메뉴 건너뛰기




Volumn 40, Issue 3, 2011, Pages 991-1002

Accurate prediction of the burial status of transmembrane residues of α-helix membrane protein by incorporating the structural and physicochemical features

Author keywords

Burial status of transmembrane residues; Least squares support vector machine (LS SVM); Recursive feature elimination (RFE)

Indexed keywords

MEMBRANE PROTEIN;

EID: 79954436123     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-010-0727-8     Document Type: Article
Times cited : (6)

References (70)
  • 1
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • DOI 10.1126/science.1088196
    • J Abramson I Smirnova V Kasho G Verner HR Kaback S Iwata 2003 Structure and mechanism of the lactose permease of Escherichia coli Science 301 610 615 1:CAS:528:DC%2BD3sXlvVKns7k%3D 10.1126/science.1088196 12893935 (Pubitemid 36927939)
    • (2003) Science , vol.301 , Issue.5633 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 2
    • 33747184794 scopus 로고    scopus 로고
    • Prediction of transmembrane helix orientation in polytopic membrane proteins
    • DOI 10.1186/1472-6807-6-13
    • L Adamian J Liang 2006 Prediction of transmembrane helix orientation in polytopic membrane proteins BMC Struct Biol 6 13 10.1186/1472-6807-6-13 16792816 (Pubitemid 44232099)
    • (2006) BMC Structural Biology , vol.6 , pp. 13
    • Adamian, L.1    Liang, J.2
  • 3
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • SF Altschul TL Madden AA Schaffer J Zhang Z Zhang W Miller DJ Lipman 1997 Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Nucleic Acids Res 25 3389 3402 1:CAS:528:DyaK2sXlvFyhu7w%3D 10.1093/nar/25.17.3389 9254694 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 6
    • 4444382786 scopus 로고    scopus 로고
    • A knowledge-based scale for the analysis and prediction of buried and exposed faces of transmembrane domain proteins
    • DOI 10.1093/bioinformatics/bth143
    • T Beuming H Weinstein 2004 A knowledge-based scale for the analysis and prediction of buried and exposed faces of transmembrane domain proteins Bioinformatics 20 1822 1835 1:CAS:528:DC%2BD2cXntFahsbo%3D 10.1093/ bioinformatics/bth143 14988128 (Pubitemid 39199046)
    • (2004) Bioinformatics , vol.20 , Issue.12 , pp. 1822-1835
    • Beuming, T.1    Weinstein, H.2
  • 7
    • 85004911383 scopus 로고
    • Positional flexibilities of amino acid residues in globular proteins
    • 1:CAS:528:DyaL1MXitVSrtg%3D%3D 10.1111/j.1399-3011.1988.tb01258.x
    • R Bhaskaran PK Ponnuswamy 1988 Positional flexibilities of amino acid residues in globular proteins J Peptide Protein Res 32 241 255 1:CAS:528:DyaL1MXitVSrtg%3D%3D 10.1111/j.1399-3011.1988.tb01258.x
    • (1988) J Peptide Protein Res , vol.32 , pp. 241-255
    • Bhaskaran, R.1    Ponnuswamy, P.K.2
  • 8
    • 0014117822 scopus 로고
    • On the average hydrophobicity of proteins and the relation between it and protein structure
    • 1:CAS:528:DyaF1cXitFc%3D 10.1016/0022-5193(67)90004-5 6048539
    • CC Bigelow 1967 On the average hydrophobicity of proteins and the relation between it and protein structure J Theor Biol 16 187 211 1:CAS:528:DyaF1cXitFc%3D 10.1016/0022-5193(67)90004-5 6048539
    • (1967) J Theor Biol , vol.16 , pp. 187-211
    • Bigelow, C.C.1
  • 9
    • 20844436424 scopus 로고    scopus 로고
    • Predicting enzyme subclass by functional domain composition and pseudo amino acid composition
    • DOI 10.1021/pr0500399
    • Y-D Cai K-C Chou 2005 Predicting enzyme subclass by functional domain composition and pseudo amino acid composition J Proteome Res 4 967 971 1:CAS:528:DC%2BD2MXjtVWnur4%3D 10.1021/pr0500399 15952744 (Pubitemid 40863286)
