메뉴 건너뛰기




Volumn 18, Issue 1, 2000, Pages 34-39

From genes to protein structure and function: Novel applications of computational approaches in the genomic era

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0033964710     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-7799(99)01398-0     Document Type: Review
Times cited : (143)

References (72)
  • 2
    • 0029895576 scopus 로고    scopus 로고
    • X-SITE: Use of empirically derived atomic packing preferences to identify favourable interaction regions in the binding sites of proteins
    • Laskowski, R.A. et al. (1996) X-SITE: Use of empirically derived atomic packing preferences to identify favourable interaction regions in the binding sites of proteins. J. Mol. Biol. 259, 175-201
    • (1996) J. Mol. Biol. , vol.259 , pp. 175-201
    • Laskowski, R.A.1
  • 3
    • 0029973830 scopus 로고    scopus 로고
    • Derivation of 3D coordinate templates for searching structural databases: Application to Ser-His-Asp catalytic triads in the serine proteinases and lipases
    • Wallace, A.C. et al. (1996) Derivation of 3D coordinate templates for searching structural databases: Application to Ser-His-Asp catalytic triads in the serine proteinases and lipases. Protein Sci. 5, 1001-1013
    • (1996) Protein Sci. , vol.5 , pp. 1001-1013
    • Wallace, A.C.1
  • 4
    • 0026410103 scopus 로고
    • Automated assembly of protein blocks for database searching
    • Henikoff, S. and Henikoff, J.G. (1991) Automated assembly of protein blocks for database searching. Nucleic Acids Res. 19, 6565-6572
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6565-6572
    • Henikoff, S.1    Henikoff, J.G.2
  • 5
    • 0027133165 scopus 로고
    • Functions of gene products of Escherichia coli
    • Riley, M. (1993) Functions of gene products of Escherichia coli. Microbiol. Rev. 57, 862-952
    • (1993) Microbiol. Rev. , vol.57 , pp. 862-952
    • Riley, M.1
  • 6
    • 0027900857 scopus 로고
    • Representations of metabolic knowledge
    • Karp, P.D. and Riley, M. (1993) Representations of metabolic knowledge. Ismb 1, 207-215
    • (1993) Ismb , vol.1 , pp. 207-215
    • Karp, P.D.1    Riley, M.2
  • 7
    • 0025183708 scopus 로고
    • Basic local alignment search tool
    • Altschul, S.F. et al. (1990) Basic local alignment search tool. J. Mol. Biol. 215, 403-410
    • (1990) J. Mol. Biol. , vol.215 , pp. 403-410
    • Altschul, S.F.1
  • 8
    • 0029933671 scopus 로고    scopus 로고
    • Effective protein sequence comparison
    • Pearson, W.R. (1996) Effective protein sequence comparison. Methods Enzymol. 266, 227-258
    • (1996) Methods Enzymol. , vol.266 , pp. 227-258
    • Pearson, W.R.1
  • 10
    • 0029916915 scopus 로고
    • The PROSITE database, its status in 1995
    • Bairoch, A. et al. (1995) The PROSITE database, its status in 1995. Nucleic Acids Res. 24, 189-196
    • (1995) Nucleic Acids Res. , vol.24 , pp. 189-196
    • Bairoch, A.1
  • 11
    • 0028118434 scopus 로고
    • Protein family classification based on searching a database of blocks
    • Henikoff, S. and Henikoff, J.G. (1994) Protein family classification based on searching a database of blocks. Genomics 19, 97-107
    • (1994) Genomics , vol.19 , pp. 97-107
    • Henikoff, S.1    Henikoff, J.G.2
  • 12
    • 0028108989 scopus 로고
    • PRINTS - A database of protein motif fingerprints
    • Attwood, T.K. et al. (1994) PRINTS - A database of protein motif fingerprints. Nucleic Acids Res. 22, 3590-3596
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3590-3596
    • Attwood, T.K.1
  • 13
    • 0030752032 scopus 로고    scopus 로고
    • Novel developments with the PRINTS protein fingerprint database
    • Attwood, T.K. et al. (1997) Novel developments with the PRINTS protein fingerprint database. Nucleic Acids Res. 25, 212-216
    • (1997) Nucleic Acids Res. , vol.25 , pp. 212-216
    • Attwood, T.K.1
  • 14
    • 0032568526 scopus 로고    scopus 로고
    • Highly specific protein sequence motifs for genome analysis
