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Volumn 426, Issue 4, 2014, Pages 945-961

Functional clustering of immunoglobulin superfamily proteins with protein-protein interaction information calibrated hidden markov model sequence profiles

Author keywords

functional prediction; immunoglobulin superfamily; protein protein interaction

Indexed keywords

ABATACEPT; AMINO ACID; BELATACEPT; IMMUNOGLOBULIN; IMMUNOGLOBULIN SUPERFAMILY PROTEIN; IPILIMUMAB; KILLER CELL IMMUNOGLOBULIN LIKE RECEPTOR; LIGAND; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN; PROTEOME; SIALIC ACID BINDING IMMUNOGLOBULIN LIKE LECTIN; UNCLASSIFIED DRUG; B7 ANTIGEN; CD86 ANTIGEN; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4;

EID: 84893690007     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.11.009     Document Type: Article
Times cited : (21)

References (67)
  • 2
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily - Domains for cell surface recognition
    • A.F. Williams, and A.N. Barclay The immunoglobulin superfamily - domains for cell-surface recognition Annu Rev Immunol 6 1988 381 405 (Pubitemid 19141589)
    • (1988) Annual Review of Immunology , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 3
    • 0042620298 scopus 로고    scopus 로고
    • Membrane proteins with immunoglobulin-like domains - A master superfamily of interaction molecules
    • DOI 10.1016/S1044-5323(03)00047-2
    • A.N. Barclay Membrane proteins with immunoglobulin-like domains - a master superfamily of interaction molecules Semin Immunol 15 2003 215 223 (Pubitemid 38167234)
    • (2003) Seminars in Immunology , vol.15 , Issue.4 , pp. 215-223
    • Barclay, A.N.1
  • 7
    • 34548257760 scopus 로고    scopus 로고
    • Review: Anti-CTLA-4 antibody ipilimumab: Case studies of clinical response and immune-related adverse events
    • DOI 10.1634/theoncologist.12-7-864
    • J. Weber Review: anti-CTLA-4 antibody ipilimumab: case studies of clinical response and immune-related adverse events Oncologist 12 2007 864 872 (Pubitemid 47328229)
    • (2007) Oncologist , vol.12 , Issue.7 , pp. 864-872
    • Weber, J.1
  • 8
    • 79952717517 scopus 로고    scopus 로고
    • VISTA, a novel mouse Ig superfamily ligand that negatively regulates T cell responses
    • L. Wang, R. Rubinstein, J.L. Lines, A. Wasiuk, C. Ahonen, and Y.X. Guo et al. VISTA, a novel mouse Ig superfamily ligand that negatively regulates T cell responses J Exp Med 208 2011 577 592
    • (2011) J Exp Med , vol.208 , pp. 577-592
    • Wang, L.1    Rubinstein, R.2    Lines, J.L.3    Wasiuk, A.4    Ahonen, C.5    Guo, Y.X.6
  • 9
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinases
    • P. Bork, C. Sander, and A. Valencia Convergent evolution of similar enzymatic function on different protein folds - the hexokinase, ribokinase, and galactokinase families of sugar kinases Protein Sci 2 1993 31 40 (Pubitemid 23029007)
    • (1993) Protein Science , vol.2 , Issue.1 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 12
    • 33745634395 scopus 로고    scopus 로고
    • Cd-hit: A fast program for clustering and comparing large sets of protein or nucleotide sequences
    • DOI 10.1093/bioinformatics/btl158
    • W.Z. Li, and A. Godzik CD-HIT: a fast program for clustering and comparing large sets of protein or nucleotide sequences Bioinformatics 22 2006 1658 1659 (Pubitemid 43985301)
    • (2006) Bioinformatics , vol.22 , Issue.13 , pp. 1658-1659
    • Li, W.1    Godzik, A.2
  • 13
    • 0030627901 scopus 로고    scopus 로고
    • Protein structures sustain evolutionary drift
    • B. Rost Protein structures sustain evolutionary drift Folding Des 2 1997 S19 S24
    • (1997) Folding des , vol.2
    • Rost, B.1
  • 14
    • 84893693440 scopus 로고    scopus 로고
    • Up-regulation of a ras effector and down-regulation of a cell adhesion molecule are associated with transformation of osteoblasts
