메뉴 건너뛰기




Volumn 7, Issue , 2007, Pages

The evolution of the vertebrate metzincins; Insights from Ciona intestinalis and Danio rerio

Author keywords

[No Author keywords available]

Indexed keywords

MEPRIN; METZINCIN; PROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE; UNCLASSIFIED DRUG; ADAM PROTEIN; MATRIX METALLOPROTEINASE; METALLOPROTEINASE; ZEBRAFISH PROTEIN;

EID: 34248549971     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-7-63     Document Type: Article
Times cited : (96)

References (81)
  • 1
    • 33646576168 scopus 로고    scopus 로고
    • Degradomics: Systems biology of the protease web. Pleiotropic roles of MMPs in cancer.
    • 16680573. 10.1007/s10555-006-7890-0
    • Degradomics: systems biology of the protease web. Pleiotropic roles of MMPs in cancer. CM Overall Dean, R.A., Cancer Metastasis Reviews 2006 25 69 75 16680573 10.1007/s10555-006-7890-0
    • (2006) Cancer Metastasis Reviews , vol.25 , pp. 69-75
    • Overall, C.M.1    Dean, R.A.2
  • 2
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the metzincins
    • 8405391. 10.1016/0014-5793(93)80312-I
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the metzincins. W Bode Gomis-Ruth, F-X., Stockler, W., FEBS Letters 1993 331 134 140 8405391 10.1016/0014-5793(93) 80312-I
    • (1993) FEBS Letters , vol.331 , pp. 134-140
    • Bode Gomis-Ruth, W.F.-X.1    Stockler, W.2
  • 3
    • 11244261160 scopus 로고    scopus 로고
    • ADAMS: Key components in EGFR signalling and development
    • 15688065. 10.1038/nrm1548
    • ADAMS: key components in EGFR signalling and development. CP Blobel, Nature Reviews Molecular Cell Biology 2005 6 32 43 15688065 10.1038/nrm1548
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , pp. 32-43
    • Blobel, C.P.1
  • 4
    • 0242710747 scopus 로고    scopus 로고
    • TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity
    • 14623079. 10.1016/S0014-5793(03)01159-1
    • TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity. N Srour Lebel, A., McMahon, S., Fournier, I., Fugere, M., Day, R., Dubois, C.M., FEBS Letters 2003 554 275 283 14623079 10.1016/S0014-5793(03)01159-1
    • (2003) FEBS Letters , vol.554 , pp. 275-283
    • Srour Lebel, N.A.1    McMahon, S.2    Fournier, I.3    Fugere, M.4    Day, R.5    Dubois, C.M.6
  • 7
    • 0033868818 scopus 로고    scopus 로고
    • A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE
    • 10882063. 10.1016/S1097-2765(00)80417-7
    • A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. C Brou Logeat, F., Gupta, N., Bessia, C., LeBail, O., Doedens, J.R., Cumano, A., Roux, P., Black, R.A., Israel, A., Molecular Cell 2000 5 207 216 10882063 10.1016/S1097-2765(00)80417-7
    • (2000) Molecular Cell , vol.5 , pp. 207-216
    • Brou Logeat, C.F.1    Gupta, N.2    Bessia, C.3    Lebail, O.4    Doedens, J.R.5    Cumano, A.6    Roux, P.7    Black, R.A.8    Israel, A.9
  • 8
    • 33749038646 scopus 로고    scopus 로고
    • Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission
    • 16931720. 10.1126/science.1129947
    • Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission. Y Fukata Adesnik, H., Iwanaga, T., Bredt, DS., Nicoll, R.A., Fukata, M., Science 2006 313 1972 1795 16931720 10.1126/science.1129947
    • (2006) Science , vol.313 , pp. 1972-1795
    • Fukata Adesnik, Y.H.1    Iwanaga, T.2    Bredt, D.S.3    Nicoll, R.A.4    Fukata, M.5
  • 9
    • 0031036524 scopus 로고    scopus 로고
    • Molecular cloning of a gene encoding a new type of metalloproteinase- disintegrin family protein with thrombospondin motifs as an inflammation associated gene
    • 8995297. 10.1074/jbc.272.1.556