    • Nevill-Manning, C.G. et al. (1998) Highly specific protein sequence motifs for genome analysis. Proc. Natl. Acad. Sci. U. S. A. 95, 5865-5871
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5865-5871
    • Nevill-Manning, C.G.1
  • 15
    • 0032483312 scopus 로고    scopus 로고
    • Method for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases
    • Fetrow, J.S. and Skolnick, J. (1998) Method for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases. J. Mol. Biol. 281, 949-968
    • (1998) J. Mol. Biol. , vol.281 , pp. 949-968
    • Fetrow, J.S.1    Skolnick, J.2
  • 16
    • 0031678064 scopus 로고    scopus 로고
    • A homology identification method that combines protein sequence and structure information
    • Yu, L. et al. (1998) A homology identification method that combines protein sequence and structure information. Protein Sci. 7, 2499-2510
    • (1998) Protein Sci. , vol.7 , pp. 2499-2510
    • Yu, L.1
  • 17
    • 0030271920 scopus 로고    scopus 로고
    • Go hunting in sequence databases but watch out for traps
    • Bork, P. and Bairoch, A. (1996) Go hunting in sequence databases but watch out for traps. Trends Genet. 12, 425-427
    • (1996) Trends Genet. , vol.12 , pp. 425-427
    • Bork, P.1    Bairoch, A.2
  • 18
    • 0031824449 scopus 로고    scopus 로고
    • Structural genomics: Bioinformatics in the driver's seat
    • Gaasterland, T. (1998) Structural genomics: Bioinformatics in the driver's seat. Nat. Biotechnol. 16, 625-627
    • (1998) Nat. Biotechnol. , vol.16 , pp. 625-627
    • Gaasterland, T.1
  • 19
    • 0030671393 scopus 로고    scopus 로고
    • Genomics: Structural and functional studies of genomes
    • McKusick, V.A. (1997) Genomics: Structural and functional studies of genomes. Genomics 45, 244-249
    • (1997) Genomics , vol.45 , pp. 244-249
    • McKusick, V.A.1
  • 20
    • 0032921818 scopus 로고    scopus 로고
    • Structural genomics: Keystone for a human proteome project
    • Montelione, G.T. and Anderson, S. (1999) Structural genomics: Keystone for a human proteome project. Nat. Struct. Biol. 6, 11-12
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 11-12
    • Montelione, G.T.1    Anderson, S.2
  • 21
    • 0028230909 scopus 로고
    • Three-dimensional, sequence order-independent structural comparison of a serine protease against the crystallographic database reveals active site similarities: Potential implications to evolution and to protein folding
    • Fischer, D. et al (1994) Three-dimensional, sequence order-independent structural comparison of a serine protease against the crystallographic database reveals active site similarities: Potential implications to evolution and to protein folding. Protein Sci. 3, 769-778
    • (1994) Protein Sci. , vol.3 , pp. 769-778
    • Fischer, D.1
  • 22
    • 0032506030 scopus 로고    scopus 로고
    • Large-scale protein structure modeling of the Saccharomyces cerevisiae genome
    • Sanchez, R. and Sali, A. (1998) Large-scale protein structure modeling of the Saccharomyces cerevisiae genome. Proc. Natl. Acad. Sci. U. S. A. 95, 13597-13602
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 13597-13602
    • Sanchez, R.1    Sali, A.2
  • 23
    • 0032411227 scopus 로고    scopus 로고
    • Functional analysis of E. coli proteins for members of the α/β; hydrolase family
    • Zhang, L. et al. (1998) Functional analysis of E. coli proteins for members of the α/β; hydrolase family. Fold. Design 3, 535-548
    • (1998) Fold. Design , vol.3 , pp. 535-548
    • Zhang, L.1
  • 24
    • 0033548460 scopus 로고    scopus 로고
    • Three-dimensional structure analysis of Prosite patterns
    • Kasuya, A. and Thornton, J.M. (1999) Three-dimensional structure analysis of Prosite patterns. J. Mol. Biol. 286, 1673-1691
    • (1999) J. Mol. Biol. , vol.286 , pp. 1673-1691
    • Kasuya, A.1    Thornton, J.M.2
  • 25
    • 0030917147 scopus 로고    scopus 로고
    • The rational design and construction of a cuboidal iron-sulfur protein