    • (2005) Journal of Proteome Research , vol.4 , Issue.3 , pp. 967-971
    • Cai, Y.-D.1    Chou, K.-C.2
  • 10
    • 32144446189 scopus 로고    scopus 로고
    • Enhanced recognition of protein transmembrane domains with prediction-based structural profiles
    • DOI 10.1093/bioinformatics/bti784
    • B Cao A Porollo R Adamczak M Jarrell J Meller 2006 Enhanced recognition of protein transmembrane domains with prediction-based structural profiles Bioinformatics 22 303 309 1:CAS:528:DC%2BD28XhtFais74%3D 10.1093/bioinformatics/ bti784 16293670 (Pubitemid 43205376)
    • (2006) Bioinformatics , vol.22 , Issue.3 , pp. 303-309
    • Cao, B.1    Porollo, A.2    Adamczak, R.3    Jarrell, M.4    Meller, J.5
  • 11
    • 0019869922 scopus 로고
    • Protein folding and the genetic code: An alternative quantitative model
    • DOI 10.1016/0022-5193(81)90377-5
    • M Charton 1981 Protein folding and the genetic code: an alterative quantitative model J Theor Biol 91 115 123 1:CAS:528:DyaL3MXlt1Olt70%3D 10.1016/0022-5193(81)90377-5 7300379 (Pubitemid 11007719)
    • (1981) Journal of Theoretical Biology , vol.91 , Issue.1 , pp. 115-123
    • Charton, M.1
  • 12
    • 0020371598 scopus 로고
    • The structural dependence of amino acid hydrophobicity parameters
    • DOI 10.1016/0022-5193(82)90191-6
    • M Charton BI Charton 1982 The structural dependence of amino acid hydrophobicity parameters J Theor Biol 99 629 644 1:CAS:528:DyaL3sXhsVers7g%3D 10.1016/0022-5193(82)90191-6 7183857 (Pubitemid 13192303)
    • (1982) Journal of Theoretical Biology , vol.99 , Issue.4 , pp. 629-644
    • Charton, M.1    Charton, B.I.2
  • 13
    • 58149269554 scopus 로고    scopus 로고
    • Prediction of integral membrane protein type by collocated hydrophobic amino acid pairs
    • 10.1002/jcc.21053 18567007
    • K Chen Y Jiang L Du L Kurgan 2009 Prediction of integral membrane protein type by collocated hydrophobic amino acid pairs J Comput Chem 30 163 172 10.1002/jcc.21053 18567007
    • (2009) J Comput Chem , vol.30 , pp. 163-172
    • Chen, K.1    Jiang, Y.2    Du, L.3    Kurgan, L.4
  • 14
    • 0034687538 scopus 로고    scopus 로고
    • Prediction of protein subcellular locations by incorporating quasi-sequence-order effect
    • 1:CAS:528:DC%2BD3cXotlKksbs%3D 10.1006/bbrc.2000.3815 11097861
    • KC Chou 2000 Prediction of protein subcellular locations by incorporating quasi-sequence-order effect Biochem Biophys Res Commun 278 477 483 1:CAS:528:DC%2BD3cXotlKksbs%3D 10.1006/bbrc.2000.3815 11097861
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 477-483
    • Chou, K.C.1
  • 15
    • 32344433486 scopus 로고    scopus 로고
    • Predicting protein-protein interactions from sequences in a hybridization space
    • 10.1021/pr050331g
    • KC Chou YD Cai 2005 Predicting protein-protein interactions from sequences in a hybridization space J Proteome Res 5 316 322 10.1021/pr050331g
    • (2005) J Proteome Res , vol.5 , pp. 316-322
    • Chou, K.C.1    Cai, Y.D.2
  • 16
    • 0026636312 scopus 로고
    • Hydrophobicity and structural classes in proteins
    • 1:CAS:528:DyaK38XlvVKrtLk%3D 10.1093/protein/5.5.373 1518784
    • H Cid M Bunster M Canales F Gazitua 1992 Hydrophobicity and structural classes in proteins Protein Eng 5 373 375 1:CAS:528:DyaK38XlvVKrtLk%3D 10.1093/protein/5.5.373 1518784
    • (1992) Protein Eng , vol.5 , pp. 373-375
    • Cid, H.1    Bunster, M.2    Canales, M.3    Gazitua, F.4
  • 17
    • 34249753618 scopus 로고
    • Support-vector networks
