메뉴 건너뛰기




Volumn 332, Issue 2, 2003, Pages 505-526

Inferring functional relationships of proteins from local sequence and spatial surface patterns

Author keywords

Pocket sequence; Pocket shape; Protein function; Protein surface; Surface pattern

Indexed keywords

PROTEIN;

EID: 0042890523     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00882-9     Document Type: Article
Times cited : (136)

References (72)
  • 1
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein F., Koetzle T., Williams G., Meyer E., Brice M., Rodgers J., et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112:1977;535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.1    Koetzle, T.2    Williams, G.3    Meyer, E.4    Brice, M.5    Rodgers, J.6
  • 3
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin A., Brenner S., Hubbard T., Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:1995;536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.1    Brenner, S.2    Hubbard, T.3    Chothia, C.4
  • 5
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I., Bourne P. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11:1998;739-747.
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.1    Bourne, P.2
  • 6
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L., Sander C. Mapping the protein universe. Science. 273:1996;595-602.
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 8
    • 0035815113 scopus 로고    scopus 로고
    • Evolution of function in protein superfamilies, from a structural perspective
    • Todd A., Orengo C., Thornton J. Evolution of function in protein superfamilies, from a structural perspective. J. Mol. Biol. 307:2001;1113-1143.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1113-1143
    • Todd, A.1    Orengo, C.2    Thornton, J.3
  • 9
    • 0030935327 scopus 로고    scopus 로고
    • New structure: Novel fold?
    • Holm L., Sander C. New structure: novel fold? Structure. 5:1997;165-171.
    • (1997) Structure , vol.5 , pp. 165-171
    • Holm, L.1    Sander, C.2
  • 12
    • 0032506030 scopus 로고    scopus 로고
    • Large scale protein structure modeling of the Saccharomyces cerevisiae genome
    • Sanchez R., Sali A. Large scale protein structure modeling of the Saccharomyces cerevisiae genome. Proc. Natl Acad. Sci. USA. 95:1998;13597-13602.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13597-13602
    • Sanchez, R.1    Sali, A.2
  • 13
  • 14
    • 0032475963 scopus 로고    scopus 로고
    • Supersites within superfolds. Binding site similarity in the absence of homology
    • Russell R., Sasieni P., Sternberg J. Supersites within superfolds. Binding site similarity in the absence of homology. J. Mol. Biol. 282:1998;903-918.
    • (1998) J. Mol. Biol. , vol.282 , pp. 903-918
    • Russell, R.1    Sasieni, P.2    Sternberg, J.3
  • 15
    • 0033597176 scopus 로고    scopus 로고
    • The relationship between protein structure and function: A comprehensive survey with application to the yeast genome
    • Hegyi H., Gerstein M. The relationship between protein structure and function: a comprehensive survey with application to the yeast genome. J. Mol. Biol. 288:1999;147-164.
    • (1999) J. Mol. Biol. , vol.288 , pp. 147-164
    • Hegyi, H.1    Gerstein, M.2
  • 16
    • 0034677669 scopus 로고    scopus 로고
    • Assessing annotation transfer for genomics: Quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores
    • Wilson C., Kreychman J., Gerstein M. Assessing annotation transfer for genomics: quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores. J. Mol. Biol. 297:2000;233-249.
    • (2000) J. Mol. Biol. , vol.297 , pp. 233-249
    • Wilson, C.1    Kreychman, J.2    Gerstein, M.3
  • 19
    • 0027967593 scopus 로고
    • A graph-theoretic approach to the identification of three-dimensional patterns of amino acid side-chains in protein structure
    • Artymiuk P., Poirrette A., Grindley H., Rice D., Willett P. A graph-theoretic approach to the identification of three-dimensional patterns of amino acid side-chains in protein structure. J. Mol. Biol. 243:1994;327-344.
    • (1994) J. Mol. Biol. , vol.243 , pp. 327-344
    • Artymiuk, P.1    Poirrette, A.2    Grindley, H.3    Rice, D.4    Willett, P.5
  • 20
    • 0027168214 scopus 로고
    • Surface motifs by a computer vision technique: Searches, detection, and implications for protein-ligand recognition
    • Fischer D., Norel R., Wolfson H., Nussinov R. Surface motifs by a computer vision technique: searches, detection, and implications for protein-ligand recognition. Proteins: Struct. Funct. Genet. 16:1993;278-292.