    • Coldren, C.D. et al. (1997) The rational design and construction of a cuboidal iron-sulfur protein. Proc. Natl. Acad. Sci. U. S. A. 94, 6635-6640
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6635-6640
    • Coldren, C.D.1
  • 26
    • 0030978103 scopus 로고    scopus 로고
    • Construction of a catalytically active iron superoxide dismutase by rational protein design
    • Pinto, A.L. et al. (1997) Construction of a catalytically active iron superoxide dismutase by rational protein design. Proc. Natl. Acad. Sci. U. S. A. 94, 5562-5567
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5562-5567
    • Pinto, A.L.1
  • 27
    • 0026335211 scopus 로고
    • Construction of new ligand binding sites in proteins of known structure: (I) computer-aided modeling of sites with pre-defined geometry
    • Hellinga, H.W. and Richards, P.M. (1991) Construction of new ligand binding sites in proteins of known structure: (I) computer-aided modeling of sites with pre-defined geometry. J. Mol. Biol. 222, 763-785
    • (1991) J. Mol. Biol. , vol.222 , pp. 763-785
    • Hellinga, H.W.1    Richards, P.M.2
  • 28
    • 0026321752 scopus 로고
    • Construction of new ligand binding sites in proteins of known structure: (II) grafting of a buried transition metal binding site into Escherichia coli thioredoxin
    • Hellinga, H.W. et al. (1991) Construction of new ligand binding sites in proteins of known structure: (II) grafting of a buried transition metal binding site into Escherichia coli thioredoxin. J. Mol. Biol. 222, 787-803
    • (1991) J. Mol. Biol. , vol.222 , pp. 787-803
    • Hellinga, H.W.1
  • 30
    • 0029017933 scopus 로고
    • Novel metal-binding proteins by design
    • Klemba, M. et al. (1995) Novel metal-binding proteins by design. Nat. Struct. Biol. 2, 368-373
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 368-373
    • Klemba, M.1
  • 31
    • 0031694147 scopus 로고    scopus 로고
    • The de novo design of a rubredoxin-like Fe site
    • Farinas, E. and Regan, L. (1998) The de novo design of a rubredoxin-like Fe site. Protein Sci. 7, 1939-1946
    • (1998) Protein Sci. , vol.7 , pp. 1939-1946
    • Farinas, E.1    Regan, L.2
  • 32
    • 0000103140 scopus 로고
    • Spectroscopic studies on the designed metal-binding sites of the 43C9 single chain antibody
    • Crowder, M.W. et al. (1995) Spectroscopic studies on the designed metal-binding sites of the 43C9 single chain antibody. J. Am. Chem. Soc. 117, 5627-5634
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5627-5634
    • Crowder, M.W.1
  • 33
    • 0029916620 scopus 로고    scopus 로고
    • Regulation of proteolytic activity by engineered tridentate metal binding loops
    • Halfon, S. and Craik, C.S. (1996) Regulation of proteolytic activity by engineered tridentate metal binding loops. J. Am. Chem. Soc. 118, 1227-1228
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1227-1228
    • Halfon, S.1    Craik, C.S.2
  • 34
    • 0030724039 scopus 로고    scopus 로고
    • TESS: A geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases: Application to enzyme active sites
    • Wallace, A.C. et al. (1997) TESS: A geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases: Application to enzyme active sites. Protein Sci. 6, 2308-2323
    • (1997) Protein Sci. , vol.6 , pp. 2308-2323
    • Wallace, A.C.1
  • 35
    • 0033613813 scopus 로고    scopus 로고
    • Recognition of spatial motifs in protein structures
    • Kleywegt, G.J. (1999) Recognition of spatial motifs in protein structures. J. Mol. Biol. 285, 1887-1897
    • (1999) J. Mol. Biol. , vol.285 , pp. 1887-1897
    • Kleywegt, G.J.1
  • 36
    • 0028579433 scopus 로고
    • Protein structural similarities predicted by a sequence-structure compatibility method
    • Matsuo, Y. and Nishikawa, K. (1994) Protein structural similarities predicted by a sequence-structure compatibility method. Protein Sci. 3, 2055-2063
    • (1994) Protein Sci. , vol.3 , pp. 2055-2063