    • C Cortes V Vapnik 1995 Support-vector networks Mach Learn 20 273 297
    • (1995) Mach Learn , vol.20 , pp. 273-297
    • Cortes, C.1    Vapnik, V.2
  • 19
    • 0023959836 scopus 로고
    • Voronoi polyhedra as structure probes in large molecular systems
    • 1:CAS:528:DyaL1cXksFSktb4%3D 10.1002/bip.360270212 3359006
    • CW David 1988 Voronoi polyhedra as structure probes in large molecular systems Biopolymers 27 339 344 1:CAS:528:DyaL1cXksFSktb4%3D 10.1002/bip. 360270212 3359006
    • (1988) Biopolymers , vol.27 , pp. 339-344
    • David, C.W.1
  • 21
    • 0029047319 scopus 로고
    • Prediction of protein folding class using global description of amino acid sequence
    • 1:CAS:528:DyaK2MXotVGqsr4%3D 10.1073/pnas.92.19.8700 7568000
    • I Dubchak I Muchnik SR Holbrook SH Kim 1995 Prediction of protein folding class using global description of amino acid sequence Proc Natl Acad Sci USA 92 8700 8704 1:CAS:528:DyaK2MXotVGqsr4%3D 10.1073/pnas.92.19.8700 7568000
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8700-8704
    • Dubchak, I.1    Muchnik, I.2    Holbrook, S.R.3    Kim, S.H.4
  • 22
    • 33747871503 scopus 로고    scopus 로고
    • ZPRED: Predicting the distance to the membrane center for residues in α-helical membrane proteins
    • DOI 10.1093/bioinformatics/btl206
    • E Granseth H Viklund A Elofsson 2006 ZPRED: predicting the distance to the membrane center for residues in {alpha}-helical membrane proteins Bioinformatics 22 e191 e196 1:CAS:528:DC%2BD28Xotl2rt74%3D 10.1093/ bioinformatics/btl206 16873471 (Pubitemid 44288286)
    • (2006) Bioinformatics , vol.22 , Issue.14
    • Granseth, E.1    Viklund, H.2    Elofsson, A.3
  • 23
    • 0036161259 scopus 로고    scopus 로고
    • Gene selection for cancer classification using support vector machines
    • DOI 10.1023/A:1012487302797
    • I Guyon J Weston S Barnhill V Vapnik 2002 Gene selection for cancer classification using support vector machines Mach Learn 46 389 422 10.1023/A:1012487302797 (Pubitemid 34129977)
    • (2002) Machine Learning , vol.46 , Issue.1-3 , pp. 389-422
    • Guyon, I.1    Weston, J.2    Barnhill, S.3    Vapnik, V.4
  • 24
    • 13444251475 scopus 로고    scopus 로고
    • Predicting functional family of novel enzymes irrespective of sequence similarity: A statistical learning approach
    • DOI 10.1093/nar/gkh984
    • LY Han CZ Cai ZL Ji ZW Cao J Cui YZ Chen 2004 Predicting functional family of novel enzymes irrespective of sequence similarity: a statistical learning approach Nucleic Acids Res 32 6437 6444 1:CAS:528:DC%2BD2cXhtVOjs73F 10.1093/nar/gkh984 15585667 (Pubitemid 40202102)
    • (2004) Nucleic Acids Research , vol.32 , Issue.21 , pp. 6437-6444
    • Han, L.Y.1    Cai, C.Z.2    Ji, Z.L.3    Cao, Z.W.4    Cui, J.5    Chen, Y.Z.6
  • 25
    • 33947600314 scopus 로고    scopus 로고
    • Support vector machines approach for predicting druggable proteins: recent progress in its exploration and investigation of its usefulness
    • DOI 10.1016/j.drudis.2007.02.015, PII S1359644607000967
    • LY Han CJ Zheng B Xie J Jia XH Ma F Zhu HH Lin X Chen YZ Chen 2007 Support vector machines approach for predicting druggable proteins: recent progress in its exploration and investigation of its usefulness Drug Disco Today 12 304 313 1:CAS:528:DC%2BD2sXjs1OntLc%3D 10.1016/j.drudis.2007.02.015 (Pubitemid 46476873)
    • (2007) Drug Discovery Today , vol.12 , Issue.7-8 , pp. 304-313
    • Han, L.Y.1    Zheng, C.J.2    Xie, B.3    Jia, J.4    Ma, X.H.5    Zhu, F.6    Lin, H.H.7    Chen, X.8    Chen, Y.Z.9
  • 26