    • (1993) Proteins: Struct. Funct. Genet. , vol.16 , pp. 278-292
    • Fischer, D.1    Norel, R.2    Wolfson, H.3    Nussinov, R.4
  • 21
    • 0028079323 scopus 로고
    • Molecular surface recognition by computer vision-based technique
    • Norel R., Fischer D., Wolfson H., Nussinov R. Molecular surface recognition by computer vision-based technique. Protein Eng. 7:1994;39-46.
    • (1994) Protein Eng. , vol.7 , pp. 39-46
    • Norel, R.1    Fischer, D.2    Wolfson, H.3    Nussinov, R.4
  • 22
    • 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., Borkakoti N., Thornton J. TESS: a geometric hashing algorithm for deriving 3d coordinate templates for searching structural databases. Application to enzyme active sites. Protein Sci. 6:1997;2308-2323.
    • (1997) Protein Sci. , vol.6 , pp. 2308-2323
    • Wallace, A.1    Borkakoti, N.2    Thornton, J.3
  • 23
    • 0032568859 scopus 로고    scopus 로고
    • Detection of protein three-dimensional side-chain patterns: New examples of convergent evolution
    • Russell R. Detection of protein three-dimensional side-chain patterns: new examples of convergent evolution. J. Mol. Biol. 279:1998;1211-1227.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1211-1227
    • Russell, R.1
  • 24
    • 0037424601 scopus 로고    scopus 로고
    • A model for statistical significance of local similarities in structure
    • Stark A., Sunyaev S., Russell R. A model for statistical significance of local similarities in structure. J. Mol. Biol. 326:2003;1307-1316.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1307-1316
    • Stark, A.1    Sunyaev, S.2    Russell, R.3
  • 25
    • 0036406643 scopus 로고    scopus 로고
    • A new method to detect related function among proteins independent of sequence and fold homology
    • Schmitt S., Kuhn D., Klebe G. A new method to detect related function among proteins independent of sequence and fold homology. J. Mol. Biol. 323:2002;387-406.
    • (2002) J. Mol. Biol. , vol.323 , pp. 387-406
    • Schmitt, S.1    Kuhn, D.2    Klebe, G.3
  • 26
    • 0034490962 scopus 로고    scopus 로고
    • Thirty-plus functional families from a single motif
    • Yu L., Gaitatzes C., Neer E., Smith T. Thirty-plus functional families from a single motif. Protein Sci. 9:2000;2470-2476.
    • (2000) Protein Sci. , vol.9 , pp. 2470-2476
    • Yu, L.1    Gaitatzes, C.2    Neer, E.3    Smith, T.4
  • 27
    • 0031678064 scopus 로고    scopus 로고
    • A homology identification method that combines protein sequence and structure information
    • Yu L., White J., Smith T. A homology identification method that combines protein sequence and structure information. Protein Sci. 7:1998;2499-2510.
    • (1998) Protein Sci. , vol.7 , pp. 2499-2510
    • Yu, L.1    White, J.2    Smith, T.3
  • 28
    • 0024046461 scopus 로고
    • Analysis and prediction for the location of catalytic residues in enzymes
    • Zvelebil M., Sternberg M. Analysis and prediction for the location of catalytic residues in enzymes. Protein Eng. 2:1988;127-138.
    • (1988) Protein Eng. , vol.2 , pp. 127-138
    • Zvelebil, M.1    Sternberg, M.2
  • 29
    • 0344405703 scopus 로고    scopus 로고
    • Prediction of catalytic residues in enzymes based on known tertiary structure, stability profile, and sequence conservation
    • Ota M., Kinoshita K., Nishikawa K. Prediction of catalytic residues in enzymes based on known tertiary structure, stability profile, and sequence conservation. J. Mol. Biol. 327:2003;1053-1064.
    • (2003) J. Mol. Biol. , vol.327 , pp. 1053-1064
    • Ota, M.1    Kinoshita, K.2    Nishikawa, K.3
  • 31
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design
    • Liang J., Edelsbrunner H., Woodward C. Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein Sci. 7:1998;1884-1897.