    • J. Toguchida, Nakamata T., Murakami H., Nakayama T., and Nakamura T. Up-regulation of a ras effector and down-regulation of a cell adhesion molecule are associated with transformation of osteoblasts DDBJ/EMBL/GenBank databases 2000
    • (2000) DDBJ/EMBL/GenBank Databases
    • Toguchida, J.1    Nakamata, T.2    Murakami, H.3    Nakayama, T.4    Nakamura, T.5
  • 15
    • 0026010655 scopus 로고
    • Molecular structure and functional testing of human L1CAM: An interspecies comparison
    • M.L. Hlavin, and V. Lemmon Molecular structure and functional testing of human L1CAM: an interspecies comparison Genomics 11 1991 416 423
    • (1991) Genomics , vol.11 , pp. 416-423
    • Hlavin, M.L.1    Lemmon, V.2
  • 16
    • 34548392746 scopus 로고    scopus 로고
    • Automated protein subfamily identification and classification
    • D.P. Brown, N. Krishnamurthy, and K. Sjölander Automated protein subfamily identification and classification PLoS Comput Biol 3 2007 e160
    • (2007) PLoS Comput Biol , vol.3 , pp. 160
    • Brown, D.P.1    Krishnamurthy, N.2    Sjölander, K.3
  • 17
    • 77950362058 scopus 로고    scopus 로고
    • GeMMA: Functional subfamily classification within superfamilies of predicted protein structural domains
    • D.A. Lee, R. Rentzsch, and C. Orengo GeMMA: functional subfamily classification within superfamilies of predicted protein structural domains Nucleic Acids Res 38 2010 720 737
    • (2010) Nucleic Acids Res , vol.38 , pp. 720-737
    • Lee, D.A.1    Rentzsch, R.2    Orengo, C.3
  • 18
    • 84876578144 scopus 로고    scopus 로고
    • New functional families (FunFams) in CATH to improve the mapping of conserved functional sites to 3D structures
    • I. Sillitoe, A.L. Cuff, B.H. Dessailly, N.L. Dawson, N. Furnham, and D. Lee et al. New functional families (FunFams) in CATH to improve the mapping of conserved functional sites to 3D structures Nucleic Acids Res 41 2013 D490 D498
    • (2013) Nucleic Acids Res , vol.41
    • Sillitoe, I.1    Cuff, A.L.2    Dessailly, B.H.3    Dawson, N.L.4    Furnham, N.5    Lee, D.6
  • 19
    • 67749137351 scopus 로고    scopus 로고
    • Functional annotations improve the predictive score of human diseaseâ€related mutations in proteins
    • R. Calabrese, E. Capriotti, P. Fariselli, P.L. Martelli, and R. Casadio Functional annotations improve the predictive score of human diseaseâ€related mutations in proteins Hum Mutat 30 2009 1237 1244
    • (2009) Hum Mutat , vol.30 , pp. 1237-1244
    • Calabrese, R.1    Capriotti, E.2    Fariselli, P.3    Martelli, P.L.4    Casadio, R.5
  • 21
    • 0036529479 scopus 로고    scopus 로고
    • An efficient algorithm for large-scale detection of protein families
    • A.J. Enright, S. Van Dongen, and C.A. Ouzounis An efficient algorithm for large-scale detection of protein families Nucleic Acids Res 30 2002 1575 1584 (Pubitemid 34679732)
    • (2002) Nucleic Acids Research , vol.30 , Issue.7 , pp. 1575-1584
    • Enright, A.J.1    Van Dongen, S.2    Ouzounis, C.A.3
  • 22
    • 33644560639 scopus 로고    scopus 로고
    • Leveraging enzyme structure-function relationships for functional inference and experimental design: The structure-function linkage database
    • S.C.-H. Pegg, S.D. Brown, S. Ojha, J. Seffernick, E.C. Meng, and J.H. Morris et al. Leveraging enzyme structure-function relationships for functional inference and experimental design: the structure-function linkage database Biochemistry 45 2006 2545 2555
    • (2006) Biochemistry , vol.45 , pp. 2545-2555
    • Pegg, S.C.-H.1    Brown, S.D.2    Ojha, S.3    Seffernick, J.4    Meng, E.C.5    Morris, J.H.6
  • 25
    • 80555156606 scopus 로고    scopus 로고
    • Genome-scale phylogenetic function annotation of large and diverse protein families
    • B.E. Engelhardt, M.I. Jordan, J.R. Srouji, and S.E. Brenner Genome-scale phylogenetic function annotation of large and diverse protein families Genome Res 21 2011 1969 1980
