메뉴 건너뛰기




Volumn 71, Issue 3, 2008, Pages 1387-1399

Remote homology detection of integral membrane proteins using conserved sequence features

Author keywords

Hidden Markov model; Homology detection; Membrane protein; Membrane topology

Indexed keywords

GLOBULAR PROTEIN; MEMBRANE PROTEIN;

EID: 42449160596     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21825     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 3042589552 scopus 로고    scopus 로고
    • Back to basics: Assigning biochemical function in the post-genomic era
    • Cane D. Back to basics: assigning biochemical function in the post-genomic era. Chem Biol 2004;11(6):741-743.
    • (2004) Chem Biol , vol.11 , Issue.6 , pp. 741-743
    • Cane, D.1
  • 2
    • 0346799108 scopus 로고    scopus 로고
    • Prediction of protein function from protein sequence and structure
    • Whisstock J, Lesk A. Prediction of protein function from protein sequence and structure. Q Rev Biophys 2003;36(3):307-340.
    • (2003) Q Rev Biophys , vol.36 , Issue.3 , pp. 307-340
    • Whisstock, J.1    Lesk, A.2
  • 3
    • 0345827718 scopus 로고    scopus 로고
    • Using evolutionary information for the query and target improves fold recognition
    • Wallner B, Fang H, Ohlson T, Frey-Skott J, Elofsson A. Using evolutionary information for the query and target improves fold recognition. Proteins 2004;54(2):342-350.
    • (2004) Proteins , vol.54 , Issue.2 , pp. 342-350
    • Wallner, B.1    Fang, H.2    Ohlson, T.3    Frey-Skott, J.4    Elofsson, A.5
  • 6
    • 0032509105 scopus 로고    scopus 로고
    • Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods
    • Park J, Karplus K, Barrett C, Hughey R, Haussler D, Hubbard T, Chothia C. Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods. J Mol Biol 1998;284(4):1201-1210.
    • (1998) J Mol Biol , vol.284 , Issue.4 , pp. 1201-1210
    • Park, J.1    Karplus, K.2    Barrett, C.3    Hughey, R.4    Haussler, D.5    Hubbard, T.6    Chothia, C.7
  • 7
    • 0033997036 scopus 로고    scopus 로고
    • Comparison of sequence profiles, strategies for structural predictions using sequence information
    • Rychlewski L, Jaroszewski L, Li W, Godzik A. Comparison of sequence profiles, strategies for structural predictions using sequence information. Protein Sci 2000;9(2):232-241.
    • (2000) Protein Sci , vol.9 , Issue.2 , pp. 232-241
    • Rychlewski, L.1    Jaroszewski, L.2    Li, W.3    Godzik, A.4
  • 8
    • 0041886960 scopus 로고    scopus 로고
    • Probabilistic scoring measures for profile-profile comparison yield more accurate short seed alignments
    • Mittelman D, Sadreyev R, Grishin N. Probabilistic scoring measures for profile-profile comparison yield more accurate short seed alignments. Bioinformatics 2003;19(12):1531-1539.
    • (2003) Bioinformatics , vol.19 , Issue.12 , pp. 1531-1539
    • Mittelman, D.1    Sadreyev, R.2    Grishin, N.3
  • 9
    • 4444298729 scopus 로고    scopus 로고
    • Profile-profile methods provide improved fold-recognition: A study of different profile-profile alignment methods
    • Ohlson T, Wallner B, Elofsson A. Profile-profile methods provide improved fold-recognition: a study of different profile-profile alignment methods. Proteins 2004;57(1):188-197.
    • (2004) Proteins , vol.57 , Issue.1 , pp. 188-197
    • Ohlson, T.1    Wallner, B.2    Elofsson, A.3
  • 10
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh A, Larsson B, vonHeijne G, Sonnhammer EL. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 2001;305(3):567-580.
    • (2001) J Mol Biol , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    vonHeijne, G.3    Sonnhammer, E.L.4
  • 11
    • 0030274647 scopus 로고    scopus 로고
    • Genomic sciences and the medicine of tomorrow
    • Drews J. Genomic sciences and the medicine of tomorrow. Nat Biotechnol 1996;14(11):1516-1518.
    • (1996) Nat Biotechnol , vol.14 , Issue.11 , pp. 1516-1518
    • Drews, J.1
  • 12
    • 0034079112 scopus 로고    scopus 로고