    • (1998) Protein Sci. , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelsbrunner, H.2    Woodward, C.3
  • 33
    • 0002052671 scopus 로고    scopus 로고
    • On the definition and the construction of pockets in macromolecules
    • Edelsbrunner H., Facello M., Liang J. On the definition and the construction of pockets in macromolecules. Discrete Appl. Math. 88:1998;83-102.
    • (1998) Discrete Appl. Math. , vol.88 , pp. 83-102
    • Edelsbrunner, H.1    Facello, M.2    Liang, J.3
  • 34
    • 0032189626 scopus 로고    scopus 로고
    • Analytic shape computation of macromolecules: II. Identification and computation of inaccessible cavities inside proteins
    • Liang J., Edelsbrunner H., Fu P., Sudhakar P., Subramaniam S. Analytic shape computation of macromolecules: II. Identification and computation of inaccessible cavities inside proteins. Proteins: Struct. Funct. Genet. 33:1998;18-29.
    • (1998) Proteins: Struct. Funct. Genet. , vol.33 , pp. 18-29
    • Liang, J.1    Edelsbrunner, H.2    Fu, P.3    Sudhakar, P.4    Subramaniam, S.5
  • 35
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins
    • Binkowski T., Naghibzadeh S., Liang J. CASTp: Computed atlas of surface topography of proteins. Nucl. Acids Res. 31:2003;3352-3355.
    • (2003) Nucl. Acids Res. , vol.31 , pp. 3352-3355
    • Binkowski, T.1    Naghibzadeh, S.2    Liang, J.3
  • 36
    • 0032749097 scopus 로고    scopus 로고
    • Unit-vector rms (urms) as a tool to analyze molecular dynamics trajectories
    • Kedem K., Chew L., Elber R. Unit-vector rms (urms) as a tool to analyze molecular dynamics trajectories. Proteins: Struct. Funct. Genet. 37:1999;554-564.
    • (1999) Proteins: Struct. Funct. Genet. , vol.37 , pp. 554-564
    • Kedem, K.1    Chew, L.2    Elber, R.3
  • 37
    • 0017429069 scopus 로고
    • Areas, volumes, packing, and protein structures
    • Richards F. Areas, volumes, packing, and protein structures. Annu. Rev. Biophys. Bioeng. 6:1977;151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.1
  • 38
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia C. Structural invariants in protein folding. Nature. 254:1975;304-308.
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 39
    • 0027815614 scopus 로고
    • An analysis of packing in the protein folding problem
    • Richards F., Lim W. An analysis of packing in the protein folding problem. Quart. Rev. Biophys. 26:1994;423-498.
    • (1994) Quart. Rev. Biophys. , vol.26 , pp. 423-498
    • Richards, F.1    Lim, W.2
  • 40
    • 0034901412 scopus 로고    scopus 로고
    • Are proteins well-packed?
    • Liang J., Dill K. Are proteins well-packed? Biophys. J. 81:2001;751-766.
    • (2001) Biophys. J. , vol.81 , pp. 751-766
    • Liang, J.1    Dill, K.2
  • 41
    • 21144462070 scopus 로고
    • Universality and cluster structures in continuum models of percolation with two different radius distributions
    • Lorenz B., Orgzall I., Heuer H.-O. Universality and cluster structures in continuum models of percolation with two different radius distributions. J. Phys. A: Math. Gen. 26:1993;4711-4722.
    • (1993) J. Phys. A: Math. Gen. , vol.26 , pp. 4711-4722
    • Lorenz, B.1    Orgzall, I.2    Heuer, H.-O.3
  • 42
    • 0037103826 scopus 로고    scopus 로고
    • Statistical geometry of packing defects of lattice chain polymer from enumeration and sequential Monte Carlo method
    • Liang J., Zhang J., Chen R. Statistical geometry of packing defects of lattice chain polymer from enumeration and sequential Monte Carlo method. J. Chem. Phys. 117:2002;3511-3521.