    • (2011) Genome Res , vol.21 , pp. 1969-1980
    • Engelhardt, B.E.1    Jordan, M.I.2    Srouji, J.R.3    Brenner, S.E.4
  • 26
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • DOI 10.1093/bioinformatics/bti125
    • J. Soding Protein homology detection by HMM-HMM comparison Bioinformatics 21 2005 951 960 (Pubitemid 40467915)
    • (2005) Bioinformatics , vol.21 , Issue.7 , pp. 951-960
    • Soding, J.1
  • 27
    • 78651324347 scopus 로고    scopus 로고
    • The STRING database in 2011: Functional interaction networks of proteins, globally integrated and scored
    • D. Szklarczyk, A. Franceschini, M. Kuhn, M. Simonovic, A. Roth, and P. Minguez et al. The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored Nucleic Acids Res 39 2011 D561 D568
    • (2011) Nucleic Acids Res , vol.39
    • Szklarczyk, D.1    Franceschini, A.2    Kuhn, M.3    Simonovic, M.4    Roth, A.5    Minguez, P.6
  • 28
    • 0025269047 scopus 로고
    • The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus
    • D.E. Staunton, M.L. Dustin, H.P. Erickson, and T.A. Springer The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus Cell 61 1990 243 254
    • (1990) Cell , vol.61 , pp. 243-254
    • Staunton, D.E.1    Dustin, M.L.2    Erickson, H.P.3    Springer, T.A.4
  • 29
    • 0029845205 scopus 로고    scopus 로고
    • Localization of the binding site on intercellular adhesion molecule-3 (ICAM-3) for lymphocyte function-associated antigen 1 (LFA-1)
    • DOI 10.1074/jbc.271.39.23920
    • L.B. Klickstein, M.R. York, A.R. deFougerolles, and T.A. Springer Localization of the binding site on intercellular adhesion molecule-3 (ICAM-3) for lymphocyte function-associated antigen 1 (LFA-1) J Biol Chem 271 1996 23920 23927 (Pubitemid 26327367)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.39 , pp. 23920-23927
    • Klickstein, L.B.1    York, M.R.2    De Fougerolles, A.R.3    Springer, T.A.4
  • 30
    • 0029443827 scopus 로고
    • Cell adhesion molecules 1: Immunoglobulin superfamily
    • T. Brummendorf, and F.G. Rathjen Cell adhesion molecules 1: immunoglobulin superfamily Protein Profile 2 1995 963 1108
    • (1995) Protein Profile , vol.2 , pp. 963-1108
    • Brummendorf, T.1    Rathjen, F.G.2
  • 31
    • 0000028423 scopus 로고
    • A quantitative approach to a problem in classification
    • C.D. Michener, and R.R. Sokal A quantitative approach to a problem in classification Evolution 11 1957 32
    • (1957) Evolution , vol.11 , pp. 32
    • Michener, C.D.1    Sokal, R.R.2
  • 32
    • 0023423785 scopus 로고
    • Characterization of binding properties of the myelin-associated glycoprotein to extracellular-matrix constituents
    • T. Fahrig, C. Landa, P. Pesheva, K. Kuhn, and M. Schachner Characterization of binding properties of the myelin-associated glycoprotein to extracellular-matrix constituents EMBO J 6 1987 2875 2883
    • (1987) EMBO J , vol.6 , pp. 2875-2883
    • Fahrig, T.1    Landa, C.2    Pesheva, P.3    Kuhn, K.4    Schachner, M.5
  • 33
    • 0035933604 scopus 로고    scopus 로고
    • Fibronectin is a binding partner for the myelin-associated glycoprotein (siglec-4a)
    • DOI 10.1016/S0014-5793(01)02566-2, PII S0014579301025662
    • K. Strenge, R. Brossmer, P. Ihrig, R. Schauer, and S. Kelm Fibronectin is a binding partner for the myelin-associated glycoprotein (siglec-4a) FEBS Lett 499 2001 262 267 (Pubitemid 32553876)
    • (2001) FEBS Letters , vol.499 , Issue.3 , pp. 262-267
    • Strenge, K.1    Brossmer, R.2    Ihrig, P.3    Schauer, R.4    Kelm, S.5
  • 34
    • 49249119291 scopus 로고    scopus 로고
    • The extended human leukocyte receptor complex: Diverse ways of modulating immune responses
    • A.D. Barrow, and J. Trowsdale The extended human leukocyte receptor complex: diverse ways of modulating immune responses Immunol Rev 224 2008 98 123
    • (2008) Immunol Rev , vol.224 , pp. 98-123
    • Barrow, A.D.1    Trowsdale, J.2
  • 35
