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Volumn 13, Issue SUPPL.7, 2012, Pages

Relationship between amino acid properties and functional parameters in olfactory receptors and discrimination of mutants with enhanced specificity

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTATIONAL BIOLOGY; CONFORMATIONAL PROPERTIES; EFFECTIVE CONCENTRATION; FUNCTIONAL PARAMETERS; HUMAN OLFACTORY RECEPTORS; IMMEDIATE ENVIRONMENT; MACHINE LEARNING METHODS; MULTIPLE REGRESSION TECHNIQUES;

EID: 84872788665     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-13-S7-S1     Document Type: Article
Times cited : (10)

References (49)
  • 1
    • 0032498150 scopus 로고    scopus 로고
    • Functional expression of a mammalian odorant receptor
    • 10.1126/science.279.5348.237, 9422698
    • Zhao H, Ivic L, Otaki JM, Hashimoto M, Mikoshiba K, Firestein S. Functional expression of a mammalian odorant receptor. Science 1998, 279:237-242. 10.1126/science.279.5348.237, 9422698.
    • (1998) Science , vol.279 , pp. 237-242
    • Zhao, H.1    Ivic, L.2    Otaki, J.M.3    Hashimoto, M.4    Mikoshiba, K.5    Firestein, S.6
  • 2
    • 55849127127 scopus 로고    scopus 로고
    • Amino acids involved in conformational dynamics and G protein coupling of an odorant receptor: targeting gain-of-function mutation
    • 10.1111/j.1471-4159.2008.05693.x, 18803693
    • Kato A, Katada S, Touhara K. Amino acids involved in conformational dynamics and G protein coupling of an odorant receptor: targeting gain-of-function mutation. J Neurochem 2008, 107:1261-1270. 10.1111/j.1471-4159.2008.05693.x, 18803693.
    • (2008) J Neurochem , vol.107 , pp. 1261-1270
    • Kato, A.1    Katada, S.2    Touhara, K.3
  • 3
    • 0029939849 scopus 로고    scopus 로고
    • Information coding in the vertebrate olfactory system
    • 10.1146/annurev.ne.19.030196.002505, 8833453
    • Buck LB. Information coding in the vertebrate olfactory system. Annu Rev Neurosci 1996, 19:517-544. 10.1146/annurev.ne.19.030196.002505, 8833453.
    • (1996) Annu Rev Neurosci , vol.19 , pp. 517-544
    • Buck, L.B.1
  • 4
    • 1842464122 scopus 로고    scopus 로고
    • Genes and ligands for odorant, vomeronasal and taste receptors
    • 10.1038/nrn1365, 15034552
    • Mombaerts P. Genes and ligands for odorant, vomeronasal and taste receptors. Nat Rev Neurosci 2004, 5:263-278. 10.1038/nrn1365, 15034552.
    • (2004) Nat Rev Neurosci , vol.5 , pp. 263-278
    • Mombaerts, P.1
  • 5
    • 77950835759 scopus 로고    scopus 로고
    • Behavioural neurobiology: The treacherous scent of a human
    • 10.1038/464037a, 20203594
    • Leal WS. Behavioural neurobiology: The treacherous scent of a human. Nature 2010, 464:37-38. 10.1038/464037a, 20203594.
    • (2010) Nature , vol.464 , pp. 37-38
    • Leal, W.S.1
  • 6
    • 77950839118 scopus 로고    scopus 로고
    • Odorant reception in the malaria mosquito Anopheles gambiae
    • 10.1038/nature08834, 2833235, 20130575
    • Carey AF, Wang G, Su CY, Zwiebel LJ, Carlson JR. Odorant reception in the malaria mosquito Anopheles gambiae. Nature 2010, 464:66-71. 10.1038/nature08834, 2833235, 20130575.
    • (2010) Nature , vol.464 , pp. 66-71
    • Carey, A.F.1    Wang, G.2    Su, C.Y.3    Zwiebel, L.J.4    Carlson, J.R.5
  • 7
    • 79952990724 scopus 로고    scopus 로고
    • Mechanisms of chloride uptake in frog olfactory receptor neurons
    • 10.1007/s00359-010-0618-1, 21253748
    • Jaén C, Ozdener MH, Reisert J. Mechanisms of chloride uptake in frog olfactory receptor neurons. J Comp Physiol A Neuroethol Sens Neural Behav Physiol 2011, 197:339-349. 10.1007/s00359-010-0618-1, 21253748.