    • (2002) J. Chem. Phys. , vol.117 , pp. 3511-3521
    • Liang, J.1    Zhang, J.2    Chen, R.3
  • 43
    • 0344088344 scopus 로고    scopus 로고
    • Origin of scaling behavior of protein packing density: A sequential Monte Carlo study of compact long chain polymers
    • Zhang J., Chen R., Tang C., Liang J. Origin of scaling behavior of protein packing density: a sequential Monte Carlo study of compact long chain polymers. J. Chem. Phys. 118:2003;6102-6109.
    • (2003) J. Chem. Phys. , vol.118 , pp. 6102-6109
    • Zhang, J.1    Chen, R.2    Tang, C.3    Liang, J.4
  • 44
    • 51249162203 scopus 로고
    • The union of balls and its dual shape
    • Edelsbrunner H. The union of balls and its dual shape. Discrete Comput. Geom. Des. 13:1995;415-440.
    • (1995) Discrete Comput. Geom. Des. , vol.13 , pp. 415-440
    • Edelsbrunner, H.1
  • 45
    • 0029325383 scopus 로고
    • Implementation of a randomized algorithm for delaunay and regular triangulations in three dimensions
    • Facello M. Implementation of a randomized algorithm for delaunay and regular triangulations in three dimensions. Comput. Aided Geom. Des. 12:1995;349-370.
    • (1995) Comput. Aided Geom. Des. , vol.12 , pp. 349-370
    • Facello, M.1
  • 46
    • 0027092678 scopus 로고
    • Selection of a representative set of structures from the Brookhaven Protein Data Bank
    • Hobohm U., Sander C. Selection of a representative set of structures from the Brookhaven Protein Data Bank. Protein Sci. 1:1992;409-417.
    • (1992) Protein Sci. , vol.1 , pp. 409-417
    • Hobohm, U.1    Sander, C.2
  • 47
  • 48
    • 0032512799 scopus 로고    scopus 로고
    • Empirical statistical estimates for sequence similarity searches
    • Pearson W. Empirical statistical estimates for sequence similarity searches. J. Mol. Biol. 276:1998;71-84.
    • (1998) J. Mol. Biol. , vol.276 , pp. 71-84
    • Pearson, W.1
  • 49
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S., Henikoff J. Amino acid substitution matrices from protein blocks. Proc. Natl Acad. Sci. USA. 89:1992;915-919.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 915-919
    • Henikoff, S.1    Henikoff, J.2
  • 50
    • 0025259313 scopus 로고
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
    • Karlin S., Altschul S.F. Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes. Proc. Natl Acad. Sci. USA. 87:1990;2264-2268.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2264-2268
    • Karlin, S.1    Altschul, S.F.2
  • 51
    • 0029889221 scopus 로고    scopus 로고
    • Local alignment statistics
    • Altschul S.F., Gish W. Local alignment statistics. Methods Enzymol. 266:1996;460-480.
    • (1996) Methods Enzymol. , vol.266 , pp. 460-480
    • Altschul, S.F.1    Gish, W.2
  • 53
    • 0033990061 scopus 로고    scopus 로고
    • Flexible sequence similarity searching with the FASTA3 program package
    • Pearson W. Flexible sequence similarity searching with the FASTA3 program package. Methods Mol. Biol. 132:2000;185-219.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 185-219
    • Pearson, W.1
  • 54
    • 0026137964 scopus 로고
    • Least-squares estimation of transformation parameters between two point patterns
    • Umeyama S. Least-squares estimation of transformation parameters between two point patterns. IEEE Trans. Pattern Anal. Mach. Intell. 13:1991;376-380.
    • (1991) IEEE Trans. Pattern Anal. Mach. Intell. , vol.13 , pp. 376-380
    • Umeyama, S.1
  • 56
    • 0041463039 scopus 로고
    • Gene duplication in the structural evolution of chymotrypsin
    • McLachlan A. Gene duplication in the structural evolution of chymotrypsin. J. Mol. Biol. 247:1979;536-540.
    • (1979) J. Mol. Biol. , vol.247 , pp. 536-540
    • McLachlan, A.1
  • 57
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallog. sect. A. 32:1976;922-923.
    • (1976) Acta Crystallog. sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 60
    • 0022648659 scopus 로고
    • Primary structure of Torpedo califonica acetylcholinesterase deduced from its cDNA sequence
    • Schumacher M., Camp S., Maulet Y., Newton M., MacPhee-Quigley K., Taylor S., et al. Primary structure of Torpedo califonica acetylcholinesterase deduced from its cDNA sequence. Nature. 319:1986;407-409.