    • 0028043552 scopus 로고
    • Position-based sequence weights
    • DOI 10.1016/0022-2836(94)90032-9
    • S Henikoff JG Henikoff 1994 Position-based sequence weights J Mol Biol 243 574 578 1:CAS:528:DyaK2MXitVKltbo%3D 10.1016/0022-2836(94)90032-9 7966282 (Pubitemid 24341703)
    • (1994) Journal of Molecular Biology , vol.243 , Issue.4 , pp. 574-578
    • Henikoff, S.1    Henikoff, J.G.2
  • 27
    • 37249037182 scopus 로고    scopus 로고
    • Molecular code for transmembrane-helix recognition by the Sec61 translocon
    • DOI 10.1038/nature06387, PII NATURE06387
    • T Hessa NM Meindl-Beinker A Bernsel H Kim Y Sato M Lerch-Bader I Nilsson SH White G Von Heijne 2007 Molecular code for transmembrane-helix recognition by the Sec61 translocon Nature 450 1026 1030 1:CAS:528:DC%2BD2sXhsVaqtrrK 10.1038/nature06387 18075582 (Pubitemid 350273612)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1026-1030
    • Hessa, T.1    Meindl-Beinker, N.M.2    Bernsel, A.3    Kim, H.4    Sato, Y.5    Lerch-Bader, M.6    Nilsson, I.7    White, S.H.8    Von Heijne, G.9
  • 28
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • DOI 10.1126/science.1087619
    • Y Huang MJ Lemieux J Song M Auer D-N Wang 2003 Structure and mechanism of the Glycerol-3-Phosphate transporter from Escherichia coli Science 301 616 620 1:CAS:528:DC%2BD3sXlvVKns7Y%3D 10.1126/science.1087619 12893936 (Pubitemid 36927940)
    • (2003) Science , vol.301 , Issue.5633 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.-N.5
  • 29
    • 77953625243 scopus 로고    scopus 로고
    • MPPAP: An accessibility predictor for alpha-helical transmembrane proteins that performs well inside and outside the membrane
    • 10.1186/1471-2105-11-333 20565847
    • K Illergard S Callegari A Elofsson 2010 MPPAP: an accessibility predictor for alpha-helical transmembrane proteins that performs well inside and outside the membrane BMC Bioinformatics 11 333 10.1186/1471-2105-11-333 20565847
    • (2010) BMC Bioinformatics , vol.11 , pp. 333
    • Illergard, K.1    Callegari, S.2    Elofsson, A.3
  • 30
    • 0035109170 scopus 로고    scopus 로고
    • MPtopo: A database of membrane protein topology
    • DOI 10.1110/ps.43501
    • S Jayasinghe K Hristova SH White 2001 MPtopo: a database of membrane protein topology Protein Sci 10 455 458 1:CAS:528:DC%2BD3MXksFKhsrk%3D 10.1110/ps.43501 11266632 (Pubitemid 32225666)
    • (2001) Protein Science , vol.10 , Issue.2 , pp. 455-458
    • Jayasinghe, S.1    Hristova, K.2    White, S.H.3
  • 31
    • 34047151404 scopus 로고    scopus 로고
    • Improving the accuracy of transmembrane protein topology prediction using evolutionary information
    • DOI 10.1093/bioinformatics/btl677
    • DT Jones 2007 Improving the accuracy of transmembrane protein topology prediction using evolutionary information Bioinformatics 23 538 544 1:CAS:528:DC%2BD2sXkt1GhsLc%3D 10.1093/bioinformatics/btl677 17237066 (Pubitemid 46522586)
    • (2007) Bioinformatics , vol.23 , Issue.5 , pp. 538-544
    • Jones, D.T.1
  • 33
    • 33747816816 scopus 로고    scopus 로고
    • PROFEAT: A web server for computing structural and physicochemical features of proteins and peptides from amino acid sequence
    • DOI 10.1093/nar/gkl305
    • ZR Li HH Lin LY Han L Jiang X Chen YZ Chen 2006 PROFEAT: a web server for computing structural and physicochemical features of proteins and peptides from amino acid sequence Nucleic Acids Res 34 W32 W37 1:CAS:528:DC%2BD28Xps1yht70%3D 10.1093/nar/gkl305 16845018 (Pubitemid 44529730)
    • (2006) Nucleic Acids Research , vol.34 , Issue.WEB. SERV. ISS.