    • (2011) J Comp Physiol A Neuroethol Sens Neural Behav Physiol , vol.197 , pp. 339-349
    • Jaén, C.1    Ozdener, M.H.2    Reisert, J.3
  • 8
    • 78651359215 scopus 로고    scopus 로고
    • Autonomic modulation of olfactory signaling
    • 10.1126/scisignal.2001672, 21224443
    • Hall RA. Autonomic modulation of olfactory signaling. Sci Signal 2011, 4:pe1. 10.1126/scisignal.2001672, 21224443.
    • (2011) Sci Signal , vol.4
    • Hall, R.A.1
  • 9
    • 78650937569 scopus 로고    scopus 로고
    • Functional architecture of olfactory ionotropic glutamate receptors
    • 10.1016/j.neuron.2010.11.042, 3050028, 21220098
    • Abuin L, Bargeton B, Ulbrich MH, Isacoff EY, Kellenberger S, Benton R. Functional architecture of olfactory ionotropic glutamate receptors. Neuron 2011, 69:44-60. 10.1016/j.neuron.2010.11.042, 3050028, 21220098.
    • (2011) Neuron , vol.69 , pp. 44-60
    • Abuin, L.1    Bargeton, B.2    Ulbrich, M.H.3    Isacoff, E.Y.4    Kellenberger, S.5    Benton, R.6
  • 10
    • 79551671741 scopus 로고    scopus 로고
    • Unitary response of mouse olfactory receptor neurons
    • 10.1073/pnas.1017983108, 3021043, 21187398
    • Ben-Chaim Y, Cheng MM, Yau KW. Unitary response of mouse olfactory receptor neurons. Proc Natl Acad Sci USA 2011, 108:822-827. 10.1073/pnas.1017983108, 3021043, 21187398.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 822-827
    • Ben-Chaim, Y.1    Cheng, M.M.2    Yau, K.W.3
  • 11
    • 79952084703 scopus 로고    scopus 로고
    • The mouse eugenol odorant receptor: structural and functional plasticity of a broadly tuned odorant binding pocket
    • 10.1021/bi1017396, 21142015
    • Baud O, Etter S, Spreafico M, Bordoli L, Schwede T, Vogel H, Pick H. The mouse eugenol odorant receptor: structural and functional plasticity of a broadly tuned odorant binding pocket. Biochemistry 2011, 50:843-853. 10.1021/bi1017396, 21142015.
    • (2011) Biochemistry , vol.50 , pp. 843-853
    • Baud, O.1    Etter, S.2    Spreafico, M.3    Bordoli, L.4    Schwede, T.5    Vogel, H.6    Pick, H.7
  • 13
    • 34547573955 scopus 로고    scopus 로고
    • Protein-protein interaction hotspots carved into sequences
    • 10.1371/journal.pcbi.0030119, 1914369, 17630824
    • Yanay O, Rost B. Protein-protein interaction hotspots carved into sequences. PLoS Comput Biol 2007, 3:e119. 10.1371/journal.pcbi.0030119, 1914369, 17630824.
    • (2007) PLoS Comput Biol , vol.3
    • Yanay, O.1    Rost, B.2
  • 14
    • 77958498250 scopus 로고    scopus 로고
    • Using manifold embedding for assessing and predicting protein interactions from high-throughput experimental data
    • 10.1093/bioinformatics/btq510, 3025743, 20817744
    • You ZH, Lei YK, Huang DS, Zhou X. Using manifold embedding for assessing and predicting protein interactions from high-throughput experimental data. Bioinformatics 2010, 26(21):2744-2751. 10.1093/bioinformatics/btq510, 3025743, 20817744.
    • (2010) Bioinformatics , vol.26 , Issue.21 , pp. 2744-2751
    • You, Z.H.1    Lei, Y.K.2    Huang, D.S.3    Zhou, X.4
  • 15
    • 77950651626 scopus 로고    scopus 로고
    • APIS: accurate prediction of hot spots in protein interfaces by combining protrusion index with solvent accessibility
    • 10.1186/1471-2105-11-174, 2874803, 20377884
    • Xia JF, Zhao XM, Song J, Huang DS. APIS: accurate prediction of hot spots in protein interfaces by combining protrusion index with solvent accessibility. BMC Bioinformatics 2010, 11:174. 10.1186/1471-2105-11-174, 2874803, 20377884.
