메뉴 건너뛰기




Volumn 75, Issue C, 2008, Pages 107-141

Chapter 4 Predicting and Characterizing Protein Functions Through Matching Geometric and Evolutionary Patterns of Binding Surfaces

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 77951010649     PISSN: 18761623     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(07)75004-0     Document Type: Review
Times cited : (4)

References (69)
  • 1
    • 0002367729 scopus 로고    scopus 로고
    • MOLPHY, version 2.3. Programs for molecular phylogenetics based on maximum likelihood
    • Adachi J., and Hasegawa M. MOLPHY, version 2.3. Programs for molecular phylogenetics based on maximum likelihood. Comput. Sci. Monogr. Inst. Stat. Math. Tokyo 28 (1996) 1-150
    • (1996) Comput. Sci. Monogr. Inst. Stat. Math. Tokyo , vol.28 , pp. 1-150
    • Adachi, J.1    Hasegawa, M.2
  • 2
    • 33846515820 scopus 로고    scopus 로고
    • Evolutionary patterns of retinal-binding pockets of type I rhodopsins and their functions
    • Adamian L., Ouyang Z., Tseng Y.Y., and Liang J. Evolutionary patterns of retinal-binding pockets of type I rhodopsins and their functions. Photochem. Photobiol. 82 6 (2006) 1426-1435
    • (2006) Photochem. Photobiol. , vol.82 , Issue.6 , pp. 1426-1435
    • Adamian, L.1    Ouyang, Z.2    Tseng, Y.Y.3    Liang, J.4
  • 5
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • Bateman A. The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem. Sci. 22 1 (1997) 12-13
    • (1997) Trends Biochem. Sci. , vol.22 , Issue.1 , pp. 12-13
    • Bateman, A.1
  • 8
    • 0002610737 scopus 로고
    • On a routing problem
    • Bellman R. On a routing problem. Q. Appl. Math. 16 1 (1958) 87-90
    • (1958) Q. Appl. Math. , vol.16 , Issue.1 , pp. 87-90
    • Bellman, R.1
  • 9
    • 0042890523 scopus 로고    scopus 로고
    • Inferring functional relationships of proteins from local sequence and spatial surface patterns
    • Binkowski T.A., Adamian L., and Liang J. Inferring functional relationships of proteins from local sequence and spatial surface patterns. J. Mol. Biol. 332 (2003) 505-526
    • (2003) J. Mol. Biol. , vol.332 , pp. 505-526
    • Binkowski, T.A.1    Adamian, L.2    Liang, J.3
  • 10
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins
    • Binkowski T.A., Naghibzadeh S., and Liang J. CASTp: Computed atlas of surface topography of proteins. Nucleic Acids Res. 31 (2003) 3352-3355
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3
  • 11
    • 3242883091 scopus 로고    scopus 로고
    • pvSOAR: Detecting similar surface patterns of pocket and void surfaces of amino acid residues on proteins
    • Binkowski T.A., Freeman P., and Liang J. pvSOAR: Detecting similar surface patterns of pocket and void surfaces of amino acid residues on proteins. Nucleic Acids Res. 32 (2004) W555-W558
    • (2004) Nucleic Acids Res. , vol.32
    • Binkowski, T.A.1    Freeman, P.2    Liang, J.3
  • 12
    • 28844492648 scopus 로고    scopus 로고
    • Protein surface analysis for function annotation in high-throughput structural genomics pipeline
    • Binkowski T.A., Joachimia A., and Liang J. Protein surface analysis for function annotation in high-throughput structural genomics pipeline. Protein Sci. 14 (2005) 2972-2981
    • (2005) Protein Sci. , vol.14 , pp. 2972-2981
    • Binkowski, T.A.1    Joachimia, A.2    Liang, J.3
  • 13
    • 31144467558 scopus 로고    scopus 로고
    • The impact of structural genomics: Expectations and outcomes
    • Chandonia J.M., and Brenner S.E. The impact of structural genomics: Expectations and outcomes. Science 311 5759 (2006) 347-351
