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Volumn 439, Issue 1-2, 2009, Pages 43-54

Functional evolution of the microfibril-associated glycoproteins

Author keywords

Coevolution; Extracellular matrix; Microfibril; Molecular evolution; Phylogenetics

Indexed keywords

GLYCOPROTEIN; MICROFIBRIL ASSOCIATED GLYCOPROTEIN 1; MICROFIBRIL ASSOCIATED GLYCOPROTEIN 2; NUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 67349124353     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2009.03.013     Document Type: Article
Times cited : (18)

References (88)
  • 1
    • 0016355478 scopus 로고
    • New look at statistical-model identification
    • Akaike H. New look at statistical-model identification. IEEE Trans. Automat. Contr. Ac19 (1974) 716-723
    • (1974) IEEE Trans. Automat. Contr. , vol.Ac19 , pp. 716-723
    • Akaike, H.1
  • 2
    • 34548150900 scopus 로고    scopus 로고
    • Transcriptome analysis of endothelial cell gene expression induced by growth on matrigel matrices: identification and characterization of MAGP-2 and lumican as novel regulators of angiogenesis
    • Albig A.R., Roy T.G., Becenti D.J., and Schiemann W.P. Transcriptome analysis of endothelial cell gene expression induced by growth on matrigel matrices: identification and characterization of MAGP-2 and lumican as novel regulators of angiogenesis. Angiogenesis 10 (2007) 197-216
    • (2007) Angiogenesis , vol.10 , pp. 197-216
    • Albig, A.R.1    Roy, T.G.2    Becenti, D.J.3    Schiemann, W.P.4
  • 3
    • 45449113538 scopus 로고    scopus 로고
    • Microfibril-associate glycoprotein-2 (MAGP-2) promotes angiogenic cell sprouting by blocking notch signaling in endothelial cells
    • Albig A.R., Becenti D.J., Roy T.G., and Schiemann W.P. Microfibril-associate glycoprotein-2 (MAGP-2) promotes angiogenic cell sprouting by blocking notch signaling in endothelial cells. Microvasc. Res. 76 (2008) 7-14
    • (2008) Microvasc. Res. , vol.76 , pp. 7-14
    • Albig, A.R.1    Becenti, D.J.2    Roy, T.G.3    Schiemann, W.P.4
  • 4
    • 37549044268 scopus 로고    scopus 로고
    • Genetic determinants of hyaloid and retinal vasculature in zebrafish
    • Alvarez Y., et al. Genetic determinants of hyaloid and retinal vasculature in zebrafish. BMC Dev. Biol. 7 (2007) 114
    • (2007) BMC Dev. Biol. , vol.7 , pp. 114
    • Alvarez, Y.1
  • 5
    • 26444482460 scopus 로고    scopus 로고
    • Molecular phylogeny and divergence times of deuterostome animals
    • Blair J.E., and Hedges S.B. Molecular phylogeny and divergence times of deuterostome animals. Mol. Biol. Evol. 22 (2005) 2275-2284
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 2275-2284
    • Blair, J.E.1    Hedges, S.B.2
  • 6
    • 0027998108 scopus 로고
    • Microfibril-associated glycoprotein binds to the carboxyl-terminal domain of tropoelastin and is a substrate for transglutaminase
    • Brown-Augsburger P., et al. Microfibril-associated glycoprotein binds to the carboxyl-terminal domain of tropoelastin and is a substrate for transglutaminase. J. Biol. Chem. 269 (1994) 28443-28449
    • (1994) J. Biol. Chem. , vol.269 , pp. 28443-28449
    • Brown-Augsburger, P.1
  • 7
    • 0029811144 scopus 로고    scopus 로고
    • Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly
    • Brown-Augsburger P., Broekelmann T., Rosenbloom J., and Mecham R.P. Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly. Biochem. J. 318 Pt 1 (1996) 149-155
    • (1996) Biochem. J. , vol.318 , Issue.PART 1 , pp. 149-155
    • Brown-Augsburger, P.1    Broekelmann, T.2    Rosenbloom, J.3    Mecham, R.P.4
  • 8
    • 33748183184 scopus 로고    scopus 로고
    • Gene loss and evolutionary rates following whole-genome duplication in teleost fishes
    • Brunet F.G., et al. Gene loss and evolutionary rates following whole-genome duplication in teleost fishes. Mol. Biol. Evol. 23 (2006) 1808-1816