    • Selective constraints, amino acid composition, and the rate of protein evolution
    • Tourasse NJ, Li WH. Selective constraints, amino acid composition, and the rate of protein evolution. Mol Biol Evol 2000;17(4):656-664.
    • (2000) Mol Biol Evol , vol.17 , Issue.4 , pp. 656-664
    • Tourasse, N.J.1    Li, W.H.2
  • 13
    • 0029874551 scopus 로고    scopus 로고
    • Protein fold recognition using sequence-derived predictions
    • Fischer D, Eisenberg D. Protein fold recognition using sequence-derived predictions. Protein Sci 1996;5:947-955.
    • (1996) Protein Sci , vol.5 , pp. 947-955
    • Fischer, D.1    Eisenberg, D.2
  • 14
    • 0031564630 scopus 로고    scopus 로고
    • A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence
    • Rice D, Eisenberg D. A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence. J Mol Biol 1997;267:1026-1038.
    • (1997) J Mol Biol , vol.267 , pp. 1026-1038
    • Rice, D.1    Eisenberg, D.2
  • 15
    • 0031577260 scopus 로고    scopus 로고
    • Protein fold recognition by prediction-based threading
    • Rost B, Schneider R, Sander C. Protein fold recognition by prediction-based threading. J Mol Biol 1997;270:471-480.
    • (1997) J Mol Biol , vol.270 , pp. 471-480
    • Rost, B.1    Schneider, R.2    Sander, C.3
  • 16
    • 0033168498 scopus 로고    scopus 로고
    • Hidden markov models that use predicted secondary structures for fold recognition
    • Hargbo J, Elofsson A. Hidden markov models that use predicted secondary structures for fold recognition. Proteins 1999;36(1):68-76.
    • (1999) Proteins , vol.36 , Issue.1 , pp. 68-76
    • Hargbo, J.1    Elofsson, A.2
  • 17
    • 0033670439 scopus 로고    scopus 로고
    • Maxsub: An automated measure to assess the quality of protein structure predictions
    • Siew N, Elofsson A, Rychlewski L, Fischer D. Maxsub: An automated measure to assess the quality of protein structure predictions. Bionformatics 2000;16:776-785.
    • (2000) Bionformatics , vol.16 , pp. 776-785
    • Siew, N.1    Elofsson, A.2    Rychlewski, L.3    Fischer, D.4
  • 18
    • 0043130635 scopus 로고    scopus 로고
    • Profile-profile alignment: A powerful tool for protein structure prediction
    • Altman RB, Dunker AK, Hunter Jung TAL, Klein TE, editors
    • vonOhsen N, Sommer I, Zimmer R. Profile-profile alignment: a powerful tool for protein structure prediction. In: Altman RB, Dunker AK, Hunter Jung TAL, Klein TE, editors, Pacific Symposium on Biocomputing. 2003:252-263.
    • (2003) Pacific Symposium on Biocomputing , pp. 252-263
    • vonOhsen, N.1    Sommer, I.2    Zimmer, R.3
  • 19
    • 0036307493 scopus 로고    scopus 로고
    • Within the twilight zone: A sensitive profile-profile comparison tool based on information theory
    • Yona G, Levitt M. Within the twilight zone: a sensitive profile-profile comparison tool based on information theory. J Mol Biol 2002;315(5):1257-1275.
    • (2002) J Mol Biol , vol.315 , Issue.5 , pp. 1257-1275
    • Yona, G.1    Levitt, M.2
  • 20
    • 0141634362 scopus 로고    scopus 로고
    • Profile-profile comparisons by COMPASS predict intricate homologies between protein families
    • Sadreyev R, Baker D, Grishin N. Profile-profile comparisons by COMPASS predict intricate homologies between protein families. Protein Sci 2003;12(10):2262-2272.
    • (2003) Protein Sci , vol.12 , Issue.10 , pp. 2262-2272
    • Sadreyev, R.1    Baker, D.2    Grishin, N.3
  • 21
    • 0042594474 scopus 로고    scopus 로고
    • SATCHMO: Sequence alignment and tree construction using hidden Markov models
    • Edgar R, Sjolander K. SATCHMO: sequence alignment and tree construction using hidden Markov models. Bioinformatics 2003;19: 1404-1411.
    • (2003) Bioinformatics , vol.19 , pp. 1404-1411
    • Edgar, R.1    Sjolander, K.2
  • 22
    • 0037433034 scopus 로고    scopus 로고
    • PCMA: Fast and accurate multiple sequence alignment based on profile consistency
    • Pei J, Sadreyev R, Grishin N. PCMA: fast and accurate multiple sequence alignment based on profile consistency. Bioinformatics 2003;19(3):427-428.