    • (2006) Science , vol.311 , Issue.5759 , pp. 347-351
    • Chandonia, J.M.1    Brenner, S.E.2
  • 14
    • 33745808624 scopus 로고    scopus 로고
    • Comparison of protein structures by multi-objective optimization
    • Chen L., Wu L.Y., Wang R., Wang Y., Zhang S., and Zhang X.S. Comparison of protein structures by multi-objective optimization. Genome Informatics 16 2 (2005) 114-124
    • (2005) Genome Informatics , vol.16 , Issue.2 , pp. 114-124
    • Chen, L.1    Wu, L.Y.2    Wang, R.3    Wang, Y.4    Zhang, S.5    Zhang, X.S.6
  • 18
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas J., Ouyang Z., Tseng J., Binkowski A., Turpaz Y., and Liang J. CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res 34 Web Server issue (2006) W116-W118
    • (2006) Nucleic Acids Res , vol.34 , Issue.Web Server issue
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 19
    • 44449165575 scopus 로고    scopus 로고
    • Novel approach to structure-based pharmacophore search using computational geometry and shape matching techniques
    • Ebalunode J.O., Ouyang Z., Liang J., and Zheng W. Novel approach to structure-based pharmacophore search using computational geometry and shape matching techniques. J. Chem. Inf. Model. 48 4 (2008) 889-901
    • (2008) J. Chem. Inf. Model. , vol.48 , Issue.4 , pp. 889-901
    • Ebalunode, J.O.1    Ouyang, Z.2    Liang, J.3    Zheng, W.4
  • 21
    • 0002052671 scopus 로고    scopus 로고
    • On the definition and the construction of pockets in macromolecules
    • Edelsbrunner H., Facello M., and 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
  • 24
    • 2542445427 scopus 로고    scopus 로고
    • Consurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser F., Pupko T., Paz I., Bell R.E., Shental D., Martz E., and Tal N. Consurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19 (2003) 163-164
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Shental, D.5    Martz, E.6    Tal, N.7
  • 25
    • 29444457054 scopus 로고    scopus 로고
    • Fold independent structural comparisons of protein-ligand binding sites for exploring functional relationships
    • Gold N.D., and Jackson R.M. Fold independent structural comparisons of protein-ligand binding sites for exploring functional relationships. J. Mol. Biol. 355 (2006) 1112-1124
    • (2006) J. Mol. Biol. , vol.355 , pp. 1112-1124
    • Gold, N.D.1    Jackson, R.M.2
  • 27
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S., and Henikoff J.G. 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.G.2
  • 28
    • 0035861456 scopus 로고    scopus 로고
    • Bayesian inference of phylogeny and its impact on evolutionary biology
    • Huelsenbeck J.P., Ronquist F., Nielsen R., and Bollback J.P. Bayesian inference of phylogeny and its impact on evolutionary biology. Science 294 (2001) 2310-2314
    • (2001) Science , vol.294 , pp. 2310-2314
    • Huelsenbeck, J.P.1    Ronquist, F.2    Nielsen, R.3    Bollback, J.P.4
  • 29
    • 8444236034 scopus 로고    scopus 로고
    • A new scoring function and associated statistical significance for structure alignment by CE
    • Jia Y., Dewey G., Shindyalov I.N., and Bourne P.E. A new scoring function and associated statistical significance for structure alignment by CE. J. Comput. Biol. 11 5 (2004) 787-799
    • (2004) J. Comput. Biol. , vol.11 , Issue.5 , pp. 787-799
    • Jia, Y.1    Dewey, G.2    Shindyalov, I.N.3    Bourne, P.E.4
  • 30