    • 0028172973 scopus 로고
    • The pregnancy-specific glycoprotein (PSG) gene cluster on human chromosome 19: Fine structure of the 11 PSG genes and identification of 6 new genes forming a third subgroup within the carcinoembryonic antigen (CEA) family
    • S. Teglund, A. Olsen, W.N. Khan, L. Frångsmyr, and S. Hammarström The pregnancy-specific glycoprotein (PSG) gene cluster on human chromosome 19: fine structure of the 11 PSG genes and identification of 6 new genes forming a third subgroup within the carcinoembryonic antigen (CEA) family Genomics 23 1994 669 684
    • (1994) Genomics , vol.23 , pp. 669-684
    • Teglund, S.1    Olsen, A.2    Khan, W.N.3    Frångsmyr, L.4    Hammarström, S.5
  • 36
    • 0035251711 scopus 로고    scopus 로고
    • The cluster of BTN genes in the extended major histocompatibility complex
    • DOI 10.1006/geno.2000.6406
    • D. Rhodes, M. Stammers, G. Malcherek, S. Beck, and J. Trowsdale The cluster of BTN genes in the extended major histocompatibility complex Genomics 71 2001 351 362 (Pubitemid 32174830)
    • (2001) Genomics , vol.71 , Issue.3 , pp. 351-362
    • Rhodes, D.A.1    Stammers, M.2    Malcherek, G.3    Beck, S.4    Trowsdale, J.5
  • 37
    • 57849101994 scopus 로고    scopus 로고
    • The surface protein TIGIT suppresses T cell activation by promoting the generation of mature immunoregulatory dendritic cells
    • X. Yu, K. Harden, L.C. Gonzalez, M. Francesco, E. Chiang, and B. Irving et al. The surface protein TIGIT suppresses T cell activation by promoting the generation of mature immunoregulatory dendritic cells Nat Immunol 10 2009 48 57
    • (2009) Nat Immunol , vol.10 , pp. 48-57
    • Yu, X.1    Harden, K.2    Gonzalez, L.C.3    Francesco, M.4    Chiang, E.5    Irving, B.6
  • 38
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • DOI 10.1093/nar/gkh340
    • R.C. Edgar MUSCLE: multiple sequence alignment with high accuracy and high throughput Nucleic Acids Res 32 2004 1792 1797 (Pubitemid 38832724)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 40
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • DOI 10.1093/bib/bbn013, Special Issue: Critical Technologies for Bioinformatics
    • K. Katoh, and H. Toh Recent developments in the MAFFT multiple sequence alignment program Brief Bioinform 9 2008 286 298 (Pubitemid 351890825)
    • (2008) Briefings in Bioinformatics , vol.9 , Issue.4 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 41
    • 0028181441 scopus 로고
    • Hidden Markov models in computational biology: Applications to protein modeling
    • A. Krogh, M. Brown, I.S. Mian, K. Sjölander, and D. Haussler Hidden Markov models in computational biology: applications to protein modeling J Mol Biol 235 1994 1501 1531
    • (1994) J Mol Biol , vol.235 , pp. 1501-1531
    • Krogh, A.1    Brown, M.2    Mian, I.S.3    Sjölander, K.4    Haussler, D.5
  • 42
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • S.R. Eddy Profile hidden Markov models Bioinformatics 14 1998 755 763 (Pubitemid 28552108)
    • (1998) Bioinformatics , vol.14 , Issue.9 , pp. 755-763
    • Eddy, S.R.1
  • 44
    • 42649092113 scopus 로고    scopus 로고
    • Skint1, the prototype of a newly identified immunoglobulin superfamily gene cluster, positively selects epidermal γδ T cells
    • DOI 10.1038/ng.108, PII NG108
    • L.M. Boyden, J.M. Lewis, S.D. Barbee, A. Bas, M. Girardi, and A.C. Hayday et al. Skint1, the prototype of a newly identified immunoglobulin superfamily gene cluster, positively selects epidermal gammadelta T cells Nat Genet 40 2008 656 662 (Pubitemid 351601202)
    • (2008) Nature Genetics , vol.40 , Issue.5 , pp. 656-662
    • Boyden, L.M.1    Lewis, J.M.2    Barbee, S.D.3    Bas, A.4    Girardi, M.5    Hayday, A.C.6    Tigelaar, R.E.7    Lifton, R.P.8
  • 45
    • 33646927209 scopus 로고    scopus 로고
    • Proteome analysis of human hair shaft: From protein identification to posttranslational modification