    • Matsuo, Y.1    Nishikawa, K.2
  • 37
    • 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
  • 38
    • 0030855217 scopus 로고    scopus 로고
    • Three-dimensional structures and contexts associated with recurrent amino acid sequence patterns
    • Han, K.F. et al. (1997) Three-dimensional structures and contexts associated with recurrent amino acid sequence patterns. Protein Sci. 6, 1587-1590
    • (1997) Protein Sci. , vol.6 , pp. 1587-1590
    • Han, K.F.1
  • 39
    • 0027967593 scopus 로고
    • A graph-theoretic approach to the identification of three-dimensional patterns of amino acid side-chains in protein structures
    • Artymiuk, P.J. et al. (1994) A graph-theoretic approach to the identification of three-dimensional patterns of amino acid side-chains in protein structures. J. Mol. Biol. 236, 327-344
    • (1994) J. Mol. Biol. , vol.236 , pp. 327-344
    • Artymiuk, P.J.1
  • 40
    • 0029738719 scopus 로고    scopus 로고
    • Characterizations of diverse residue clusters in protein three-dimensional structures
    • Karlin, S. and Zhu, Z.Y. (1996) Characterizations of diverse residue clusters in protein three-dimensional structures. Proc. Natl. Acad. Sci. U. S. A. 93, 8344-8349
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8344-8349
    • Karlin, S.1    Zhu, Z.Y.2
  • 41
    • 0032475938 scopus 로고    scopus 로고
    • Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: Identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity
    • Fetrow, J.S. et al. (1998) Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: Identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity. J. Mol. Biol. 282, 703-711
    • (1998) J. Mol. Biol. , vol.282 , pp. 703-711
    • Fetrow, J.S.1
  • 43
    • 0032843737 scopus 로고    scopus 로고
    • Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily
    • Fetrow, J.S. et al. (1999) Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily. FASEB J. 13, 1866-1874
    • (1999) FASEB J. , vol.13 , pp. 1866-1874
    • Fetrow, J.S.1
  • 44
    • 0028871814 scopus 로고
    • Evaluation of comparative protein modeling by MODELLER
    • Sali, A. et al. (1995) Evaluation of comparative protein modeling by MODELLER. Proteins 23, 318-326
    • (1995) Proteins , vol.23 , pp. 318-326
    • Sali, A.1
  • 45
    • 0032555696 scopus 로고    scopus 로고
    • Prediction of local structure in proteins using a library of sequence-structure motifs
    • Bystroff, C. and Baker, D. (1998) Prediction of local structure in proteins using a library of sequence-structure motifs. J. Mol. Biol. 281, 565-577
    • (1998) J. Mol. Biol. , vol.281 , pp. 565-577
    • Bystroff, C.1    Baker, D.2
  • 46
    • 0033602488 scopus 로고    scopus 로고
    • The state of the art
    • Shortle, D. (1999) The state of the art. Curr. Biol. 9, R205-R209
    • (1999) Curr. Biol. , vol.9
    • Shortle, D.1
  • 47
    • 0032605909 scopus 로고    scopus 로고
    • Calculation of protein conformation by global optimization of a potential energy function
    • Lee, J. et al. (1999) Calculation of protein conformation by global optimization of a potential energy function. Proteins 3 (Suppl.), 204-208
    • (1999) Proteins , vol.3 , Issue.SUPPL. , pp. 204-208
    • Lee, J.1
  • 48
    • 0032613288 scopus 로고    scopus 로고
    • Ab initio folding of proteins using restraints derived from evolutionary information
    • Ortiz, A. et al. (1999) Ab initio folding of proteins using restraints derived from evolutionary information. Proteins 3 (Suppl.), 177-185
    • (1999) Proteins , vol.3 , Issue.SUPPL. , pp. 177-185
    • Ortiz, A.1
  • 49
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie, J.U. et al. (1991) A method to identify protein sequences that fold into a known three-dimensional structure. Science 253, 164-170
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1
  • 50
    • 0026418178 scopus 로고
    • A search for the most stable folds of protein chains