    • Li, Z.R.1    Lin, H.H.2    Han, L.Y.3    Jiang, L.4    Chen, X.5    Chen, Y.Z.6
  • 34
    • 50949094134 scopus 로고    scopus 로고
    • Prediction of protein structure class by coupling improved genetic algorithm and support vector machine
    • 1:CAS:528:DC%2BD1cXhtVGntr%2FI 10.1007/s00726-008-0084-z 18427714
    • ZC Li XB Zhou YR Lin XY Zou 2008 Prediction of protein structure class by coupling improved genetic algorithm and support vector machine Amino Acids 35 581 590 1:CAS:528:DC%2BD1cXhtVGntr%2FI 10.1007/s00726-008-0084-z 18427714
    • (2008) Amino Acids , vol.35 , pp. 581-590
    • Li, Z.C.1    Zhou, X.B.2    Lin, Y.R.3    Zou, X.Y.4
  • 35
    • 65449147106 scopus 로고    scopus 로고
    • A novel method for protein-ligand binding affinity prediction and the related descriptors exploration
    • 1:CAS:528:DC%2BD1MXjvFantrc%3D 10.1002/jcc.21078 18785151
    • S Li L Xi C Wang J Li B Lei H Liu X Yao 2009 A novel method for protein-ligand binding affinity prediction and the related descriptors exploration J Comput Chem 30 900 909 1:CAS:528:DC%2BD1MXjvFantrc%3D 10.1002/jcc.21078 18785151
    • (2009) J Comput Chem , vol.30 , pp. 900-909
    • Li, S.1    Xi, L.2    Wang, C.3    Li, J.4    Lei, B.5    Liu, H.6    Yao, X.7
  • 36
    • 0034874330 scopus 로고    scopus 로고
    • Accurate prediction of protein secondary structural content
    • DOI 10.1023/A:1010967008838
    • Z Lin X-M Pan 2001 Accurate prediction of protein secondary structural content J Protein Chem 20 217 220 10.1023/A:1010967008838 11565901 (Pubitemid 32801840)
    • (2001) Journal of Protein Chemistry , vol.20 , Issue.3 , pp. 217-220
    • Lin, Z.1    Pan, X.-M.2
  • 37
    • 0037136435 scopus 로고    scopus 로고
    • Genomic analysis of membrane protein families: Abundance and conserved motifs
    • Liu Y, Engelman D, Gerstein M (2002) Genomic analysis of membrane protein families: abundance and conserved motifs. Genome Biol 3: research0054.0051- research0054.0012
    • (2002) Genome Biol , vol.3
    • Liu, Y.1    Engelman, D.2    Gerstein, M.3
  • 39
    • 14744270888 scopus 로고    scopus 로고
    • Membrane protein insertion and stability
    • DOI 10.1126/science.1110525
    • R MacKinnon 2005 STRUCTURAL BIOLOGY: membrane protein insertion and stability Science 307 1425 1426 1:CAS:528:DC%2BD2MXitV2jtrw%3D 10.1126/science.1110525 15746418 (Pubitemid 40321931)
    • (2005) Science , vol.307 , Issue.5714 , pp. 1425-1426
    • Mackinnon, R.1
  • 40
    • 0016772212 scopus 로고
    • Comparison of the predicted and observed secondary structure of T4 phage lysozyme
    • 1:CAS:528:DyaE2MXlslCksbk%3D
    • BW Matthews 1975 Comparison of the predicted and observed secondary structure of T4 phage lysozyme Biochimica Biophys Acta 405 442 451 1:CAS:528:DyaE2MXlslCksbk%3D
    • (1975) Biochimica Biophys Acta , vol.405 , pp. 442-451
    • Matthews, B.W.1
  • 41
    • 50949084329 scopus 로고    scopus 로고
    • An ensemble of support vector machines for predicting the membrane protein type directly from the amino acid sequence
    • 1:CAS:528:DC%2BD1cXhtVGntr%2FM 10.1007/s00726-008-0083-0 18427715
    • L Nanni A Lumini 2008 An ensemble of support vector machines for predicting the membrane protein type directly from the amino acid sequence Amino Acids 35 573 580 1:CAS:528:DC%2BD1cXhtVGntr%2FM 10.1007/s00726-008-0083-0 18427715
    • (2008) Amino Acids , vol.35 , pp. 573-580
    • Nanni, L.1    Lumini, A.2
  • 42
    • 58149475508 scopus 로고    scopus 로고
    • Backbone structure of a small helical integral membrane protein: A unique structural characterization
    • 1:CAS:528:DC%2BD1MXmslCiur8%3D 19177358
    • RC Page S Lee JD Moore SJ Opella TA Cross 2009 Backbone structure of a small helical integral membrane protein: a unique structural characterization Protein Sci 18 134 146 1:CAS:528:DC%2BD1MXmslCiur8%3D 19177358
    • (2009) Protein Sci , vol.18 , pp. 134-146
    • Page, R.C.1    Lee, S.2    Moore, J.D.3    Opella, S.J.4    Cross, T.A.5
  • 44
    • 33750596099 scopus 로고    scopus 로고
    • How strongly do sequence conservation patterns and empirical scales correlate with exposure patterns of transmembrane helices of membrane proteins?
