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Volumn 456, Issue 1-2, 2010, Pages 1-14

CRTAC1 homolog proteins are conserved from cyanobacteria to man and secreted by the teleost fish pituitary gland

Author keywords

Propeller; Cartilage acidic protein 1; EGF like calcium binding domain; Extracellular matrix; Integrin

Indexed keywords

ALPHA INTEGRIN; CARTILAGE ACIDIC PROTEIN 1; CARTILAGE ACIDIC PROTEIN 2; SCLEROPROTEIN; UNCLASSIFIED DRUG;

EID: 77951090807     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2010.02.003     Document Type: Article
Times cited : (12)

References (41)
  • 2
    • 0036295210 scopus 로고    scopus 로고
    • Molecular analysis of expansion, differentiation, and growth factor treatment of human chondrocytes identifies differentiation markers and growth-related genes
    • Benz K., Breit S., Lukoschek M., Mau H., Richter W. Molecular analysis of expansion, differentiation, and growth factor treatment of human chondrocytes identifies differentiation markers and growth-related genes. Biochem. Biophys. Res. Commun. 2002, 293:284-292.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 284-292
    • Benz, K.1    Breit, S.2    Lukoschek, M.3    Mau, H.4    Richter, W.5
  • 4
    • 0037251969 scopus 로고    scopus 로고
    • The Ribosomal Database Project (RDP-II): previewing a new autoaligner that allows regular updates and the new prokaryotic taxonomy
    • Cole J.R., et al. The Ribosomal Database Project (RDP-II): previewing a new autoaligner that allows regular updates and the new prokaryotic taxonomy. Nucleic Acids Res. 2003, 31:442-443.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 442-443
    • Cole, J.R.1
  • 5
    • 0242534101 scopus 로고    scopus 로고
    • Marfan Database (third edition): new mutations and new routines for the software
    • Collod-Beroud G., et al. Marfan Database (third edition): new mutations and new routines for the software. Nucleic Acids Res. 1998, 26:229-233.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 229-233
    • Collod-Beroud, G.1
  • 8
    • 3042688356 scopus 로고    scopus 로고
    • Proteomic analysis of multiple sclerosis cerebrospinal fluid
    • Hammack B.N., et al. Proteomic analysis of multiple sclerosis cerebrospinal fluid. Mult. Scler. 2004, 10:245-260.
    • (2004) Mult. Scler. , vol.10 , pp. 245-260
    • Hammack, B.N.1
  • 10
    • 0035145187 scopus 로고    scopus 로고
    • Evolution of the integrin Α and Β protein families
    • Hughes A.L. Evolution of the integrin Α and Β protein families. J. Mol. Evol. 2001, 52:63-72.
    • (2001) J. Mol. Evol. , vol.52 , pp. 63-72
    • Hughes, A.L.1
  • 11
    • 7244259101 scopus 로고    scopus 로고
    • Genome duplication in the teleost fish Tetraodon nigroviridis reveals the early vertebrate proto-karyotype
    • Jaillon O., et al. Genome duplication in the teleost fish Tetraodon nigroviridis reveals the early vertebrate proto-karyotype. Nature 2004, 431:946-957.
    • (2004) Nature , vol.431 , pp. 946-957
    • Jaillon, O.1
  • 12
    • 0035941265 scopus 로고    scopus 로고
    • Amino acid residues in the ΑIIb subunit that are critical for ligand binding to integrin ΑIIbΒ3 are clustered in the Β-propeller model
    • Kamata T., Tieu K.K., Irie A., Springer T.A., Takada Y. Amino acid residues in the ΑIIb subunit that are critical for ligand binding to integrin ΑIIbΒ3 are clustered in the Β-propeller model. J. Biol. Chem. 2001, 276:44275-44283.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44275-44283
    • Kamata, T.1    Tieu, K.K.2    Irie, A.3    Springer, T.A.4    Takada, Y.5
  • 13
    • 0002063405 scopus 로고
    • Role of prolactin and somatolactin in calcium regulation in fish
    • Kaneko T., Hirano T. Role of prolactin and somatolactin in calcium regulation in fish. J. Exp. Biol. 1993, 184:31-45.
    • (1993) J. Exp. Biol. , vol.184 , pp. 31-45