    • Finkelstein, A.V. and Reva, B.A. (1991) A search for the most stable folds of protein chains. Nature 351, 497-499
    • (1991) Nature , vol.351 , pp. 497-499
    • Finkelstein, A.V.1    Reva, B.A.2
  • 51
    • 0027318317 scopus 로고
    • An empirical energy function for threading protein sequence through folding motif
    • Bryant, S.H. and Lawrence, C.E. (1993) An empirical energy function for threading protein sequence through folding motif. Proteins 16, 92-112
    • (1993) Proteins , vol.16 , pp. 92-112
    • Bryant, S.H.1    Lawrence, C.E.2
  • 52
    • 0029912991 scopus 로고    scopus 로고
    • Global optimum protein threading with gapped alignment and empirical pair scoring function
    • Lathrop, R. and Smith, T.F. (1996) Global optimum protein threading with gapped alignment and empirical pair scoring function. J. Mol. Biol. 255, 641-665
    • (1996) J. Mol. Biol. , vol.255 , pp. 641-665
    • Lathrop, R.1    Smith, T.F.2
  • 53
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • Jones, D.T. et al (1992). A new approach to protein fold recognition. Nature 358, 86-89
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1
  • 54
    • 0033150685 scopus 로고    scopus 로고
    • Progress in protein structure prediction: Assessment of CASP3
    • Sternberg, M.J. et al. (1999) Progress in protein structure prediction: Assessment of CASP3. Curr. Opin. Struct. Biol. 9, 368-373
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 368-373
    • Sternberg, M.J.1
  • 55
    • 0030052366 scopus 로고    scopus 로고
    • Protein fold recognition by sequence threading tools and assessment techniques
    • Miller, R.T. et al. (1996) Protein fold recognition by sequence threading tools and assessment techniques. FASEB J. 10, 171-178
    • (1996) FASEB J. , vol.10 , pp. 171-178
    • Miller, R.T.1
  • 56
    • 0032571390 scopus 로고    scopus 로고
    • Fold assembly of small proteins using Monte Carlo simulations driven by restraints derived from multiple sequence alignments
    • Ortiz, A.R. et al. (1998) Fold assembly of small proteins using Monte Carlo simulations driven by restraints derived from multiple sequence alignments. J. Mol. Biol. 277, 419-448
    • (1998) J. Mol. Biol. , vol.277 , pp. 419-448
    • Ortiz, A.R.1
  • 57
    • 0031758128 scopus 로고    scopus 로고
    • Reduced protein models and their application to the protein folding problem
    • Skolnick, J. et al. (1998) Reduced protein models and their application to the protein folding problem. J. Biomol. Struct. Dyn. 16, 381-396
    • (1998) J. Biomol. Struct. Dyn. , vol.16 , pp. 381-396
    • Skolnick, J.1
  • 58
    • 0031746105 scopus 로고    scopus 로고
    • Fold prediction by a hierarchy of sequence, threading and modeling methods
    • Jaroszewski, L. et al. (1998) Fold prediction by a hierarchy of sequence, threading and modeling methods. Protein Sci. 7, 1431-1440
    • (1998) Protein Sci. , vol.7 , pp. 1431-1440
    • Jaroszewski, L.1
  • 59
    • 0029902963 scopus 로고    scopus 로고
    • Locations of functional domains in the RecA protein: Overlap of domains and regulation of activities
    • Takahashi, M. et al. (1996) Locations of functional domains in the RecA protein: Overlap of domains and regulation of activities. Eur. J. Biochem. 242, 20-28
    • (1996) Eur. J. Biochem. , vol.242 , pp. 20-28
    • Takahashi, M.1
  • 60
    • 0027500787 scopus 로고
    • Human rhinovirus-14 protease 3C (3Cpro) binds specifically to the 5 noncoding region of the viral RNA: Evidence that 3Cpro has different domains for the RNA binding and proteolytic activities
    • Leong, L.E. et al. (1993) Human rhinovirus-14 protease 3C (3Cpro) binds specifically to the 5 noncoding region of the viral RNA: Evidence that 3Cpro has different domains for the RNA binding and proteolytic activities. J. Biol. Chem. 268, 25735-25739
    • (1993) J. Biol. Chem. , vol.268 , pp. 25735-25739
    • Leong, L.E.1
  • 61
    • 0028235532 scopus 로고
    • Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site and means for cleaving precursor polyprotein
    • Matthews, D.A. et al. (1994) Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site and means for cleaving precursor polyprotein. Cell 77, 761-771
    • (1994) Cell , vol.77 , pp. 761-771
    • Matthews, D.A.1
  • 62
    • 0031259779 scopus 로고    scopus 로고
    • Multifunctional proteins suggest connections between transcriptional and post-transcriptional processes
    • Ladomery, M. (1997) Multifunctional proteins suggest connections between transcriptional and post-transcriptional processes. Bioessays 19, 903-909
    • (1997) Bioessays , vol.19 , pp. 903-909
    • Ladomery, M.1
  • 63
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg, J. et al. (1995) Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 376, 745-753
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1
  • 64
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: Structure, regulation and functions in cell growth
    • Mumby, M.C. and Walter, G. (1993) Protein serine/threonine phosphatases: Structure, regulation and functions in cell growth. Physiol. Rev. 73, 673-699
    • (1993) Physiol. Rev. , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 65
    • 0030628307 scopus 로고    scopus 로고
    • Protein phosphatases: Structures and implications
    • Jia, Z. (1997) Protein phosphatases: Structures and implications. Biochem. Cell Biol. 75, 17-26
    • (1997) Biochem. Cell Biol. , vol.75 , pp. 17-26
    • Jia, Z.1
  • 66
    • 0027138757 scopus 로고
    • Inhibitors of protein phosphatase-1 and -2A: Two of the major serine/threonine protein phosphatases involved in cellular regulation
    • Holmes, C.F.B. and Boland, M.P. (1993) Inhibitors of protein phosphatase-1 and -2A: Two of the major serine/threonine protein phosphatases involved in cellular regulation. Curr. Opin. Struct. Biol. 3, 934-943
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 934-943
    • Holmes, C.F.B.1    Boland, M.P.2
  • 67
    • 0027292006 scopus 로고
    • Reactivity of sulfhydryl groups of the catalytic subunits of rabbit skeletal muscle protein phosphatases 1 and 2A
    • Nemani, R. and Lee, E.Y.C. (1993) Reactivity of sulfhydryl groups of the catalytic subunits of rabbit skeletal muscle protein phosphatases 1 and 2A. Arch. Biochem. Biophys. 300, 24-29
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 24-29
    • Nemani, R.1    Lee, E.Y.C.2
  • 68
    • 0028961335 scopus 로고
    • Scop: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G. et al. (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
  • 69
    • 0030777303 scopus 로고    scopus 로고
    • CATH: A hierarchic classification of protein domain structures
    • Orengo, C.A. et al. (1997) CATH: A hierarchic classification of protein domain structures. Structure 5, 1093-1108
    • (1997) Structure , vol.5 , pp. 1093-1108
    • Orengo, C.A.1
  • 70
    • 0024529940 scopus 로고
    • Structural principles of α/β proteins: The packing of the interior of the sheet
    • Lesk, A.M. et al. (1989) Structural principles of α/β proteins: The packing of the interior of the sheet. Proteins Struct. Fund. Genet. 5, 139-148
    • (1989) Proteins Struct. Fund. Genet. , vol.5 , pp. 139-148
    • Lesk, A.M.1
  • 71
    • 0025284257 scopus 로고
    • The evolution of α/β barrel enzymes
    • Farber, G.K. and Petsko, G.A. (1990) The evolution of α/β barrel enzymes. Trends Biochem. Sci. 15, 228-234
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 72
    • 0033597176 scopus 로고    scopus 로고
    • The relationship between protein structure and function: A comprehensive survey with application to the yeast genome
    • Hegyi, H. and Gerstein, M. (1999) The relationship between protein structure and function: A comprehensive survey with application to the yeast genome. J. Mol. Biol. 288, 147-164
    • (1999) J. Mol. Biol. , vol.288 , pp. 147-164
    • Hegyi, H.1    Gerstein, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.