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones D.T., Taylor W.R., and Thornton J.M. The rapid generation of mutation data matrices from protein sequences. CABIOS 8 (1992) 275-282
    • (1992) CABIOS , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 31
    • 0025259313 scopus 로고
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
    • Karlin S., and 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
  • 32
    • 44649186755 scopus 로고    scopus 로고
    • Screening and characterization of proteorhodopsin color-tuning mutations in Escherichia coli with endogenous retinal synthesis
    • Kim S.Y., Waschuk S.A., Brown L.S., and Jung K.H. Screening and characterization of proteorhodopsin color-tuning mutations in Escherichia coli with endogenous retinal synthesis. Biochim. Biophys. Acta 1777 6 (2008) 504-513
    • (2008) Biochim. Biophys. Acta , vol.1777 , Issue.6 , pp. 504-513
    • Kim, S.Y.1    Waschuk, S.A.2    Brown, L.S.3    Jung, K.H.4
  • 33
    • 0002719797 scopus 로고
    • The Hungarian method for the assignment problem
    • Kuhn H.W. The Hungarian method for the assignment problem. Nav. Res. Logist. Q. 2 (1955) 83-97
    • (1955) Nav. Res. Logist. Q. , vol.2 , pp. 83-97
    • Kuhn, H.W.1
  • 34
    • 22544486576 scopus 로고    scopus 로고
    • Protein function prediction using local 3D templates
    • Laskowski R.A., Watson J.D., and Thornton J.M. Protein function prediction using local 3D templates. J. Mol. Biol. 351 (2005) 614-626
    • (2005) J. Mol. Biol. , vol.351 , pp. 614-626
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 35
    • 0032568649 scopus 로고    scopus 로고
    • A unified statistical framework for sequence comparison and structure comparison
    • Levitt M., and Gerstein M. A unified statistical framework for sequence comparison and structure comparison. Proc. Natl Acad. Sci. USA 95 (1998) 5913-5920
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5913-5920
    • Levitt, M.1    Gerstein, M.2
  • 36
    • 0034901412 scopus 로고    scopus 로고
    • Are proteins well-packed?
    • Liang J., and Dill K.A. Are proteins well-packed?. Biophys. J. 81 2 (2001) 751-766
    • (2001) Biophys. J. , vol.81 , Issue.2 , pp. 751-766
    • Liang, J.1    Dill, K.A.2
  • 37
    • 0032190305 scopus 로고    scopus 로고
    • Analytical shape computing of macromolecules I: Molecular area and volume through alpha-shape
    • Liang J., Edelsbrunner H., Fu P., Sudhakar P.V., and Subramaniam S. Analytical shape computing of macromolecules I: Molecular area and volume through alpha-shape. Proteins 33 (1998) 1-17
    • (1998) Proteins , vol.33 , pp. 1-17
    • Liang, J.1    Edelsbrunner, H.2    Fu, P.3    Sudhakar, P.V.4    Subramaniam, S.5
  • 38
    • 0032189626 scopus 로고    scopus 로고
    • Analytical shape computing of macromolecules II: Identification and computation of inaccessible cavities inside proteins
    • Liang J., Edelsbrunner H., Fu P., Sudhakar P.V., and Subramaniam S. Analytical shape computing of macromolecules II: Identification and computation of inaccessible cavities inside proteins. Proteins 33 (1998) 18-29
    • (1998) Proteins , vol.33 , pp. 18-29
    • Liang, J.1    Edelsbrunner, H.2    Fu, P.3    Sudhakar, P.V.4    Subramaniam, S.5
  • 39
    • 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., and 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
  • 41
    • 0032359151 scopus 로고    scopus 로고
    • Sequential Monte Carlo methods for dynamic systems
    • Liu J.S., and Chen R. Sequential Monte Carlo methods for dynamic systems. J. Am. Stat. Assoc. 93 (1998) 1032-1044