    • DOI 10.1002/bip.20569
    • Y Park V Helms 2006 How strongly do sequence conservation patterns and empirical scales correlate with exposure patterns of transmembrane helices of membrane proteins? Biopolymers 83 389 399 1:CAS:528:DC%2BD28XhtFCgtL%2FF 10.1002/bip.20569 16838301 (Pubitemid 44683083)
    • (2006) Biopolymers , vol.83 , Issue.4 , pp. 389-399
    • Park, Y.1    Helms, V.2
  • 45
    • 34147156227 scopus 로고    scopus 로고
    • On the derivation of propensity scales for predicting exposed transmembrane residues of helical membrane proteins
    • DOI 10.1093/bioinformatics/btl653
    • Y Park V Helms 2007 On the derivation of propensity scales for predicting exposed transmembrane residues of helical membrane proteins Bioinformatics 23 701 708 1:CAS:528:DC%2BD2sXkt1Ghtrs%3D 10.1093/bioinformatics/btl653 17237049 (Pubitemid 46554721)
    • (2007) Bioinformatics , vol.23 , Issue.6 , pp. 701-708
    • Park, Y.1    Helms, V.2
  • 46
    • 34948861813 scopus 로고    scopus 로고
    • Prediction of the burial status of transmembrane residues of helical membrane proteins
    • DOI 10.1186/1471-2105-8-302
    • Y Park S Hayat V Helms 2007 Prediction of the burial status of transmembrane residues of helical membrane proteins BMC Bioinformatics 8 302 10.1186/1471-2105-8-302 17708758 (Pubitemid 47527295)
    • (2007) BMC Bioinformatics , vol.8 , pp. 302
    • Park, Y.1    Hayat, S.2    Helms, V.3
  • 47
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • DOI 10.1126/science.277.5332.1676
    • E Pebay-Peyroula G Rummel JP Rosenbusch EM Landau 1997 X-ray Structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases Science 277 1676 1681 1:CAS:528:DyaK2sXmtVSntrc%3D 10.1126/science.277. 5332.1676 9287223 (Pubitemid 27446232)
    • (1997) Science , vol.277 , Issue.5332 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 48
    • 0034843597 scopus 로고    scopus 로고
    • AL2CO: Calculation of positional conservation in a protein sequence alignment
    • J Pei NV Grishin 2001 AL2CO: calculation of positional conservation in a protein sequence alignment Bioinformatics 17 700 712 1:CAS:528: DC%2BD3MXntFKjsb8%3D 10.1093/bioinformatics/17.8.700 11524371 (Pubitemid 32851378)
    • (2001) Bioinformatics , vol.17 , Issue.8 , pp. 700-712
    • Pei, J.1    Grishin, N.V.2
  • 49
    • 33847626984 scopus 로고    scopus 로고
    • A missing link in membrane protein evolution
    • DOI 10.1126/science.1140073
    • B Poolman ER Geertsma D-J Slotboom 2007 BIOCHEMISTRY: a missing link in membrane protein evolution Science 315 1229 1231 1:CAS:528:DC%2BD2sXislektbg%3D 10.1126/science.1140073 17332400 (Pubitemid 46364250)
    • (2007) Science , vol.315 , Issue.5816 , pp. 1229-1231
    • Footman, B.1    Geertsma, E.R.2    Slotboom, D.-J.3
  • 50
    • 0030814427 scopus 로고    scopus 로고
    • An update of the DEF database of protein fold class predictions
    • DOI 10.1093/nar/25.1.235
    • M Reczko D Karras H Bohr 1997 An update of the DEF database of protein fold class predictions Nucleic Acids Res 25 235 1:CAS:528:DyaK2sXpvFKiuw%3D%3D 10.1093/nar/25.1.235 9016543 (Pubitemid 27303186)
    • (1997) Nucleic Acids Research , vol.25 , Issue.1 , pp. 235
    • Reczko, M.1    Karras, D.2    Bohr, H.3
  • 51
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • 1:CAS:528:DC%2BD3cXhtFakt74%3D 10.1006/jmbi.1999.3489 10677291
    • WP Russ DM Engelman 2000 The GxxxG motif: a framework for transmembrane helix-helix association J Mol Biol 296 911 919 1:CAS:528:DC%2BD3cXhtFakt74%3D 10.1006/jmbi.1999.3489 10677291
    • (2000) J Mol Biol , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 52
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helix: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • 1:CAS:528:DC%2BD3cXhtFaktrc%3D 10.1006/jmbi.1999.3488 10677292
    • A Senes M Gerstein DM Engelman 2000 Statistical analysis of amino acid patterns in transmembrane helix: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions J Mol Biol 296 921 936 1:CAS:528:DC%2BD3cXhtFaktrc%3D 10.1006/jmbi.1999.3488 10677292