    • DOI 10.1074/mcp.M500278-MCP200
    • Y.J. Lee, R.H. Rice, and Y.M. Lee Proteome analysis of human hair shaft: from protein identification to posttranslational modification Mol Cell Proteomics 5 2006 789 800 (Pubitemid 43792789)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.5 , pp. 789-800
    • Lee, Y.J.1    Rice, R.H.2    Lee, Y.M.3
  • 46
    • 80955180089 scopus 로고    scopus 로고
    • Localization of the novel hair shaft protein VSIG8 in the hair follicle, nail unit and oral cavity
    • R.H. Rice, M.A. Phillips, and J.P. Sundberg Localization of the novel hair shaft protein VSIG8 in the hair follicle, nail unit and oral cavity J Invest Dermatol 131 2011 1936 1938
    • (2011) J Invest Dermatol , vol.131 , pp. 1936-1938
    • Rice, R.H.1    Phillips, M.A.2    Sundberg, J.P.3
  • 47
    • 0035844164 scopus 로고    scopus 로고
    • Cloning of an immunoglobulin family adhesion molecule selectively expressed by endothelial cells
    • K. Hirata, T. Ishida, K. Penta, M. Rezaee, E. Yang, and J. Wohlgemuth et al. Cloning of an immunoglobulin family adhesion molecule selectively expressed by endothelial cells J Biol Chem 276 2001 16223 16231
    • (2001) J Biol Chem , vol.276 , pp. 16223-16231
    • Hirata, K.1    Ishida, T.2    Penta, K.3    Rezaee, M.4    Yang, E.5    Wohlgemuth, J.6
  • 49
    • 20244369880 scopus 로고    scopus 로고
    • Identification of adipocyte adhesion molecule (ACAM), a novel CTX gene family, implicated in adipocyte maturation and development of obesity
    • DOI 10.1042/BJ20041709
    • J. Eguchi, J. Wada, K. Hida, H. Zhang, T. Matsuoka, and M. Baba et al. Identification of adipocyte adhesion molecule (ACAM), a novel CTX gene family, implicated in adipocyte maturation and development of obesity Biochem J 387 2005 343 353 (Pubitemid 40571220)
    • (2005) Biochemical Journal , vol.387 , Issue.2 , pp. 343-353
    • Eguchi, J.1    Wada, J.2    Hida, K.3    Zhang, H.4    Matsuoka, T.5    Baba, M.6    Hashimoto, I.7    Shikata, K.8    Ogawa, N.9    Makino, H.10
  • 50
    • 23244447637 scopus 로고    scopus 로고
    • BT-IgSF, a novel immunoglobulin superfamily protein, functions as a cell adhesion molecule
    • H. Harada, S. Suzu, Y. Hayashi, and S. Okada BT-IgSF, a novel immunoglobulin superfamily protein, functions as a cell adhesion molecule J Cell Physiol 204 2005 8
    • (2005) J Cell Physiol , vol.204 , pp. 8
    • Harada, H.1    Suzu, S.2    Hayashi, Y.3    Okada, S.4
  • 51
    • 0028227022 scopus 로고
    • The neuronal chondroitin sulfate proteoglycan neurocan binds to the neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM, and inhibits neuronal adhesion and neurite outgrowth
    • D.R. Friedlander, P. Milev, L. Karthikeyan, R.K. Margolis, R.U. Margolis, and M. Grumet Neuronal chondroitin sulfate proteoglycan neurocan binds to the neural cell-adhesion molecules Ng-Cam/L1/Nile and N-Cam, and inhibits neuronal adhesion and neurite outgrowth J Cell Biol 125 1994 669 680 (Pubitemid 24149848)
    • (1994) Journal of Cell Biology , vol.125 , Issue.3 , pp. 669-680
    • Friedlander, D.R.1    Milev, P.2    Karthikeyan, L.3    Margolis, R.K.4    Margolis, R.U.5    Grumet, M.6
  • 52
    • 0029896991 scopus 로고    scopus 로고
    • TAG-1/axonin-1 is a high-affinity ligand of neurocan, phosphacan/protein-tyrosine phosphatase-ζ/β, and N-CAM
    • DOI 10.1074/jbc.271.26.15716
    • P. Milev, P. Maurel, M. Haring, R.K. Margolis, and R.U. Margolis TAG-1/axonin-1 is a high-affinity ligand of neurocan, phosphacan/protein- tyrosine phosphatase-zeta/beta, and N-CAM J Biol Chem 271 1996 15716 15723 (Pubitemid 26225350)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.26 , pp. 15716-15723
    • Milev, P.1    Maurel, P.2    Haring, M.3    Margolis, R.K.4    Margolis, R.U.5
  • 53
    • 25644446111 scopus 로고    scopus 로고
    • Modulation of the homophilic interaction between the first and second Ig modules of neural cell adhesion molecule by heparin