    • (1998) J. Am. Stat. Assoc. , vol.93 , pp. 1032-1044
    • Liu, J.S.1    Chen, R.2
  • 42
    • 16344374288 scopus 로고    scopus 로고
    • Structural basis for high-affinity volatile anesthetic binding in a natural 4-helix bundle protein
    • Liu R., Loll P.J., and Eckenhoff R.G. Structural basis for high-affinity volatile anesthetic binding in a natural 4-helix bundle protein. FASEB J. 19 6 (2005) 567-576
    • (2005) FASEB J. , vol.19 , Issue.6 , pp. 567-576
    • Liu, R.1    Loll, P.J.2    Eckenhoff, R.G.3
  • 43
    • 21144462070 scopus 로고
    • Universality and cluster structures in continuum models of percolation with two different radius distributions
    • Lorenz B., Orgzall I., and 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
  • 45
    • 4143051195 scopus 로고    scopus 로고
    • Comparison of site-specific rate-inference methods for protein sequences: Empirical Bayesian methods are superior
    • Mayrose I., Graur D., Tal N., and Pupko T. Comparison of site-specific rate-inference methods for protein sequences: Empirical Bayesian methods are superior. Mol. Biol. Evol. 21 (2004) 1781-1791
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1781-1791
    • Mayrose, I.1    Graur, D.2    Tal, N.3    Pupko, T.4
  • 46
    • 27744571119 scopus 로고    scopus 로고
    • Prediction of protein function from structure: Insights from methods for the detection of local structural similarities
    • Najmanovich R.J., Torrance J.W., and Thornton J.M. Prediction of protein function from structure: Insights from methods for the detection of local structural similarities. BioTechniques 38 6 (2005) 847-851
    • (2005) BioTechniques , vol.38 , Issue.6 , pp. 847-851
    • Najmanovich, R.J.1    Torrance, J.W.2    Thornton, J.M.3
  • 47
    • 6944227836 scopus 로고    scopus 로고
    • Automated prediction of protein function and detection of functional sites from structure
    • Pazos F., and Sternberg M.J. Automated prediction of protein function and detection of functional sites from structure. Proc. Natl Acad. Sci. USA 101 41 (2004) 14754-14759
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.41 , pp. 14754-14759
    • Pazos, F.1    Sternberg, M.J.2
  • 48
    • 0025950944 scopus 로고
    • Searching protein sequence libraries: Comparison of the sensitivity and selectivity of the Smith-Waterman and FASTA algorithms
    • Pearson W.R. Searching protein sequence libraries: Comparison of the sensitivity and selectivity of the Smith-Waterman and FASTA algorithms. Genomics 11 (1991) 635-650
    • (1991) Genomics , vol.11 , pp. 635-650
    • Pearson, W.R.1
  • 49
  • 50
    • 0027815614 scopus 로고
    • An analysis of packing in the protein folding problem
    • Richards F.M., and Lim W.A. An analysis of packing in the protein folding problem. Q. Rev. Biophys. 26 (1994) 423-498
    • (1994) Q. Rev. Biophys. , vol.26 , pp. 423-498
    • Richards, F.M.1    Lim, W.A.2
  • 51
    • 0036308741 scopus 로고    scopus 로고
    • Enzyme function less conserved than anticipated
    • Rost B. Enzyme function less conserved than anticipated. J. Mol. Biol. 318 (2002) 595-608
    • (2002) J. Mol. Biol. , vol.318 , pp. 595-608
    • Rost, B.1
  • 52
    • 0032568859 scopus 로고    scopus 로고
    • Detection of protein three-dimensional side-chain patterns: New examples of convergent evolution
    • Russell R.B. 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.B.1
  • 57
    • 0142106373 scopus 로고    scopus 로고
    • How well is enzyme function conserved as a function of pairwise sequence identity?