    • (2010) BMC Bioinformatics , vol.11 , pp. 174
    • Xia, J.F.1    Zhao, X.M.2    Song, J.3    Huang, D.S.4
  • 16
    • 78449281410 scopus 로고    scopus 로고
    • Predicting protein-protein interactions from protein sequences using meta predictor
    • 10.1007/s00726-010-0588-1, 20386937
    • Xia JF, Zhao XM, Huang DS. Predicting protein-protein interactions from protein sequences using meta predictor. Amino Acids 2010, 39:1595-1599. 10.1007/s00726-010-0588-1, 20386937.
    • (2010) Amino Acids , vol.39 , pp. 1595-1599
    • Xia, J.F.1    Zhao, X.M.2    Huang, D.S.3
  • 17
    • 72949113228 scopus 로고    scopus 로고
    • Energy based approach for understanding the recognition mechanism in protein-protein complexes
    • 10.1039/b904161n, 19593470
    • Gromiha MM, Yokota K, Fukui K. Energy based approach for understanding the recognition mechanism in protein-protein complexes. Mol Biosyst 2009, 5(12):1779-1786. 10.1039/b904161n, 19593470.
    • (2009) Mol Biosyst , vol.5 , Issue.12 , pp. 1779-1786
    • Gromiha, M.M.1    Yokota, K.2    Fukui, K.3
  • 18
    • 58149177176 scopus 로고    scopus 로고
    • TMFunction: database for functional residues in membrane proteins
    • 10.1093/nar/gkn672, 2686444, 18842639
    • Gromiha MM, Yabuki Y, Suresh MX, Thangakani AM, Suwa M, Fukui K. TMFunction: database for functional residues in membrane proteins. Nucleic Acids Res 2009, 37:D201-D204. 10.1093/nar/gkn672, 2686444, 18842639.
    • (2009) Nucleic Acids Res , vol.37
    • Gromiha, M.M.1    Yabuki, Y.2    Suresh, M.X.3    Thangakani, A.M.4    Suwa, M.5    Fukui, K.6
  • 19
    • 0142149078 scopus 로고    scopus 로고
    • Molecular similarities in the ligand binding pockets of an odorant receptor and the metabotropic glutamate receptors
    • 10.1074/jbc.M307120200, 12912984
    • Kuang D, Yao Y, Wang M, Pattabiraman N, Kotra LP, Hampson DR. Molecular similarities in the ligand binding pockets of an odorant receptor and the metabotropic glutamate receptors. J Biol Chem 2003, 278:42551-42559. 10.1074/jbc.M307120200, 12912984.
    • (2003) J Biol Chem , vol.278 , pp. 42551-42559
    • Kuang, D.1    Yao, Y.2    Wang, M.3    Pattabiraman, N.4    Kotra, L.P.5    Hampson, D.R.6
  • 20
    • 8544260348 scopus 로고    scopus 로고
    • Molecular determinants of ligand selectivity in a vertebrate odorant receptor
    • 10.1523/JNEUROSCI.3117-04.2004, 15537883
    • Luu P, Acher F, Bertrand HO, Fan J, Ngai J. Molecular determinants of ligand selectivity in a vertebrate odorant receptor. J Neurosci 2004, 24:10128-10137. 10.1523/JNEUROSCI.3117-04.2004, 15537883.
    • (2004) J Neurosci , vol.24 , pp. 10128-10137
    • Luu, P.1    Acher, F.2    Bertrand, H.O.3    Fan, J.4    Ngai, J.5
  • 21
    • 14044270215 scopus 로고    scopus 로고
    • Structural basis for a broad but selective ligand spectrum of a mouse olfactory receptor: mapping the odorant-binding site
    • 10.1523/JNEUROSCI.4723-04.2005, 15716417
    • Katada S, Hirokawa T, Oka Y, Suwa M, Touhara K. Structural basis for a broad but selective ligand spectrum of a mouse olfactory receptor: mapping the odorant-binding site. J Neurosci 2005, 25:1806-1815. 10.1523/JNEUROSCI.4723-04.2005, 15716417.