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 1808-1816
    • Brunet, F.G.1
  • 10
    • 0027742514 scopus 로고
    • Structure, chromosomal localization, and expression pattern of the murine Magp gene
    • Chen Y., Faraco J., Yin W., Germiller J., Francke U., and Bonadio J. Structure, chromosomal localization, and expression pattern of the murine Magp gene. J. Biol. Chem. 268 (1993) 27381-27389
    • (1993) J. Biol. Chem. , vol.268 , pp. 27381-27389
    • Chen, Y.1    Faraco, J.2    Yin, W.3    Germiller, J.4    Francke, U.5    Bonadio, J.6
  • 11
    • 33646809625 scopus 로고    scopus 로고
    • Functional analysis of zebrafish microfibril-associated glycoprotein-1 (Magp1) in vivo reveals roles for microfibrils in vascular development and function
    • Chen E., Larson J.D., and Ekker S.C. Functional analysis of zebrafish microfibril-associated glycoprotein-1 (Magp1) in vivo reveals roles for microfibrils in vascular development and function. Blood 107 (2006) 4364-4374
    • (2006) Blood , vol.107 , pp. 4364-4374
    • Chen, E.1    Larson, J.D.2    Ekker, S.C.3
  • 12
    • 33751009077 scopus 로고    scopus 로고
    • Sequences and domain structures of mammalian, avian, amphibian and teleost tropoelastins: clues to the evolutionary history of elastins
    • Chung M.I., Miao M., Stahl R.J., Chan E., Parkinson J., and Keeley F.W. Sequences and domain structures of mammalian, avian, amphibian and teleost tropoelastins: clues to the evolutionary history of elastins. Matrix Biol. 25 (2006) 492-504
    • (2006) Matrix Biol. , vol.25 , pp. 492-504
    • Chung, M.I.1    Miao, M.2    Stahl, R.J.3    Chan, E.4    Parkinson, J.5    Keeley, F.W.6
  • 13
    • 3242812775 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-1 binding to tropoelastin: multiple binding sites and the role of divalent cations
    • Clarke A.W., and Weiss A.S. Microfibril-associated glycoprotein-1 binding to tropoelastin: multiple binding sites and the role of divalent cations. Eur. J. Biochem. 271 (2004) 3085-3090
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3085-3090
    • Clarke, A.W.1    Weiss, A.S.2
  • 14
    • 38449119517 scopus 로고    scopus 로고
    • Gene duplication: a drive for phenotypic diversity and cause of human disease
    • Conrad B., and Antonarakis S.E. Gene duplication: a drive for phenotypic diversity and cause of human disease. Annu. Rev. Genomics. Hum. Genet. 8 (2007) 17-35
    • (2007) Annu. Rev. Genomics. Hum. Genet. , vol.8 , pp. 17-35
    • Conrad, B.1    Antonarakis, S.E.2
  • 16
    • 0027397525 scopus 로고
    • Elastic arteries in a primitive vertebrate - mechanics of the lamprey ventral aorta
    • Demont M.E., and Wright G.M. Elastic arteries in a primitive vertebrate - mechanics of the lamprey ventral aorta. Experientia 49 (1993) 43-46
    • (1993) Experientia , vol.49 , pp. 43-46
    • Demont, M.E.1    Wright, G.M.2
  • 18
    • 33846818777 scopus 로고    scopus 로고
    • A combined empirical and mechanistic codon model
    • Doron-Faigenboim A., and Pupko T. A combined empirical and mechanistic codon model. Mol. Biol. Evol. 24 (2007) 388-397
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 388-397
    • Doron-Faigenboim, A.1    Pupko, T.2
  • 19
    • 33745268919 scopus 로고    scopus 로고
    • Sonic Hedgehog, a key development gene, experienced intensified molecular evolution in primates
    • Dorus S., et al. Sonic Hedgehog, a key development gene, experienced intensified molecular evolution in primates. Hum. Mol. Genet. 15 (2006) 2031-2037
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2031-2037
    • Dorus, S.1
  • 20
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O., Brunak S., von Heijne G., and Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat. Protoc. 2 (2007) 953-971