    • (2000) J Mol Biol , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 53
    • 34249074523 scopus 로고    scopus 로고
    • Using ensemble classifier to identify membrane protein types
    • DOI 10.1007/s00726-006-0439-2, Special Issue: Focus on Amino Acid and Protein Modification by Oxygen and Nitrogen Species
    • HB Shen KC Chou 2007 Using ensemble classifier to identify membrane protein types Amino Acids 32 483 488 1:CAS:528:DC%2BD2sXlsVGnsLY%3D 10.1007/s00726-006-0439-2 17031474 (Pubitemid 46790941)
    • (2007) Amino Acids , vol.32 , Issue.4 , pp. 483-488
    • Shen, H.-B.1    Chou, K.-C.2
  • 54
    • 29244463544 scopus 로고    scopus 로고
    • Population structure inferred by local spatial autocorrelation: An example from an Amerindian tribal population
    • DOI 10.1002/ajpa.20250
    • RR Sokal BA Thomson 2006 Population structure inferred by local spatial autocorrelation: an example from an Amerindian tribal population Am J Phys Anthropol 129 121 131 10.1002/ajpa.20250 16261547 (Pubitemid 41821668)
    • (2006) American Journal of Physical Anthropology , vol.129 , Issue.1 , pp. 121-131
    • Sokal, R.R.1    Thomson, B.A.2
  • 55
    • 0035182559 scopus 로고    scopus 로고
    • Substitution rates in α-helical transmembrane proteins
    • DOI 10.1110/ps.ps.10501
    • TJ Stevens IT Arkin 2001 Substitution rates in alpha-helical transmembrane proteins Protein Sci 10 2507 2517 1:CAS:528:DC%2BD3MXovVyru7w%3D 10.1110/ps.ps.10501 11714918 (Pubitemid 33091574)
    • (2001) Protein Science , vol.10 , Issue.12 , pp. 2507-2517
    • Stevens, T.J.1    Arkin, I.T.2
  • 56
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • DOI 10.1038/414872a
    • H Sui B-G Han JK Lee P Walian BK Jap 2001 Structural basis of water-specific transport through the AQP1 water channel Nature 414 872 878 1:CAS:528:DC%2BD38XhtlOjuw%3D%3D 10.1038/414872a 11780053 (Pubitemid 34024731)
    • (2001) Nature , vol.414 , Issue.6866 , pp. 872-878
    • Sui, H.1    Han, B.-G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 57
    • 0033028454 scopus 로고    scopus 로고
    • PSIC: Profile extraction from sequence alignments with position-specific counts of independent observations
    • SR Sunyaev F Eisenhaber IV Rodchenkov B Eisenhaber VG Tumanyan EN Kuznetsov 1999 PSIC: profile extraction from sequence alignments with position-specific counts of independent observations Protein Eng 12 387 394 1:CAS:528:DyaK1MXktVeluro%3D 10.1093/protein/12.5.387 10360979 (Pubitemid 29265395)
    • (1999) Protein Engineering , vol.12 , Issue.5 , pp. 387-394
    • Sunyaev, S.R.1    Eisenhaber, F.2    Rodchenkov, I.V.3    Eisenhaber, B.4    Tumanyan, V.G.5    Kuznetsov, E.N.6
  • 58
    • 0032638628 scopus 로고    scopus 로고
    • Least squares support vector machine classifiers
    • 10.1023/A:1018628609742
    • JAK Suykens J Vandewalle 1999 Least squares support vector machine classifiers Neural Process Lett 9 293 300 10.1023/A:1018628609742
    • (1999) Neural Process Lett , vol.9 , pp. 293-300
    • Suykens, J.A.K.1    Vandewalle, J.2
  • 59
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • JD Thompson DG Higgins TJ Gibson 1994 CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res 22 4673 4680 1:CAS:528:DyaK2MXitlSgu74%3D 10.1093/nar/22.22.4673 7984417 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 61
    • 3042579686 scopus 로고    scopus 로고
    • Best α-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information
    • DOI 10.1110/ps.04625404
    • H Viklund A Elofsson 2004 Best alpha-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information Protein Sci 13 1908 1917 1:CAS:528:DC%2BD2cXlsFWktbk%3D 10.1110/ps.04625404 15215532 (Pubitemid 38822130)
    • (2004) Protein Science , vol.13 , Issue.7 , pp. 1908-1917
    • Viklund, H.1    Elofsson, A.2
  • 62
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled receptor structures and mechanisms
    • DOI 10.1016/S0076-6879(02)43145-X
    • I Visiers JA Ballesteros H Weistein 2002 Three-dimensional representations of G protein-coupled receptor structures and mechanisms Methods Enzymol 343 329 371 10.1016/S0076-6879(02)43145-X 11665578 (Pubitemid 32954152)