    • (2005) J Neurosci , vol.25 , pp. 1806-1815
    • Katada, S.1    Hirokawa, T.2    Oka, Y.3    Suwa, M.4    Touhara, K.5
  • 22
    • 34547881027 scopus 로고    scopus 로고
    • Structural determinants of odorant recognition by the human olfactory receptors OR1A1 and OR1A2
    • 10.1016/j.jsb.2007.04.013, 17601748
    • Schmiedeberg K, Shirokova E, Weber HP, Schilling B, Meyerhof W, Krautwurst D. Structural determinants of odorant recognition by the human olfactory receptors OR1A1 and OR1A2. J Struct Biol 2007, 159:400-412. 10.1016/j.jsb.2007.04.013, 17601748.
    • (2007) J Struct Biol , vol.159 , pp. 400-412
    • Schmiedeberg, K.1    Shirokova, E.2    Weber, H.P.3    Schilling, B.4    Meyerhof, W.5    Krautwurst, D.6
  • 24
    • 0346102906 scopus 로고    scopus 로고
    • Prediction of the odorant binding site of olfactory receptor proteins by human-mouse comparisons
    • 10.1110/ps.03296404, 2286516, 14691239
    • Man O, Gilad Y, Lancet D. Prediction of the odorant binding site of olfactory receptor proteins by human-mouse comparisons. Protein Sci 2004, 13:240-254. 10.1110/ps.03296404, 2286516, 14691239.
    • (2004) Protein Sci , vol.13 , pp. 240-254
    • Man, O.1    Gilad, Y.2    Lancet, D.3
  • 25
    • 14644389485 scopus 로고    scopus 로고
    • The olfactory receptor universe - from whole genome analysis to structure and evolution
    • Olender T, Feldmesser E, Atarot T, Eisenstein M, Lancet D. The olfactory receptor universe - from whole genome analysis to structure and evolution. Genet Mol Res 2004, 3:545-553.
    • (2004) Genet Mol Res , vol.3 , pp. 545-553
    • Olender, T.1    Feldmesser, E.2    Atarot, T.3    Eisenstein, M.4    Lancet, D.5
  • 26
    • 0029922443 scopus 로고    scopus 로고
    • Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins
    • 10.1093/protein/9.1.27, 9053899
    • Tomii K, Kanehisa M. Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins. Protein Eng 1996, 9:27-36. 10.1093/protein/9.1.27, 9053899.
    • (1996) Protein Eng , vol.9 , pp. 27-36
    • Tomii, K.1    Kanehisa, M.2
  • 27
    • 0032715527 scopus 로고    scopus 로고
    • Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins
    • 10.1016/S0301-4622(99)00103-9, 10584295
    • Gromiha MM, Oobatake M, Sarai A. Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins. Biophys Chem 1999, 82:51-67. 10.1016/S0301-4622(99)00103-9, 10584295.
    • (1999) Biophys Chem , vol.82 , pp. 51-67
    • Gromiha, M.M.1    Oobatake, M.2    Sarai, A.3
  • 28
    • 0033747515 scopus 로고    scopus 로고
    • Importance of surrounding residues for protein stability of partially buried mutations
    • 10.1080/07391102.2000.10506666, 11089649
    • Gromiha MM, Oobatake M, Kono H, Uedaira H, Sarai A. Importance of surrounding residues for protein stability of partially buried mutations. J Biomol Struct Dyn 2000, 18:281-295. 10.1080/07391102.2000.10506666, 11089649.
    • (2000) J Biomol Struct Dyn , vol.18 , pp. 281-295
    • Gromiha, M.M.1    Oobatake, M.2    Kono, H.3    Uedaira, H.4    Sarai, A.5
  • 29
    • 0032773941 scopus 로고    scopus 로고
    • Role of structural and sequence information in the prediction of protein stability changes: comparison between buried and partially buried mutations
    • 10.1093/protein/12.7.549, 10436080
    • Gromiha MM, Oobatake M, Kono H, Uedaira H, Sarai A. Role of structural and sequence information in the prediction of protein stability changes: comparison between buried and partially buried mutations. Protein Eng 1999, 12:549-555. 10.1093/protein/12.7.549, 10436080.