    • (2007) Nat. Protoc. , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 21
    • 0028904634 scopus 로고
    • Characterization of the human gene for microfibril-associated glycoprotein (MFAP2), assignment to chromosome 1p36.1-p35, and linkage to D1S170
    • Faraco J., Bashir M., Rosenbloom J., and Francke U. Characterization of the human gene for microfibril-associated glycoprotein (MFAP2), assignment to chromosome 1p36.1-p35, and linkage to D1S170. Genomics 25 (1995) 630-637
    • (1995) Genomics , vol.25 , pp. 630-637
    • Faraco, J.1    Bashir, M.2    Rosenbloom, J.3    Francke, U.4
  • 22
    • 0347356449 scopus 로고    scopus 로고
    • Selection on coding regions determined Hox7 genes evolution
    • Fares M.A., Bezemer D., Moya A., and Marin I. Selection on coding regions determined Hox7 genes evolution. Mol. Biol. Evol. 20 (2003) 2104-2112
    • (2003) Mol. Biol. Evol. , vol.20 , pp. 2104-2112
    • Fares, M.A.1    Bezemer, D.2    Moya, A.3    Marin, I.4
  • 24
    • 0035011427 scopus 로고    scopus 로고
    • Function-structure relationship of elastic arteries in evolution: from microfibrils to elastin and elastic fibres
    • Faury G. Function-structure relationship of elastic arteries in evolution: from microfibrils to elastin and elastic fibres. Pathol. Biol. (Paris). 49 (2001) 310-325
    • (2001) Pathol. Biol. (Paris). , vol.49 , pp. 310-325
    • Faury, G.1
  • 25
    • 0000461280 scopus 로고
    • Confidence-limits on phylogenies - an approach using the bootstrap
    • Felsenstein J. Confidence-limits on phylogenies - an approach using the bootstrap. Evolution 39 (1985) 783-791
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 26
    • 0030930661 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the alpha3(VI) chain of type VI collagen
    • Finnis M.L., and Gibson M.A. Microfibril-associated glycoprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the alpha3(VI) chain of type VI collagen. J. Biol. Chem. 272 (1997) 22817-22823
    • (1997) J. Biol. Chem. , vol.272 , pp. 22817-22823
    • Finnis, M.L.1    Gibson, M.A.2
  • 27
    • 0034052885 scopus 로고    scopus 로고
    • Organization of the mouse microfibril-associated glycoprotein-2 (MAGP-2) gene
    • Frankfater C., et al. Organization of the mouse microfibril-associated glycoprotein-2 (MAGP-2) gene. Mamm. Genome 11 (2000) 191-195
    • (2000) Mamm. Genome , vol.11 , pp. 191-195
    • Frankfater, C.1
  • 28
    • 33750932315 scopus 로고    scopus 로고
    • Coevolution, modularity and human disease
    • Fraser H.B. Coevolution, modularity and human disease. Curr. Opin. Genet. Dev. 16 (2006) 637-644
    • (2006) Curr. Opin. Genet. Dev. , vol.16 , pp. 637-644
    • Fraser, H.B.1
  • 29
    • 0025887137 scopus 로고
    • Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils
    • Gibson M.A., Sandberg L.B., Grosso L.E., and Cleary E.G. Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils. J. Biol. Chem. 266 (1991) 7596-7601
    • (1991) J. Biol. Chem. , vol.266 , pp. 7596-7601
    • Gibson, M.A.1    Sandberg, L.B.2    Grosso, L.E.3    Cleary, E.G.4
  • 30
    • 0030021441 scopus 로고    scopus 로고
    • Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25)
    • Gibson M.A., et al. Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25). J. Biol. Chem. 271 (1996) 1096-1103
    • (1996) J. Biol. Chem. , vol.271 , pp. 1096-1103
    • Gibson, M.A.1
  • 31
    • 0033532072 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-2 specifically interacts with a range of bovine and human cell types via alphaVbeta3 integrin
    • Gibson M.A., Leavesley D.I., and Ashman L.K. Microfibril-associated glycoprotein-2 specifically interacts with a range of bovine and human cell types via alphaVbeta3 integrin. J. Biol. Chem. 274 (1999) 13060-13065
    • (1999) J. Biol. Chem. , vol.274 , pp. 13060-13065