    • Tian W., and Skolnick J. How well is enzyme function conserved as a function of pairwise sequence identity?. J. Mol. Biol. 333 (2003) 863-882
    • (2003) J. Mol. Biol. , vol.333 , pp. 863-882
    • Tian, W.1    Skolnick, J.2
  • 58
    • 14744305761 scopus 로고    scopus 로고
    • Using a library of structural templates to recognise catalytic sites and explore their evolution in homologous families
    • Torrance J.W., Bartlett G.J., Porter C.T., and Thornton J.M. Using a library of structural templates to recognise catalytic sites and explore their evolution in homologous families. J. Mol. Biol. 347 (2005) 565-581
    • (2005) J. Mol. Biol. , vol.347 , pp. 565-581
    • Torrance, J.W.1    Bartlett, G.J.2    Porter, C.T.3    Thornton, J.M.4
  • 59
    • 30744465573 scopus 로고    scopus 로고
    • Estimation of amino acid residue substitution rates at local spatial regions and application in protein function inference: A Bayesian Monte Carlo approach
    • Tseng Y.Y., and Liang J. Estimation of amino acid residue substitution rates at local spatial regions and application in protein function inference: A Bayesian Monte Carlo approach. Mol. Biol. Evol. 23 2 (2006) 421-436
    • (2006) Mol. Biol. Evol. , vol.23 , Issue.2 , pp. 421-436
    • Tseng, Y.Y.1    Liang, J.2
  • 60
    • 34249712850 scopus 로고    scopus 로고
    • Predicting enzyme functional surfaces and locating key residues automatically from structures
    • Tseng Y.Y., and Liang J. Predicting enzyme functional surfaces and locating key residues automatically from structures. Ann. Biomed. Eng. 35 6 (2007) 1037-1042
    • (2007) Ann. Biomed. Eng. , vol.35 , Issue.6 , pp. 1037-1042
    • Tseng, Y.Y.1    Liang, J.2
  • 61
    • 0026137964 scopus 로고
    • Least-square estimation of transformation parameters between two point patterns
    • Umeyama S. Least-square 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
  • 62
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S., and 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
  • 63
    • 0035339920 scopus 로고    scopus 로고
    • Molecular phylogenetics: State-of-the-art methods for looking into the past
    • Whelan S., Liò P., and Goldman N. Molecular phylogenetics: State-of-the-art methods for looking into the past. Trends Genet. 17 (2001) 262-272
    • (2001) Trends Genet. , vol.17 , pp. 262-272
    • Whelan, S.1    Liò, P.2    Goldman, N.3
  • 64
    • 0030683599 scopus 로고    scopus 로고
    • PAML: A program package for phylogenetic analysis by maximum likelihood
    • Yang Z. PAML: A program package for phylogenetic analysis by maximum likelihood. Comput. Appl. Biosci. 13 (1997) 555-556
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 555-556
    • Yang, Z.1
  • 65
    • 3042533398 scopus 로고    scopus 로고
    • Database searching by flexible protein structure alignment
    • Ye Y., and Godzik A. Database searching by flexible protein structure alignment. Protein Sci. 13 (2004) 1841-1850
    • (2004) Protein Sci. , vol.13 , pp. 1841-1850
    • Ye, Y.1    Godzik, A.2
  • 66
    • 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., and 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
  • 67
    • 0037403053 scopus 로고    scopus 로고
    • Conserved protein YecM from Escherichia coli shows structural homology to metal-binding isomerases and oxygenases
    • Zhang R.G., Duke N., Laskowski R., Evdokimova E., Skarina T., Edwards A., Joachimiak A., and Savchenko A. Conserved protein YecM from Escherichia coli shows structural homology to metal-binding isomerases and oxygenases. Proteins 51 2 (2003) 311-314
    • (2003) Proteins , vol.51 , Issue.2 , pp. 311-314
    • Zhang, R.G.1    Duke, N.2    Laskowski, R.3    Evdokimova, E.4    Skarina, T.5    Edwards, A.6    Joachimiak, A.7    Savchenko, A.8
  • 68
    • 0041384346 scopus 로고    scopus 로고
    • The 2.2 A resolution structure of RpiB/AlsB from Escherichia coli illustrates a new approach to the ribose-5-phosphate isomerase reaction
    • Zhang R.G., Andersson C.E., Skarina T., Evdokimova E., Edwards A.M., Joachimiak A., Savchenko A., and Mowbray S.L. The 2.2 A resolution structure of RpiB/AlsB from Escherichia coli illustrates a new approach to the ribose-5-phosphate isomerase reaction. J. Mol. Biol. 332 5 (2003) 1083-1094
    • (2003) J. Mol. Biol. , vol.332 , Issue.5 , pp. 1083-1094
    • Zhang, R.G.1    Andersson, C.E.2    Skarina, T.3    Evdokimova, E.4    Edwards, A.M.5    Joachimiak, A.6    Savchenko, A.7    Mowbray, S.L.8
  • 69
    • 34447292952 scopus 로고    scopus 로고
    • A novel protein structure alignment algorithm
    • Zhu J., and Weng Z. A novel protein structure alignment algorithm. Proteins: Struct. Funct. Bioinf. 14 (2005) 417-423
    • (2005) Proteins: Struct. Funct. Bioinf. , vol.14 , pp. 417-423
    • Zhu, J.1    Weng, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.