    • (2001) Methods in Enzymology , vol.343 , pp. 329-371
    • Visiers, I.1    Ballesteros, J.A.2    Weinstein, H.3
  • 63
    • 0033342531 scopus 로고    scopus 로고
    • Recent advances in the understanding of membrane protein assembly and structure
    • DOI 10.1017/S0033583500003541
    • G von Heijine 1999 Recent advances in the understanding of membrane protein assembly and structure Q Rev Biophys 32 285 307 10.1017/ S0033583500003541 (Pubitemid 30636355)
    • (1999) Quarterly Reviews of Biophysics , vol.32 , Issue.4 , pp. 285-307
    • Von Heijne, G.1
  • 65
    • 48249095616 scopus 로고    scopus 로고
    • How translocons select transmembrane helices
    • 1:CAS:528:DC%2BD1cXnsVGltb4%3D 10.1146/annurev.biophys.37.032807.125904 18573071
    • SH White G von Heijine 2008 How translocons select transmembrane helices Annu Rev Biophys 37 23 42 1:CAS:528:DC%2BD1cXnsVGltb4%3D 10.1146/annurev. biophys.37.032807.125904 18573071
    • (2008) Annu Rev Biophys , vol.37 , pp. 23-42
    • White, S.H.1    Von Heijine, G.2
  • 66
    • 32944461574 scopus 로고    scopus 로고
    • Using cellular automata images and pseudo amino acid composition to predict protein subcellular location
    • 1:CAS:528:DC%2BD28XhsFCksrk%3D 10.1007/s00726-005-0225-6 16044193
    • X Xiao S Shao Y Ding Z Huang KC Chou 2006 Using cellular automata images and pseudo amino acid composition to predict protein subcellular location Amino Acids 30 49 54 1:CAS:528:DC%2BD28XhsFCksrk%3D 10.1007/s00726-005-0225-6 16044193
    • (2006) Amino Acids , vol.30 , pp. 49-54
    • Xiao, X.1    Shao, S.2    Ding, Y.3    Huang, Z.4    Chou, K.C.5
  • 67
    • 26944447129 scopus 로고    scopus 로고
    • Prediction of T-cell epitopes using biosupport vector machines
    • DOI 10.1021/ci050004t
    • ZR Yang FC Johnson 2005 Prediction of T-cell epitopes using biosupport vector machines J Chem Inf Model 45 1424 1428 1:CAS:528:DC%2BD2MXls1SjtLo%3D 10.1021/ci050004t 16180919 (Pubitemid 41476025)
    • (2005) Journal of Chemical Information and Modeling , vol.45 , Issue.5 , pp. 1424-1428
    • Yang, Z.R.1    Johnson, F.C.2
  • 68
    • 77955877726 scopus 로고    scopus 로고
    • Using auto covariance method for functional discrimination of membrane proteins based on evolution information
    • 1:CAS:528:DC%2BC3cXlt1Omurg%3D 10.1007/s00726-009-0362-4 19820894
    • L Yang Y Li R Xiao Y Zeng J Xiao F Tan M Li 2010 Using auto covariance method for functional discrimination of membrane proteins based on evolution information Amino Acids 38 1497 1503 1:CAS:528:DC%2BC3cXlt1Omurg%3D 10.1007/s00726-009-0362-4 19820894
    • (2010) Amino Acids , vol.38 , pp. 1497-1503
    • Yang, L.1    Li, Y.2    Xiao, R.3    Zeng, Y.4    Xiao, J.5    Tan, F.6    Li, M.7
  • 69
    • 33646596891 scopus 로고    scopus 로고
    • Predicting the solvent accessibility of transmembrane residues from protein sequence
    • DOI 10.1021/pr050397b
    • Z Yuan F Zhang MJ Davis M Bodén RD Teasdale 2006 Predicting the solvent accessibility of transmembrane residues from protein sequence J Proteome Res 5 1063 1070 1:CAS:528:DC%2BD28XivFelsr0%3D 10.1021/pr050397b 16674095 (Pubitemid 43727784)
    • (2006) Journal of Proteome Research , vol.5 , Issue.5 , pp. 1063-1070
    • Yuan, Z.1    Zhang, F.2    Davis, M.J.3    Boden, M.4    Teasdale, R.D.5
  • 70
    • 33745076136 scopus 로고    scopus 로고
    • Prediction of protein homo-oligomer types by pseudo amino acid composition: Approached with an improved feature extraction and Naive Bayes Feature Fusion
    • DOI 10.1007/s00726-006-0263-8
    • SW Zhang Q Pan HC Zhang ZC Shao JY Shi 2006 Prediction of protein homo-oligomer types by pseudo amino acid composition: approached with an improved feature extraction and Naive Bayes Feature Fusion Amino Acids 30 461 468 1:CAS:528:DC%2BD28Xls1egsr0%3D 10.1007/s00726-006-0263-8 16773245 (Pubitemid 43886907)
    • (2006) Amino Acids , vol.30 , Issue.4 , pp. 461-468
    • Zhang, S.-W.1    Pan, Q.2    Zhang, H.-C.3    Shao, Z.-C.4    Shi, J.-Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.