    • Gibson, M.A.1    Leavesley, D.I.2    Ashman, L.K.3
  • 32
    • 0020402387 scopus 로고
    • Exaptation - a missing term in the science of form
    • Gould S.J., and Vrba E.S. Exaptation - a missing term in the science of form. Paleobiology 8 (1982) 4-15
    • (1982) Paleobiology , vol.8 , pp. 4-15
    • Gould, S.J.1    Vrba, E.S.2
  • 33
    • 0032728408 scopus 로고    scopus 로고
    • Statistical methods for testing functional divergence after gene duplication
    • Gu X. Statistical methods for testing functional divergence after gene duplication. Mol. Biol. Evol. 16 (1999) 1664-1674
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 1664-1674
    • Gu, X.1
  • 34
    • 0035061686 scopus 로고    scopus 로고
    • Maximum-likelihood approach for gene family evolution under functional divergence
    • Gu X. Maximum-likelihood approach for gene family evolution under functional divergence. Mol. Biol. Evol. 18 (2001) 453-464
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 453-464
    • Gu, X.1
  • 35
    • 33748784344 scopus 로고    scopus 로고
    • A simple statistical method for estimating type-II (cluster-specific) functional divergence of protein sequences
    • Gu X. A simple statistical method for estimating type-II (cluster-specific) functional divergence of protein sequences. Mol. Biol. Evol. 23 (2006) 1937-1945
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 1937-1945
    • Gu, X.1
  • 36
    • 0036205440 scopus 로고    scopus 로고
    • DIVERGE: phylogeny-based analysis for functional-structural divergence of a protein family
    • Gu X., and Vander Velden K. DIVERGE: phylogeny-based analysis for functional-structural divergence of a protein family. Bioinformatics 18 (2002) 500-501
    • (2002) Bioinformatics , vol.18 , pp. 500-501
    • Gu, X.1    Vander Velden, K.2
  • 37
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl. Acids Symp. Ser. 41 (1999) 95-98
    • (1999) Nucl. Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 38
    • 0030447195 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-1 (MAGP-1) is specifically located on the beads of the beaded-filament structure for fibrillin-containing microfibrils as visualized by the rotary shadowing technique
    • Henderson M., Polewski R., Fanning J.C., and Gibson M.A. Microfibril-associated glycoprotein-1 (MAGP-1) is specifically located on the beads of the beaded-filament structure for fibrillin-containing microfibrils as visualized by the rotary shadowing technique. J. Histochem. Cytochem. 44 (1996) 1389-1397
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 1389-1397
    • Henderson, M.1    Polewski, R.2    Fanning, J.C.3    Gibson, M.A.4
  • 39
    • 46449117597 scopus 로고    scopus 로고
    • The amphioxus genome illuminates vertebrate origins and cephalochordate biology
    • Holland L.Z., et al. The amphioxus genome illuminates vertebrate origins and cephalochordate biology. Genome Res. 18 (2008) 1100-1111
    • (2008) Genome Res. , vol.18 , pp. 1100-1111
    • Holland, L.Z.1
  • 41
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones D.T., Taylor W.R., and Thornton J.M. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8 (1992) 275-282
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 42
    • 34648816680 scopus 로고    scopus 로고
    • The 2R hypothesis: an update
    • Kasahara M. The 2R hypothesis: an update. Curr. Opin. Immunol. 19 (2007) 547-552
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 547-552
    • Kasahara, M.1
  • 43
    • 0017368336 scopus 로고
    • Preponderance of synonymous changes as evidence for the neutral theory of molecular evolution
    • Kimura M. Preponderance of synonymous changes as evidence for the neutral theory of molecular evolution. Nature 267 (1977) 275-276
    • (1977) Nature , vol.267 , pp. 275-276
    • Kimura, M.1
  • 45