    • DOI 10.1111/j.1471-4159.2005.03338.x
    • N. Kulahin, O. Rudenko, V. Kiselyov, F.M. Poulsen, V. Berezin, and E. Bock Modulation of the homophilic interaction between the first and second Ig modules of neural cell adhesion molecule by heparin J Neurochem 95 2005 46 55 (Pubitemid 41384424)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.1 , pp. 46-55
    • Kulahin, N.1    Rudenko, O.2    Kiselyov, V.3    Poulsen, F.M.4    Berezin, V.5    Bock, E.6
  • 54
    • 0034602297 scopus 로고    scopus 로고
    • Characterization of the L1-neurocan-binding site. Implications for L1-L1 homophilic binding
    • M. Oleszewski, P. Gutwein, W. von der Lieth, U. Rauch, and P. Altevogt Characterization of the L1-neurocan-binding site. Implications for L1-L1 homophilic binding J Biol Chem 275 2000 34478 34485
    • (2000) J Biol Chem , vol.275 , pp. 34478-34485
    • Oleszewski, M.1    Gutwein, P.2    Von Der Lieth, W.3    Rauch, U.4    Altevogt, P.5
  • 55
    • 59049083508 scopus 로고    scopus 로고
    • CD96 interaction with CD155 via its first Ig-like domain is modulated by alternative splicing or mutations in distal Ig-like domains
    • D. Meyer, S. Seth, J. Albrecht, M.K. Maier, L. du Pasquier, and I. Ravens et al. CD96 interaction with CD155 via its first Ig-like domain is modulated by alternative splicing or mutations in distal Ig-like domains J Biol Chem 284 2009 2235 2244
    • (2009) J Biol Chem , vol.284 , pp. 2235-2244
    • Meyer, D.1    Seth, S.2    Albrecht, J.3    Maier, M.K.4    Du Pasquier, L.5    Ravens, I.6
  • 57
    • 0042733027 scopus 로고    scopus 로고
    • 3 integrin-containing membrane microdomains
    • DOI 10.1074/jbc.M304166200
    • S. Mueller, and E. Wimmer Recruitment of nectin-3 to cell-cell junctions through trans-heterophilic interaction with CD155, a vitronectin and poliovirus receptor that localizes to alpha(v)beta(3) integrin-containing membrane microdomains J Biol Chem 278 2003 31251 31260 (Pubitemid 36994642)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31251-31260
    • Mueller, S.1    Wimmer, E.2
  • 59
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • DOI 10.1016/j.jmb.2004.03.016, PII S0022283604002943
    • L. Kall, A. Krogh, and E.L.L. Sonnhammer A combined transmembrane topology and signal peptide prediction method J Mol Biol 338 2004 1027 1036 (Pubitemid 38542831)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.5 , pp. 1027-1036
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.L.3
  • 61
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • DOI 10.1006/jmbi.1999.3091
    • D.T. Jones Protein secondary structure prediction based on position-specific scoring matrices J Mol Biol 292 1999 195 202 (Pubitemid 29435759)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 63
    • 5344244656 scopus 로고    scopus 로고
    • R Development Core Team R Foundation for Statistical Computing Vienna, Austria
    • R Development Core Team R: a language and environment for statistical computing 2008 R Foundation for Statistical Computing Vienna, Austria
    • (2008) R: A Language and Environment for Statistical Computing
  • 65
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • T.N. Petersen, S. Brunak, G. von Heijne, and H. Nielsen SignalP 4.0: discriminating signal peptides from transmembrane regions Nat Methods 8 2011 785 786
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 67
    • 0036775035 scopus 로고    scopus 로고
    • Coming to grips with integrin binding to ligands: Opinion
    • DOI 10.1016/S0955-0674(02)00371-X
    • M.A. Arnaout, S.L. Goodman, and J.P. Xiong Coming to grips with integrin binding to ligands Curr Opin Cell Biol 14 2002 641 651 (Pubitemid 35247749)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.5 , pp. 641-651
    • Arnaout M.Amin1    Goodman, S.L.2    Xiong, J.-P.3


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