    • Kaneko, T.1    Hirano, T.2
  • 14
    • 0036021444 scopus 로고    scopus 로고
    • Emerging links between initiation of translation and human diseases
    • Kozak M. Emerging links between initiation of translation and human diseases. Mamm. Genome 2002, 13:401-410.
    • (2002) Mamm. Genome , vol.13 , pp. 401-410
    • Kozak, M.1
  • 15
    • 0142124263 scopus 로고    scopus 로고
    • Gene loss, protein sequence divergence, gene dispensability, expression level, and interactivity are correlated in eukaryotic evolution
    • Krylov D.M., Wolf Y.I., Rogozin I.B., Koonin E.V. Gene loss, protein sequence divergence, gene dispensability, expression level, and interactivity are correlated in eukaryotic evolution. Genome Res. 2003, 13:2229-2235.
    • (2003) Genome Res. , vol.13 , pp. 2229-2235
    • Krylov, D.M.1    Wolf, Y.I.2    Rogozin, I.B.3    Koonin, E.V.4
  • 16
    • 0003421005 scopus 로고    scopus 로고
    • Sinauer Associates, Sunderland, MA
    • Li W.-H. Molecular Evolution 1997, Sinauer Associates, Sunderland, MA.
    • (1997) Molecular Evolution
    • Li, W.-H.1
  • 17
    • 34249794029 scopus 로고    scopus 로고
    • A genorne-wide analysis of biomineralization-related proteins in the sea urchin Strongylocentrotus purpuratus
    • Livingston B.T., et al. A genorne-wide analysis of biomineralization-related proteins in the sea urchin Strongylocentrotus purpuratus. Dev. Biol. 2006, 300:335-348.
    • (2006) Dev. Biol. , vol.300 , pp. 335-348
    • Livingston, B.T.1
  • 19
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai K., Horton P. PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 1999, 24:34-36.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 20
    • 12444292075 scopus 로고    scopus 로고
    • Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids
    • Nakamura Y., et al. Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids. DNA Res. 2003, 10:137-145.
    • (2003) DNA Res. , vol.10 , pp. 137-145
    • Nakamura, Y.1
  • 21
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 1997, 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 22
    • 0038270852 scopus 로고    scopus 로고
    • Comparative genomics of Physcomitrella patens gametophytic transcriptome and Arabidopsis thaliana: implication for land plant evolution
    • Nishiyama T., et al. Comparative genomics of Physcomitrella patens gametophytic transcriptome and Arabidopsis thaliana: implication for land plant evolution. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:8007-8012.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 8007-8012
    • Nishiyama, T.1
  • 23
    • 0027473885 scopus 로고
    • A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors
    • Peitsch M.C., Jongeneel C.V. A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors. Int. Immunol. 1993, 5:233-238.
    • (1993) Int. Immunol. , vol.5 , pp. 233-238
    • Peitsch, M.C.1    Jongeneel, C.V.2
  • 25
    • 15344347625 scopus 로고    scopus 로고
    • Isolation and characterization of piscine osteonectin and downregulation of its expression by parathyroid hormone-related protein
    • Redruello B., et al. Isolation and characterization of piscine osteonectin and downregulation of its expression by parathyroid hormone-related protein. J. Bone Miner. Res. 2005, 20:682-692.
    • (2005) J. Bone Miner. Res. , vol.20 , pp. 682-692
    • Redruello, B.1
  • 26
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987, 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 28
    • 0033306810 scopus 로고    scopus 로고
    • Identification of transthyretin in fish (Sparus aurata): cDNA cloning and characterisation
    • Santos C.R.A., Power D.M. Identification of transthyretin in fish (Sparus aurata): cDNA cloning and characterisation. Endocrinology 1999, 140:2430-2433.
    • (1999) Endocrinology , vol.140 , pp. 2430-2433
    • Santos, C.R.A.1    Power, D.M.2