    • (1999) Protein Eng , vol.12 , pp. 549-555
    • Gromiha, M.M.1    Oobatake, M.2    Kono, H.3    Uedaira, H.4    Sarai, A.5
  • 30
    • 0037189911 scopus 로고    scopus 로고
    • Important amino acid properties for determining the transition state structures of two-state protein mutants
    • 10.1016/S0014-5793(02)03122-8, 12208519
    • Gromiha MM, Selvaraj S. Important amino acid properties for determining the transition state structures of two-state protein mutants. FEBS Lett 2002, 526:129-134. 10.1016/S0014-5793(02)03122-8, 12208519.
    • (2002) FEBS Lett , vol.526 , pp. 129-134
    • Gromiha, M.M.1    Selvaraj, S.2
  • 31
    • 69949115157 scopus 로고    scopus 로고
    • Reliable prediction of protein thermostability change upon double mutation from amino acid sequence
    • 10.1093/bioinformatics/btp370, 19535532
    • Huang LT, Gromiha MM. Reliable prediction of protein thermostability change upon double mutation from amino acid sequence. Bioinformatics 2009, 25:2181-2187. 10.1093/bioinformatics/btp370, 19535532.
    • (2009) Bioinformatics , vol.25 , pp. 2181-2187
    • Huang, L.T.1    Gromiha, M.M.2
  • 32
    • 77955951200 scopus 로고    scopus 로고
    • First insight into the prediction of protein folding rate change upon point mutation
    • 10.1093/bioinformatics/btq350, 20616385
    • Huang LT, Gromiha MM. First insight into the prediction of protein folding rate change upon point mutation. Bioinformatics 2010, 26:2121-2127. 10.1093/bioinformatics/btq350, 20616385.
    • (2010) Bioinformatics , vol.26 , pp. 2121-2127
    • Huang, L.T.1    Gromiha, M.M.2
  • 33
    • 77951225212 scopus 로고    scopus 로고
    • Classification of transporters using efficient radial basis function networks with position-specific scoring matrices and biochemical properties
    • Ou YY, Chen SA, Gromiha MM. Classification of transporters using efficient radial basis function networks with position-specific scoring matrices and biochemical properties. Proteins 2010, 78:1789-1797.
    • (2010) Proteins , vol.78 , pp. 1789-1797
    • Ou, Y.Y.1    Chen, S.A.2    Gromiha, M.M.3
  • 34
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • 10.1093/bioinformatics/17.9.849, 11590105
    • Tusndy GE, Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics 2001, 17:849-850. 10.1093/bioinformatics/17.9.849, 11590105.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusndy, G.E.1    Simon, I.2
  • 35
    • 39149144057 scopus 로고    scopus 로고
    • PRALINETM: a strategy for improved multiple alignment of transmembrane proteins
    • Pirovano W, Feenstra KA, Heringa J. PRALINETM: a strategy for improved multiple alignment of transmembrane proteins. Bioinformatics 2008, 24(2):492-497.
    • (2008) Bioinformatics , vol.24 , Issue.2 , pp. 492-497
    • Pirovano, W.1    Feenstra, K.A.2    Heringa, J.3
  • 36
    • 65449188232 scopus 로고    scopus 로고
    • Jalview version 2--a multiple sequence alignment editor and analysis workbench
    • doi: 10.1093/bioinformatics/btp033, 10.1093/bioinformatics/btp033, 2672624, 19151095
    • Waterhouse AM, Procter JB, Martin DMA, Clamp M, Barton GJ. Jalview version 2--a multiple sequence alignment editor and analysis workbench. Bioinformatics 2009, 25:1189-1191. doi: 10.1093/bioinformatics/btp033, 10.1093/bioinformatics/btp033, 2672624, 19151095.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.A.3    Clamp, M.4    Barton, G.J.5
  • 37
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • 10.1006/jmbi.1993.1626, 8254673
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993, 234:779-815. 10.1006/jmbi.1993.1626, 8254673.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 38
  • 39
    • 1842464687 scopus 로고    scopus 로고
    • Inter-residue interactions in protein folding and stability
    • 10.1016/j.pbiomolbio.2003.09.003, 15288760
    • Gromiha MM, Selvaraj S. Inter-residue interactions in protein folding and stability. Prog Biophys Mol Biol 2004, 86:235-277. 10.1016/j.pbiomolbio.2003.09.003, 15288760.