    • (1986) Nature , vol.319 , pp. 407-409
    • Schumacher, M.1    Camp, S.2    Maulet, Y.3    Newton, M.4    MacPhee-Quigley, K.5    Taylor, S.6
  • 61
    • 0025108755 scopus 로고
    • Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0 Å resolution
    • Fitzgerald P., McKeever B., Van Middlesworth J.F., Springer J., Heimbach J.C., Leu C.T., et al. Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0 Å resolution. J. Biol. Chem. 265:1990;14209-14219.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14209-14219
    • Fitzgerald, P.1    McKeever, B.2    Van Middlesworth, J.F.3    Springer, J.4    Heimbach, J.C.5    Leu, C.T.6
  • 62
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins C., Russo A., Schneider C., Rosen N., Hartl F., Pavletich N. Crystal structure of an hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell. 89:1998;239-250.
    • (1998) Cell , vol.89 , pp. 239-250
    • Stebbins, C.1    Russo, A.2    Schneider, C.3    Rosen, N.4    Hartl, F.5    Pavletich, N.6
  • 63
    • 0032540849 scopus 로고    scopus 로고
    • Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: A substrate recognition site constructed by rearrangement of hydrogen bond network
    • Okamoto A., Nakai Y., Hayashi K., Kagamiyma H. Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network. J. Mol. Biol. 280:1998;1176-1999.
    • (1998) J. Mol. Biol. , vol.280 , pp. 1176-1999
    • Okamoto, A.1    Nakai, Y.2    Hayashi, K.3    Kagamiyma, H.4
  • 64
    • 0033604853 scopus 로고    scopus 로고
    • The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: Flexibility and rigidity
    • Okamoto A., Ishii S., Hirotsu K., Kagamiyama H. The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: flexibility and rigidity. Biochemistry. 38:1999;1176-1184.
    • (1999) Biochemistry , vol.38 , pp. 1176-1184
    • Okamoto, A.1    Ishii, S.2    Hirotsu, K.3    Kagamiyama, H.4
  • 66
    • 0030720480 scopus 로고    scopus 로고
    • A structural census of the current population of protein sequences
    • Gerstein M., Levitt M. A structural census of the current population of protein sequences. Proc. Natl Acad. Sci. USA. 94:1997;11911-11916.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11911-11916
    • Gerstein, M.1    Levitt, M.2
  • 67
    • 0019001660 scopus 로고
    • On the prediction of protein structure: The significance of the root-mean square deviation
    • Cohen F., Sternberg M. On the prediction of protein structure: the significance of the root-mean square deviation. J. Mol. Biol. 138:1980;321-333.
    • (1980) J. Mol. Biol. , vol.138 , pp. 321-333
    • Cohen, F.1    Sternberg, M.2
  • 68
    • 0000939821 scopus 로고    scopus 로고
    • What is the probability of a chance prediction of a protein structure with an rmsd of 6 Å?
    • Reva B., Finkelstein A., Skolnick J. What is the probability of a chance prediction of a protein structure with an rmsd of 6 Å? Fold. Des. 3:1998;141-147.
    • (1998) Fold. Des. , vol.3 , pp. 141-147
    • Reva, B.1    Finkelstein, A.2    Skolnick, J.3
  • 69
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S., Henikoff J. Amino acid substitution matrices from protein blocks. Proc. Natl Acad. Sci. USA. 89:1992;10915-10919.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.2
  • 70
    • 0025878149 scopus 로고
    • Amino acid substitution matrices
    • Altschul S. Amino acid substitution matrices. J. Mol. Biol. 219:1991;555-565.
    • (1991) J. Mol. Biol. , vol.219 , pp. 555-565
    • Altschul, S.1
  • 71
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S., Goldman N. A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 18:2001;691-699.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 72
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology
    • Consortium T.G.O. Gene ontology: tool for the unification of biology. Nature Genet. 25:2000;25-29.
    • (2000) Nature Genet. , vol.25 , pp. 25-29
    • Consortium, T.G.O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.