    • 0034921432 scopus 로고    scopus 로고
    • Evolutionary analysis of vertebrate Notch genes
    • Kortschak R.D., Tamme R., and Lardelli M. Evolutionary analysis of vertebrate Notch genes. Dev. Genes Evol. 211 (2001) 350-354
    • (2001) Dev. Genes Evol. , vol.211 , pp. 350-354
    • Kortschak, R.D.1    Tamme, R.2    Lardelli, M.3
  • 46
    • 0030623944 scopus 로고    scopus 로고
    • Two methods for improving performance of an HMM and their application for gene finding
    • Gaasterland T.e.a. (Ed), AAAI Press, Menlo Park, CA
    • Krogh A. Two methods for improving performance of an HMM and their application for gene finding. In: Gaasterland T.e.a. (Ed). Proc. of Fifth Int. Conf. on Intelligent Systems for Molecular Biology (1997), AAAI Press, Menlo Park, CA 179-186
    • (1997) Proc. of Fifth Int. Conf. on Intelligent Systems for Molecular Biology , pp. 179-186
    • Krogh, A.1
  • 47
    • 0032580152 scopus 로고    scopus 로고
    • A molecular timescale for vertebrate evolution
    • Kumar S., and Hedges S.B. A molecular timescale for vertebrate evolution. Nature 392 (1998) 917-920
    • (1998) Nature , vol.392 , pp. 917-920
    • Kumar, S.1    Hedges, S.B.2
  • 48
    • 33846978751 scopus 로고    scopus 로고
    • Microfibril-associated MAGP-2 stimulates elastic fiber assembly
    • Lemaire R., Bayle J., Mecham R.P., and Lafyatis R. Microfibril-associated MAGP-2 stimulates elastic fiber assembly. J. Biol. Chem. 282 (2006) 800-808
    • (2006) J. Biol. Chem. , vol.282 , pp. 800-808
    • Lemaire, R.1    Bayle, J.2    Mecham, R.P.3    Lafyatis, R.4
  • 50
    • 33644872117 scopus 로고    scopus 로고
    • Evolutionary origins of the endocannabinoid system
    • McPartland J.M., Matias I., Di Marzo V., and Glass M. Evolutionary origins of the endocannabinoid system. Gene 370 (2006) 64-74
    • (2006) Gene , vol.370 , pp. 64-74
    • McPartland, J.M.1    Matias, I.2    Di Marzo, V.3    Glass, M.4
  • 51
    • 33744523404 scopus 로고    scopus 로고
    • Microfibrillar proteins MAGP-1 and MAGP-2 induce Notch1 extracellular domain dissociation and receptor activation
    • Miyamoto A., Lau R., Hein P.W., Shipley J.M., and Weinmaster G. Microfibrillar proteins MAGP-1 and MAGP-2 induce Notch1 extracellular domain dissociation and receptor activation. J. Biol. Chem. 281 (2006) 10089-10097
    • (2006) J. Biol. Chem. , vol.281 , pp. 10089-10097
    • Miyamoto, A.1    Lau, R.2    Hein, P.W.3    Shipley, J.M.4    Weinmaster, G.5
  • 52
    • 20144377499 scopus 로고    scopus 로고
    • The extracellular matrix protein MAGP-2 interacts with Jagged1 and induces its shedding from the cell surface
    • Nehring L.C., Miyamoto A., Hein P.W., Weinmaster G., and Shipley J.M. The extracellular matrix protein MAGP-2 interacts with Jagged1 and induces its shedding from the cell surface. J. Biol. Chem. 280 (2005) 20349-20355
    • (2005) J. Biol. Chem. , vol.280 , pp. 20349-20355
    • Nehring, L.C.1    Miyamoto, A.2    Hein, P.W.3    Weinmaster, G.4    Shipley, J.M.5
  • 54
    • 34447300950 scopus 로고    scopus 로고
    • Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization
    • Putnam N.H., et al. Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization. Science 317 (2007) 86-94
    • (2007) Science , vol.317 , pp. 86-94
    • Putnam, N.H.1
  • 55
    • 34848842170 scopus 로고    scopus 로고
    • Fibrillin-rich microfibrils: structural determinants of morphogenetic and homeostatic events
    • Ramirez F., and Dietz H.C. Fibrillin-rich microfibrils: structural determinants of morphogenetic and homeostatic events. J. Cell. Physiol. 213 (2007) 326-330
    • (2007) J. Cell. Physiol. , vol.213 , pp. 326-330
    • Ramirez, F.1    Dietz, H.C.2
  • 56
    • 0027306001 scopus 로고
    • Specific truncations of Drosophila Notch define dominant activated and dominant negative forms of the receptor