    • (2004) Prog Biophys Mol Biol , vol.86 , pp. 235-277
    • Gromiha, M.M.1    Selvaraj, S.2
  • 40
    • 77958510302 scopus 로고    scopus 로고
    • Influence of long-range contacts and surrounding residues on the transition state structures of proteins
    • 10.1016/j.ab.2010.08.029, 20807494
    • Gromiha MM. Influence of long-range contacts and surrounding residues on the transition state structures of proteins. Anal Biochem 2011, 408:32-36. 10.1016/j.ab.2010.08.029, 20807494.
    • (2011) Anal Biochem , vol.408 , pp. 32-36
    • Gromiha, M.M.1
  • 43
    • 33646780174 scopus 로고    scopus 로고
    • Discrimination of outer membrane proteins using machine learning algorithms
    • 10.1002/prot.20929, 16493651
    • Gromiha MM, Suwa M. Discrimination of outer membrane proteins using machine learning algorithms. Proteins 2006, 63:1031-1037. 10.1002/prot.20929, 16493651.
    • (2006) Proteins , vol.63 , pp. 1031-1037
    • Gromiha, M.M.1    Suwa, M.2
  • 44
    • 41049110433 scopus 로고    scopus 로고
    • Functional discrimination of membrane proteins using machine learning techniques
    • 10.1186/1471-2105-9-135, 2375119, 18312695
    • Gromiha MM, Yabuki Y. Functional discrimination of membrane proteins using machine learning techniques. BMC Bioinformatics 2008, 9:135. 10.1186/1471-2105-9-135, 2375119, 18312695.
    • (2008) BMC Bioinformatics , vol.9 , pp. 135
    • Gromiha, M.M.1    Yabuki, Y.2
  • 45
    • 33748489925 scopus 로고    scopus 로고
    • Influence of amino acid properties for discriminating outer membrane proteins at better accuracy
    • Gromiha MM, Suwa M. Influence of amino acid properties for discriminating outer membrane proteins at better accuracy. Biochim Biophys Acta 2006, 1764:1493-1497.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1493-1497
    • Gromiha, M.M.1    Suwa, M.2
  • 46
    • 84855676756 scopus 로고    scopus 로고
    • Structure-function relationship in olfactory receptors
    • Gromiha MM, Sowdhamini R, Fukui K. Structure-function relationship in olfactory receptors. Lect Notes Bioinf 2011, 6840:618-623.
    • (2011) Lect Notes Bioinf , vol.6840 , pp. 618-623
    • Gromiha, M.M.1    Sowdhamini, R.2    Fukui, K.3
  • 47
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility
    • 10.1016/0022-2836(71)90324-X, 5551392
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971, 55(3):379-400. 10.1016/0022-2836(71)90324-X, 5551392.
    • (1971) J Mol Biol , vol.55 , Issue.3 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 48
    • 0025104478 scopus 로고
    • Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction
    • 10.1098/rspb.1990.0077, 1978340
    • Overington J, Johnson MS, Sali A, Blundell TL. Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction. Proc Biol Sci 1990, 241:132-145. 10.1098/rspb.1990.0077, 1978340.
    • (1990) Proc Biol Sci , vol.241 , pp. 132-145
    • Overington, J.1    Johnson, M.S.2    Sali, A.3    Blundell, T.L.4
  • 49
    • 0031714858 scopus 로고    scopus 로고
    • JOY: protein sequence-structure representation and analysis
    • 10.1093/bioinformatics/14.7.617, 9730927
    • Mizuguchi K, Deane CM, Blundell TL, Johnson MS, Overington JP. JOY: protein sequence-structure representation and analysis. Bioinformatics 1998, 14:617-623. 10.1093/bioinformatics/14.7.617, 9730927.
    • (1998) Bioinformatics , vol.14 , pp. 617-623
    • Mizuguchi, K.1    Deane, C.M.2    Blundell, T.L.3    Johnson, M.S.4    Overington, J.P.5


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