    • (2003) Bioinformatics , vol.19 , Issue.3 , pp. 427-428
    • Pei, J.1    Sadreyev, R.2    Grishin, N.3
  • 23
    • 0033670313 scopus 로고    scopus 로고
    • PHAT: A transmembrane-specific substitution matrix. Predicted hydrophobic and transmembrane
    • Ng PC, Henikoff JG, Henikoff S. PHAT: a transmembrane-specific substitution matrix. Predicted hydrophobic and transmembrane. Bioinformatics 2000;16(9):760-766.
    • (2000) Bioinformatics , vol.16 , Issue.9 , pp. 760-766
    • Ng, P.C.1    Henikoff, J.G.2    Henikoff, S.3
  • 24
    • 0036177476 scopus 로고    scopus 로고
    • Improved detection of homologous membrane proteins by inclusion of information from topology predictions
    • Hedman M, Deloof H, Von Heijne G, Elofsson A. Improved detection of homologous membrane proteins by inclusion of information from topology predictions. Protein Sci 2002;11(3):652-658.
    • (2002) Protein Sci , vol.11 , Issue.3 , pp. 652-658
    • Hedman, M.1    Deloof, H.2    Von Heijne, G.3    Elofsson, A.4
  • 25
    • 33745714411 scopus 로고    scopus 로고
    • On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins
    • Forrest L, Tang C, Honig B. On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins. Biophys J 2006;91:508-517.
    • (2006) Biophys J , vol.91 , pp. 508-517
    • Forrest, L.1    Tang, C.2    Honig, B.3
  • 26
    • 0029887381 scopus 로고    scopus 로고
    • Hidden Markov models for sequence analysis: Extension and analysis of the basic method
    • Hughey R, Krogh A. Hidden Markov models for sequence analysis: extension and analysis of the basic method. Comput Appl Biosci 1996;12(2):95-107.
    • (1996) Comput Appl Biosci , vol.12 , Issue.2 , pp. 95-107
    • Hughey, R.1    Krogh, A.2
  • 27
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR. Profile hidden Markov models. Bioinformatics 1998; 14(9):755-763.
    • (1998) Bioinformatics , vol.14 , Issue.9 , pp. 755-763
    • Eddy, S.R.1
  • 28
    • 23144452044 scopus 로고    scopus 로고
    • Soding J, Biegert A, Lupas AN. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 2005;33(Web Server issue):244-248.
    • Soding J, Biegert A, Lupas AN. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 2005;33(Web Server issue):244-248.
  • 29
    • 0242362161 scopus 로고    scopus 로고
    • Combining local-structure, fold-recognition, and new fold methods for protein structure prediction
    • Karplus K, Karchin R, Draper J, Casper J, Mandel-Gutfreund Y, Diekhans M, Hughey R. Combining local-structure, fold-recognition, and new fold methods for protein structure prediction. Proteins 2003;53(Suppl 6):491-496.
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 491-496
    • Karplus, K.1    Karchin, R.2    Draper, J.3    Casper, J.4    Mandel-Gutfreund, Y.5    Diekhans, M.6    Hughey, R.7
  • 30
    • 13444273448 scopus 로고    scopus 로고
    • Bairoch A, Apweiler R, Wu CH, Barker WC, Boeckmann B, Ferro S, Gasteiger E, Huang H, Lopez R, Magrane M, Martin MJ, Natale DA, O'Donovan C, Redaschi N, Yeh L-SL. The Universal Protein Resource (UniProt). Nucleic Acids Res 2005;33(Database issue): 154-159.
    • Bairoch A, Apweiler R, Wu CH, Barker WC, Boeckmann B, Ferro S, Gasteiger E, Huang H, Lopez R, Magrane M, Martin MJ, Natale DA, O'Donovan C, Redaschi N, Yeh L-SL. The Universal Protein Resource (UniProt). Nucleic Acids Res 2005;33(Database issue): 154-159.
  • 31
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman DM, Steitz TA, Goldman A. Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu Rev Biophys Biophys Chem 1986;15:321-353.
    • (1986) Annu Rev Biophys Biophys Chem , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 32
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • vonHeijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J Mol Biol 1992;225(2): 487-494.
    • (1992) J Mol Biol , vol.225 , Issue.2 , pp. 487-494
    • vonHeijne, G.1
  • 34
    • 3042579686 scopus 로고    scopus 로고