    • Rebay I., Fehon R.G., and Artavanis-Tsakonas S. Specific truncations of Drosophila Notch define dominant activated and dominant negative forms of the receptor. Cell 74 (1993) 319-329
    • (1993) Cell , vol.74 , pp. 319-329
    • Rebay, I.1    Fehon, R.G.2    Artavanis-Tsakonas, S.3
  • 57
    • 0029063160 scopus 로고
    • An extracellular matrix protein of jellyfish homologous to mammalian fibrillins forms different fibrils depending on the life stage of the animal
    • Reber-Muller S., Spissinger T., Schuchert P., Spring J., and Schmid V. An extracellular matrix protein of jellyfish homologous to mammalian fibrillins forms different fibrils depending on the life stage of the animal. Dev. Biol. 169 (1995) 662-672
    • (1995) Dev. Biol. , vol.169 , pp. 662-672
    • Reber-Muller, S.1    Spissinger, T.2    Schuchert, P.3    Spring, J.4    Schmid, V.5
  • 58
    • 0034017021 scopus 로고    scopus 로고
    • The molecular genetics of Marfan syndrome and related microfibrillopathies
    • Robinson P.N., and Godfrey M. The molecular genetics of Marfan syndrome and related microfibrillopathies. J. Med. Genet. 37 (2000) 9-25
    • (2000) J. Med. Genet. , vol.37 , pp. 9-25
    • Robinson, P.N.1    Godfrey, M.2
  • 59
    • 0034129663 scopus 로고    scopus 로고
    • RRTree: relative-rate tests between groups of sequences on a phylogenetic tree
    • Robinson-Rechavi M., and Huchon D. RRTree: relative-rate tests between groups of sequences on a phylogenetic tree. Bioinformatics 16 (2000) 296-297
    • (2000) Bioinformatics , vol.16 , pp. 296-297
    • Robinson-Rechavi, M.1    Huchon, D.2
  • 60
    • 0033744203 scopus 로고    scopus 로고
    • The structure and organization of lamprin genes: multiple-copy genes with alternative splicing and convergent evolution with insect structural proteins
    • Robson P., Wright G.M., Youson J.H., and Keeley F.W. The structure and organization of lamprin genes: multiple-copy genes with alternative splicing and convergent evolution with insect structural proteins. Mol. Biol. Evol. 17 (2000) 1739-1752
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 1739-1752
    • Robson, P.1    Wright, G.M.2    Youson, J.H.3    Keeley, F.W.4
  • 61
    • 58149149757 scopus 로고    scopus 로고
    • Developmental constraints on vertebrate genome evolution
    • Roux J., and Robinson-Rechavi M. Developmental constraints on vertebrate genome evolution. PLoS Genet. 4 (2008) e1000311
    • (2008) PLoS Genet. , vol.4
    • Roux, J.1    Robinson-Rechavi, M.2
  • 62
    • 0026660413 scopus 로고
    • A simple method for estimating and testing minimum-evolution trees
    • Rzhetsky A., and Nei M. A simple method for estimating and testing minimum-evolution trees. Mol. Biol. Evol. 9 (1992) 945-967
    • (1992) Mol. Biol. Evol. , vol.9 , pp. 945-967
    • Rzhetsky, A.1    Nei, M.2
  • 63
    • 0020687590 scopus 로고
    • The evolution of elastin: correlation of functional properties with protein structure and phylogenetic distribution
    • Sage H. The evolution of elastin: correlation of functional properties with protein structure and phylogenetic distribution. Comp. Biochem. Physiol., B 74 (1983) 373-380
    • (1983) Comp. Biochem. Physiol., B , vol.74 , pp. 373-380
    • Sage, H.1
  • 64
    • 0018657591 scopus 로고
    • Studies on the evolution of elastin-I. Phylogenetic distribution
    • Sage H., and Gray W.R. Studies on the evolution of elastin-I. Phylogenetic distribution. Comp. Biochem. Physiol., B. 64 (1979) 313-327
    • (1979) Comp. Biochem. Physiol., B. , vol.64 , pp. 313-327
    • Sage, H.1    Gray, W.R.2
  • 65
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., and Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4 (1987) 406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 66
    • 0033752306 scopus 로고    scopus 로고
