H., and Suh, S. W. (1995) Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop, FEBS Lett. 377, 150-154.
    • (1995) FEBS Lett. , vol.377 , pp. 150-154
    • Song, H.K.1    Lee, K.N.2    Kwon, K.S.3    Yu, M.H.4    Suh, S.W.5
  • 112
    • 0027385038 scopus 로고
    • Crystal structure of the catalytic domain of a thermophilic endocellulase
    • Spezio, M., Wilson, D. B., and Karplus, P. A. (1993) Crystal structure of the catalytic domain of a thermophilic endocellulase, Biochemistry 32, 9906-9916.
    • (1993) Biochemistry , vol.32 , pp. 9906-9916
    • Spezio, M.1    Wilson, D.B.2    Karplus, P.A.3
  • 113
    • 0025996658 scopus 로고
    • Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 Å resolution
    • Stehle, T., Ahmed, S. A., Claiborne, A., and Schulz, G. E. (1991) Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 Å resolution, J. Mol. Biol. 221, 1325-1344.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1325-1344
    • Stehle, T.1    Ahmed, S.A.2    Claiborne, A.3    Schulz, G.E.4
  • 114
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story, R. M., Weber, I. T., and Steitz, T. A. (1992) The structure of the E. coli recA protein monomer and polymer, Nature 355, 318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 115
    • 0028030520 scopus 로고
    • The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
    • Su, X. D., Taddei, N., Stefani, M., Ramponi, G., and Nordlund, P. (1994) The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase, Nature 370, 575-578.
    • (1994) Nature , vol.370 , pp. 575-578
    • Su, X.D.1    Taddei, N.2    Stefani, M.3    Ramponi, G.4    Nordlund, P.5
  • 119
    • 0020520185 scopus 로고
    • Amino and carboxy-terminal regions in globular proteins
    • Thornton, J. M., and Sibanda, B. L. (1983) Amino and carboxy-terminal regions in globular proteins, J. Mol. Biol. 167, 443-460.
    • (1983) J. Mol. Biol. , vol.167 , pp. 443-460
    • Thornton, J.M.1    Sibanda, B.L.2
  • 120
    • 0033370743 scopus 로고    scopus 로고
    • A simple algorithm for detecting circular permutations in proteins
    • Uliel, S., Fliess, A., Amir, A., and Unger, R. (1999) A simple algorithm for detecting circular permutations in proteins, Bioinformatics, 15, 930-936.
    • (1999) Bioinformatics , vol.15 , pp. 930-936
    • Uliel, S.1    Fliess, A.2    Amir, A.3    Unger, R.4
  • 121
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera, A. R., Blanco, F. J., and Serrano, L. (1995) The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics, J. Mol. Biol. 247, 670-681.
    • (1995) J. Mol. Biol. , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 122
    • 0028085434 scopus 로고
    • Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase
    • Waldrop, G. L., Rayment, I., and Holden, H. M. (1994) Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase, Biochemistry 33, 10249-10256.
    • (1994) Biochemistry , vol.33 , pp. 10249-10256
    • Waldrop, G.L.1    Rayment, I.2    Holden, H.M.3
  • 123
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J. (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold, EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 125
    • 0026512524 scopus 로고
    • Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 Å resolution
    • Wigley, D. B., Gamblin, S. J., Turkenburg, J. P., Dodson, E. J., Piontek, K., Muirhead, H., and Holbrook, J. J. (1992) Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 Å resolution, J. Mol. Biol. 223, 317-335.
    • (1992) J. Mol. Biol. , vol.223 , pp. 317-335
    • Wigley, D.B.1    Gamblin, S.J.2    Turkenburg, J.P.3    Dodson, E.J.4    Piontek, K.5    Muirhead, H.6    Holbrook, J.J.7
  • 126
    • 0027023842 scopus 로고
    • Amino acid sequence arrangements of DNA-methyltransferases
    • Wilson, G. G. (1992) Amino acid sequence arrangements of DNA-methyltransferases, Methods Enzymol. 216, 259-279.
    • (1992) Methods Enzymol. , vol.216 , pp. 259-279
    • Wilson, G.G.1
  • 127
    • 0026666377 scopus 로고
    • Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin-and DNA-binding domains
    • Wilson, K. P., Shewchuk, L. M., Brennan, R. G., Otsuka, A. J., and Matthews, B. W. (1992) Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin-and DNA-binding domains, Proc. Natl. Acad. Sci. USA 89, 9257-9261.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9257-9261
    • Wilson, K.P.1    Shewchuk, L.M.2    Brennan, R.G.3    Otsuka, A.J.4    Matthews, B.W.5
  • 129
    • 0033008596 scopus 로고    scopus 로고
    • Distribution of protein folds in the three superkingdoms of life
    • Wolf, Y. I., Brenner, S. E., Bash, P. A., and Koonin, E. V. (1999) Distribution of protein folds in the three superkingdoms of life, Genome Res. 9, 17-26.
    • (1999) Genome Res. , vol.9 , pp. 17-26
    • Wolf, Y.I.1    Brenner, S.E.2    Bash, P.A.3    Koonin, E.V.4
  • 130
    • 0031024655 scopus 로고    scopus 로고
    • The RNA binding domain of ribosomal protein L11 is structurally similar to homeodomains
    • Xing, Y., Guha Thakurta, D., and Draper, D. E. (1997) The RNA binding domain of ribosomal protein L11 is structurally similar to homeodomains, Nat. Struct. Biol. 4, 24-27.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 24-27
    • Xing, Y.1    Guha Thakurta, D.2    Draper, D.E.3
  • 131
    • 0027530140 scopus 로고
    • Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution
    • Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J., and Katsube, Y. (1993) Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution, J. Mol. Biol. 229, 1083-1100.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1083-1100
    • Yamaguchi, H.1    Kato, H.2    Hata, Y.3    Nishioka, T.4    Kimura, A.5    Oda, J.6    Katsube, Y.7
  • 132
    • 0032006183 scopus 로고    scopus 로고
    • A hybrid sequence approach to the Paracelsus challenge
    • Yuan, S. M., and Clarke, N. D. (1998) A hybrid sequence approach to the Paracelsus challenge, Proteins 30, 136-143.
    • (1998) Proteins , vol.30 , pp. 136-143
    • Yuan, S.M.1    Clarke, N.D.2
  • 133
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual specificity protein phosphatase VHR
    • Yuvaniyama, J., Denu, J. M., Dixon, J. E., and Saper, M. A. (1996) Crystal structure of the dual specificity protein phosphatase VHR, Science 272, 1328-1331.
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 134
    • 0027302351 scopus 로고
    • Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein
    • Zanotti, G., Berni, R., and Monaco, H. L. (1993) Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein, J. Biol. Chem. 268, 10728-10738.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10728-10738
    • Zanotti, G.1    Berni, R.2    Monaco, H.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.