    • Best α-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information
    • Viklund H, Elofsson A. Best α-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information. Protein Sci 2004;13(7):1908-1917.
    • (2004) Protein Sci , vol.13 , Issue.7 , pp. 1908-1917
    • Viklund, H.1    Elofsson, A.2
  • 35
    • 0024610919 scopus 로고
    • A tutorial on hidden markov models and selected applications in speech recognition
    • Rabiner LR. A tutorial on hidden markov models and selected applications in speech recognition. Proceedings of the IEEE 1989;77(2):257-285.
    • (1989) Proceedings of the IEEE , vol.77 , Issue.2 , pp. 257-285
    • Rabiner, L.R.1
  • 36
    • 0037083541 scopus 로고    scopus 로고
    • A study on protein sequence alignment quality
    • Elofsson A. A study on protein sequence alignment quality. Proteins 2002;46(3):330-339.
    • (2002) Proteins , vol.46 , Issue.3 , pp. 330-339
    • Elofsson, A.1
  • 37
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999;292(2):195-202.
    • (1999) J Mol Biol , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.1
  • 39
    • 33745634395 scopus 로고    scopus 로고
    • Li W, Godzik A. Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics 2006;22(13):1658-1659.
    • Li W, Godzik A. Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics 2006;22(13):1658-1659.
  • 40
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell T. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993;234(3):779-815.
    • (1993) J Mol Biol , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.2
  • 42
    • 10344232638 scopus 로고    scopus 로고
    • Scoring function for automated assessment of protein structure template quality
    • Zhang Y, Skolnick J. Scoring function for automated assessment of protein structure template quality. Proteins 2004;57(4):702-710.
    • (2004) Proteins , vol.57 , Issue.4 , pp. 702-710
    • Zhang, Y.1    Skolnick, J.2
  • 43
    • 33744490360 scopus 로고    scopus 로고
    • Positioning of proteins in membranes: A computational approach
    • Lomize A, Pogozheva I, Lomize M, Mosberg H. Positioning of proteins in membranes: a computational approach. Protein Sci 2006;15(6):1318-1333.
    • (2006) Protein Sci , vol.15 , Issue.6 , pp. 1318-1333
    • Lomize, A.1    Pogozheva, I.2    Lomize, M.3    Mosberg, H.4
  • 44
    • 0031938039 scopus 로고    scopus 로고
    • Comprehensive assessment of automatic structural alignment against a manual standard, the scop classification of proteins
    • Gerstein M, Levitt M. Comprehensive assessment of automatic structural alignment against a manual standard, the scop classification of proteins. Protein Sci 1998;7(2):445-456.
    • (1998) Protein Sci , vol.7 , Issue.2 , pp. 445-456
    • Gerstein, M.1    Levitt, M.2
  • 46
    • 33644509247 scopus 로고    scopus 로고
    • A general model of G protein-coupled receptor sequences and its application to detect remote homologs
    • Wistrand M, Kall L, Sonnhammer ELL. A general model of G protein-coupled receptor sequences and its application to detect remote homologs. Protein Sci 2006;15(3):509-521.
    • (2006) Protein Sci , vol.15 , Issue.3 , pp. 509-521
    • Wistrand, M.1    Kall, L.2    Sonnhammer, E.L.L.3
  • 47
    • 0035283313 scopus 로고    scopus 로고
    • Robust classification for imprecise environments
    • Provost F, Fawcett T. Robust classification for imprecise environments. Mach Learn 2001;42(3):203-231.
    • (2001) Mach Learn , vol.42 , Issue.3 , pp. 203-231
    • Provost, F.1    Fawcett, T.2
  • 48
    • 29144483361 scopus 로고    scopus 로고
    • An HMM posterior decoder for sequence feature prediction that includes homology information
    • Kall L, Krogh A, Sonnhammer ELL. An HMM posterior decoder for sequence feature prediction that includes homology information. Bioinformatics 2005;21(Suppl 1):251-257.
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 1 , pp. 251-257
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.