    • Revised genomic structure of the human MAGP1 gene and identification of alternate transcripts in human and mouse tissues
    • Segade F., Broekelmann T.J., Pierce R.A., and Mecham R.P. Revised genomic structure of the human MAGP1 gene and identification of alternate transcripts in human and mouse tissues. Matrix Biol. 19 (2000) 671-682
    • (2000) Matrix Biol. , vol.19 , pp. 671-682
    • Segade, F.1    Broekelmann, T.J.2    Pierce, R.A.3    Mecham, R.P.4
  • 67
    • 28444434743 scopus 로고    scopus 로고
    • Regulatory elements of microfibril-associated glycoprotein-1 gene expression in muscle cells
    • Segade F., and Mecham R.P. Regulatory elements of microfibril-associated glycoprotein-1 gene expression in muscle cells. Biochim. Biophys. Acta 1731 (2005) 215-224
    • (2005) Biochim. Biophys. Acta , vol.1731 , pp. 215-224
    • Segade, F.1    Mecham, R.P.2
  • 68
    • 0037192804 scopus 로고    scopus 로고
    • Identification of a matrix-binding domain in MAGP1 and MAGP2 and intracellular localization of alternative splice forms
    • Segade F., Trask B.C., Broekelmann T.J., Pierce R.A., and Mecham R.P. Identification of a matrix-binding domain in MAGP1 and MAGP2 and intracellular localization of alternative splice forms. J. Biol. Chem. 277 (2002) 11050-11057
    • (2002) J. Biol. Chem. , vol.277 , pp. 11050-11057
    • Segade, F.1    Trask, B.C.2    Broekelmann, T.J.3    Pierce, R.A.4    Mecham, R.P.5
  • 70
    • 0035943685 scopus 로고    scopus 로고
    • Soluble Jagged 1 represses the function of its transmembrane form to induce the formation of the Src-dependent chord-like phenotype
    • Small D., et al. Soluble Jagged 1 represses the function of its transmembrane form to induce the formation of the Src-dependent chord-like phenotype. J. Biol. Chem. 276 (2001) 32022-32030
    • (2001) J. Biol. Chem. , vol.276 , pp. 32022-32030
    • Small, D.1
  • 71
    • 33750403801 scopus 로고    scopus 로고
    • RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models
    • Stamatakis A. RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models. Bioinformatics 22 (2006) 2688-2690
    • (2006) Bioinformatics , vol.22 , pp. 2688-2690
    • Stamatakis, A.1
  • 72
    • 34547567977 scopus 로고    scopus 로고
    • Selecton 2007: advanced models for detecting positive and purifying selection using a Bayesian inference approach
    • Stern A., Doron-Faigenboim A., Erez E., Martz E., Bacharach E., and Pupko T. Selecton 2007: advanced models for detecting positive and purifying selection using a Bayesian inference approach. Nucleic Acids Res. 35 (2007) W506-W511
    • (2007) Nucleic Acids Res. , vol.35
    • Stern, A.1    Doron-Faigenboim, A.2    Erez, E.3    Martz, E.4    Bacharach, E.5    Pupko, T.6
  • 73
    • 0037230001 scopus 로고    scopus 로고
    • Pervasive adaptive evolution in mammalian fertilization proteins
    • Swanson W.J., Nielsen R., and Yang Q. Pervasive adaptive evolution in mammalian fertilization proteins. Mol. Biol. Evol. 20 (2003) 18-20
    • (2003) Mol. Biol. Evol. , vol.20 , pp. 18-20
    • Swanson, W.J.1    Nielsen, R.2    Yang, Q.3
  • 74
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., and Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24 (2007) 1596-1599
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 75
    • 34547585235 scopus 로고    scopus 로고
    • Phylemon: a suite of web tools for molecular evolution, phylogenetics and phylogenomics
    • Tarraga J., et al. Phylemon: a suite of web tools for molecular evolution, phylogenetics and phylogenomics. Nucleic Acids Res. 35 (2007) W38-42
    • (2007) Nucleic Acids Res. , vol.35
    • Tarraga, J.1
  • 76
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. 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 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 78
    • 0029878263 scopus 로고    scopus 로고
    • Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone
    • Tudor J.E., Pallaghy P.K., Pennington M.W., and Norton R.S. Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone. Nat. Struct. Biol. 3 (1996) 317-320
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 317-320
    • Tudor, J.E.1    Pallaghy, P.K.2    Pennington, M.W.3    Norton, R.S.4
  • 79
    • 1242274629 scopus 로고    scopus 로고
    • Major events in the genome evolution of vertebrates: paranome age and size differ considerably between ray-finned fishes and land vertebrates
    • Vandepoele K., De Vos W., Taylor J.S., Meyer A., and Van de Peer Y. Major events in the genome evolution of vertebrates: paranome age and size differ considerably between ray-finned fishes and land vertebrates. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 1638-1643
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1638-1643
    • Vandepoele, K.1    De Vos, W.2    Taylor, J.S.3    Meyer, A.4    Van de Peer, Y.5
  • 80
    • 34247342594 scopus 로고    scopus 로고
    • Survey sequencing and comparative analysis of the elephant shark (Callorhinchus milii) genome
    • Venkatesh B., et al. Survey sequencing and comparative analysis of the elephant shark (Callorhinchus milii) genome. PLoS Biol. 5 (2007) e101
    • (2007) PLoS Biol. , vol.5
    • Venkatesh, B.1
  • 82
    • 54449085747 scopus 로고    scopus 로고
    • Deficiency in microfibril-associated glycoprotein-1 leads to complex phenotypes in multiple organ systems
    • Weinbaum J.S., et al. Deficiency in microfibril-associated glycoprotein-1 leads to complex phenotypes in multiple organ systems. J. Biol. Chem. 283 (2008) 25533-25543
    • (2008) J. Biol. Chem. , vol.283 , pp. 25533-25543
    • Weinbaum, J.S.1
  • 83
    • 2542432055 scopus 로고    scopus 로고
    • Identification of a major microfibril-associated glycoprotein-1-binding domain in fibrillin-2
    • Werneck C.C., et al. Identification of a major microfibril-associated glycoprotein-1-binding domain in fibrillin-2. J. Biol. Chem. 279 (2004) 23045-23051
    • (2004) J. Biol. Chem. , vol.279 , pp. 23045-23051
    • Werneck, C.C.1
  • 84
    • 43249125237 scopus 로고    scopus 로고
    • Mice lacking the extracellular matrix protein MAGP1 display delayed thrombotic occlusion following vessel injury
    • Werneck C.C., et al. Mice lacking the extracellular matrix protein MAGP1 display delayed thrombotic occlusion following vessel injury. Blood 111 (2008) 4137-4144
    • (2008) Blood , vol.111 , pp. 4137-4144
    • Werneck, C.C.1
  • 86
    • 0015363136 scopus 로고
    • The isolation of pure cholinergic synaptic vesicles from the electric organs of elasmobranch fish of the family Torpedinidae
    • Whittaker V.P., Essman W.B., and Dowe G.H. The isolation of pure cholinergic synaptic vesicles from the electric organs of elasmobranch fish of the family Torpedinidae. Biochem. J. 128 (1972) 833-845
    • (1972) Biochem. J. , vol.128 , pp. 833-845
    • Whittaker, V.P.1    Essman, W.B.2    Dowe, G.H.3
  • 87
    • 0033639150 scopus 로고    scopus 로고
    • Statistical methods for detecting molecular adaptation
    • Yang Z., and Bielawski J.P. Statistical methods for detecting molecular adaptation. Trends Ecol. Evol. 15 (2000) 496-503
    • (2000) Trends Ecol. Evol. , vol.15 , pp. 496-503
    • Yang, Z.1    Bielawski, J.P.2
  • 88
    • 0034097381 scopus 로고    scopus 로고
    • Codon-substitution models for heterogeneous selection pressure at amino acid sites
    • Yang Z., Nielsen R., Goldman N., and Pedersen A.M. Codon-substitution models for heterogeneous selection pressure at amino acid sites. Genetics 155 (2000) 431-449
    • (2000) Genetics , vol.155 , pp. 431-449
    • Yang, Z.1    Nielsen, R.2    Goldman, N.3    Pedersen, A.M.4


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