  • 29
    • 85047684536 scopus 로고    scopus 로고
    • The moss Physcomitrella patens, now and then
    • Schaefer D.G., Zrÿd J.P. The moss Physcomitrella patens, now and then. Plant Physiol. 2001, 127:1430-1438.
    • (2001) Plant Physiol. , vol.127 , pp. 1430-1438
    • Schaefer, D.G.1    Zrÿd, J.P.2
  • 30
    • 0028307171 scopus 로고
    • Split genes and RNA splicing
    • Sharp P.A. Split genes and RNA splicing. Cell 1994, 77:805-815.
    • (1994) Cell , vol.77 , pp. 805-815
    • Sharp, P.A.1
  • 31
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin Α-subunits into a Β-propeller domain
    • Springer T.A. Folding of the N-terminal, ligand-binding region of integrin Α-subunits into a Β-propeller domain. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:65-72.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 32
    • 0034604295 scopus 로고    scopus 로고
    • 2+ binding Β hairpin loop better resembles integrin sequence motifs than the EF hand
    • 2+ binding Β hairpin loop better resembles integrin sequence motifs than the EF hand. Cell 2000, 102:275-277.
    • (2000) Cell , vol.102 , pp. 275-277
    • Springer, T.A.1    Jing, H.2    Takagi, J.3
  • 33
    • 0035864184 scopus 로고    scopus 로고
    • Chondrocyte expressed protein-68 (CEP-68), a novel human marker gene for cultured chondrocytes
    • Steck E., Benz K., Lorenz H., Loew M., Gress T., Richter W. Chondrocyte expressed protein-68 (CEP-68), a novel human marker gene for cultured chondrocytes. Biochem. J. 2001, 353:169-174.
    • (2001) Biochem. J. , vol.353 , pp. 169-174
    • Steck, E.1    Benz, K.2    Lorenz, H.3    Loew, M.4    Gress, T.5    Richter, W.6
  • 34
    • 33846070018 scopus 로고    scopus 로고
    • Chondrocyte secreted CRTAC1: a glycosylated extracellular matrix molecule of human articular cartilage
    • Steck E., Braun J., Pelttari K., Kadel S., Kalbacher H., Richter W. Chondrocyte secreted CRTAC1: a glycosylated extracellular matrix molecule of human articular cartilage. Matrix Biol. 2007, 26:30-41.
    • (2007) Matrix Biol. , vol.26 , pp. 30-41
    • Steck, E.1    Braun, J.2    Pelttari, K.3    Kadel, S.4    Kalbacher, H.5    Richter, W.6
  • 36
    • 20444451594 scopus 로고    scopus 로고
    • Tracking repeats using significance and transitivity
    • Szklarczyk R., Heringa J. Tracking repeats using significance and transitivity. Bioinformatics 2004, 20(Suppl 1):i311-i317.
    • (2004) Bioinformatics , vol.20 , Issue.SUPPL. 1
    • Szklarczyk, R.1    Heringa, J.2
  • 37
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997, 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 38
    • 0026643364 scopus 로고
    • Homology modelling of integrin EF-hands. Evidence for widespread use of a conserved cation-binding site
    • Tuckwell D.S., Brass A., Humphries M.J. Homology modelling of integrin EF-hands. Evidence for widespread use of a conserved cation-binding site. Biochem. J. 1992, 285(Pt 1):325-331.
    • (1992) Biochem. J. , vol.285 , Issue.PART. 1 , pp. 325-331
    • Tuckwell, D.S.1    Brass, A.2    Humphries, M.J.3
  • 39
    • 0025946375 scopus 로고
    • Control of calcium regulating hormones in the vertebrates: parathyroid hormone, calcitonin, prolactin and stanniocalcin
    • Wendelaar Bonga S., Pang P. Control of calcium regulating hormones in the vertebrates: parathyroid hormone, calcitonin, prolactin and stanniocalcin. Int. Rev. Cytol. 1991, 128:139-213.
    • (1991) Int. Rev. Cytol. , vol.128 , pp. 139-213
    • Wendelaar Bonga, S.1    Pang, P.2
  • 40
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • Xiao T., Takagi J., Coller B.S., Wang J.H., Springer T.A. Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature 2004, 432:59-67.
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Coller, B.S.3    Wang, J.H.4    Springer, T.A.5
  • 41


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.