    • Molecular cloning of a gene encoding a new type of metalloproteinase- disintegrin family protein with thrombospondin motifs as an inflammation associated gene. K Kuno Kanada, N., Nakashima, E., Fujiki, F., Ichimura, F., Matsushima, K., Journal of Biological Chemistry 1997 272 556 562 8995297 10.1074/jbc.272.1.556
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 556-562
    • Kuno Kanada, K.N.1    Nakashima, E.2    Fujiki, F.3    Ichimura, F.4    Matsushima, K.5
  • 10
    • 0037160539 scopus 로고    scopus 로고
    • Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains
    • 11867212. 10.1016/S0378-1119(01)00861-7
    • Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains. S Cal Obaya, A.J., Llamazares, M., Garabaya, C., Quesada, V., Lopez-Otin, C., Gene 2002 283 49 62 11867212 10.1016/S0378-1119(01) 00861-7
    • (2002) Gene , vol.283 , pp. 49-62
    • Cal Obaya, S.A.J.1    Llamazares, M.2    Garabaya, C.3    Quesada, V.4    Lopez-Otin, C.5
  • 11
    • 4143112912 scopus 로고    scopus 로고
    • A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type-1 motifs: The ADAMTS family
    • 10.1016/j.biocel.2004.01.014
    • A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type-1 motifs: the ADAMTS family. SS Apte, The International Journal of Biochemistry and Cell Biology 2004 36 981 985 10.1016/j.biocel.2004. 01.014
    • (2004) The International Journal of Biochemistry and Cell Biology , vol.36 , pp. 981-985
    • Apte, S.S.1
  • 14
    • 0345118901 scopus 로고    scopus 로고
    • ADAMTSL-3/punctin-2, a novel glycoprotein in extracellular matrix related to the ADAMTS family of metalloproteases
    • 14667842. 10.1016/S0945-053X(03)00075-1
    • ADAMTSL-3/punctin-2, a novel glycoprotein in extracellular matrix related to the ADAMTS family of metalloproteases. NG Hall Klentoic, P., Anand-Apte, B., Apte, S.S., Matrix Biology 2003 22 501 510 14667842 10.1016/S0945-053X(03) 00075-1
    • (2003) Matrix Biology , vol.22 , pp. 501-510
    • Hall, N.G.1    Klentoic, P.2    Anand-Apte, B.3    Apte, S.S.4
  • 15
    • 0038043187 scopus 로고    scopus 로고
    • Paired Basic/Furin-like Proprotein Convertase Cleavage of Pro-BMP-1 in the trans-Golgi Network
    • 12637569. 10.1074/jbc.M213021200
    • Paired Basic/Furin-like Proprotein Convertase Cleavage of Pro-BMP-1 in the trans-Golgi Network. M Leighton Kadler, K., Journal of Biological Chemistry 2003 278 18478 18484 12637569 10.1074/jbc.M213021200
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 18478-18484
    • Leighton, M.1    Kadler, K.2
  • 16
    • 33646567450 scopus 로고    scopus 로고
    • Developmental roles of the BMP1/TLD metalloproteinases
    • 10.1002/bdrc.20060
    • Developmental roles of the BMP1/TLD metalloproteinases. G Ge Greenspan, D.S., Birth Defects Research (Part C) 2006 78 47 68 10.1002/bdrc.20060
    • (2006) Birth Defects Research (Part C) , vol.78 , pp. 47-68
    • Greenspan, D.S.1    Ge, G.2
  • 17
    • 0033568003 scopus 로고    scopus 로고
    • Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis
    • 10479448. 10.1006/dbio.1999.9383
    • Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis. IC Scott Blitz, I.L., Pappano, W.N., Imamura, Y., Clark, T.G., Steiglitz, B.M., Thomas, C.L.; Maas, S.A., Takahara, K., Cho, K.W.Y., Greenspan, D.S., Developmental Biology 1999 213 283 300 10479448 10.1006/dbio.1999.9383
    • (1999) Developmental Biology , vol.213 , pp. 283-300
    • Scott, I.C.1    Blitz, I.L.2    Pappano, W.N.3    Imamura, Y.4    Clark, T.G.5    Steiglitz, B.M.6    Thomas, C.L.7    Maas, S.A.8    Takahara, K.9    Cho, K.W.Y.10    Greenspan, D.S.11
  • 18
    • 0037174846 scopus 로고    scopus 로고
    • Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system
    • 12189145. 10.1074/jbc.M206203200
    • Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system. S Rosmann Hahn, D., Lottaz, D., Kruse, M-N., Stocker, W., Sterchi, E.E., Journal of Biological Chemistry 2002 277 40650 40658 12189145 10.1074/jbc.M206203200
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 40650-40658
    • Rosmann Hahn, S.D.1    Lottaz, D.2    Kruse, M.-N.3    Stocker, W.4    Sterchi, E.E.5
  • 19
    • 0027361420 scopus 로고
    • Expression of the alpha subunit of PABA peptide hydrolase (EC 3.4.24.18) in MDCK cells. Synthesis and secretion of an enzymatically inactive homodimer
    • 8262186. 10.1016/0014-5793(93)80422-Q
    • Expression of the alpha subunit of PABA peptide hydrolase (EC 3.4.24.18) in MDCK cells. Synthesis and secretion of an enzymatically inactive homodimer. J Grunberg Dumermuth, E., Eldering, J.A., Sterchi, E.E., FEBS Letters 1993 335 376 379 8262186 10.1016/0014-5793(93)80422-Q
    • (1993) FEBS Letters , vol.335 , pp. 376-379
    • Grunberg Dumermuth, J.E.1    Eldering, J.A.2    Sterchi, E.E.3
  • 20
    • 0029027631 scopus 로고
    • Meprins a and B
    • New York , Academic Press Barrett AJ
    • Meprins A and B. RL Wolz Bond, J.S., Methods Enzymology New York, Academic Press, Barrett AJ, 1995
    • (1995) Methods Enzymology
    • Wolz, R.L.1    Bond, J.S.2
  • 21
    • 0027934376 scopus 로고
    • An old enzyme with a new function: Purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin
    • 8063866. 10.1083/jcb.126.5.1319
    • An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin. GP Kaushal Walker, P.D., Shah, SV., Journal of Cell Biology 1994 126 1319 1327 8063866 10.1083/jcb.126.5.1319
    • (1994) Journal of Cell Biology , vol.126 , pp. 1319-1327
    • Kaushal, G.P.1    Walker, P.D.2    Shah, S.V.3
  • 22
    • 0037622285 scopus 로고    scopus 로고
    • Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro
    • 10620696. 10.1016/S0014-5793(99)01712-3
    • Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro. D Kohler Kruse, M., Stocker, W., Sterchi, E.E., FEBS Letters 2000 465 2 7 10620696 10.1016/S0014-5793(99)01712-3
    • (2000) FEBS Letters , vol.465 , pp. 2-7
    • Kohler Kruse, D.M.1    Stocker, W.2    Sterchi, E.E.3
  • 23
    • 1642373361 scopus 로고    scopus 로고
    • Deletion of the mouse meprin beta metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix
    • Deletion of the mouse meprin beta metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix. JM Crisman Zhang, B., Norman, L.P., Bond, J.S., Journal of Immunology 2004 172 4510 4519
    • (2004) Journal of Immunology , vol.172 , pp. 4510-4519
    • Crisman, J.M.1    Zhang, B.2    Norman, L.P.3    Bond, J.S.4
  • 24
    • 0030273873 scopus 로고    scopus 로고
    • Snake venome metalloproteinases: Structure, function and relationship to the ADAMs family of proteins
    • 9027982. 10.1016/S0041-0101(96)00108-0
    • Snake venome metalloproteinases: structure, function and relationship to the ADAMs family of proteins. LG Jia Simokawa, K-I., Bjarnsason, J.B., Fox, J.W., Toxicon 1996 34 1269 1276 9027982 10.1016/S0041-0101(96)00108-0
    • (1996) Toxicon , vol.34 , pp. 1269-1276
    • Jia, L.G.1    Simokawa, K.-I.2    Bjarnsason, J.B.3    Fox, J.W.4
  • 25
    • 0027683226 scopus 로고
    • Structural biochemistry and activation of matrix metalloproteases
    • 8240832. 10.1016/0955-0674(93)90040-W
    • Structural biochemistry and activation of matrix metalloproteases. DE Kleine Stetler-Stevenson, W.G., Current Opinion in Cell Biology 1993 5 891 897 8240832 10.1016/0955-0674(93)90040-W
    • (1993) Current Opinion in Cell Biology , vol.5 , pp. 891-897
    • Kleiner, D.E.1    Stetler-Stevenson, W.G.2
  • 26
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • 16405877. 10.1016/j.cardiores.2005.12.002
    • Structure and function of matrix metalloproteinases and TIMPs. H Nagase Visse, R., Murphy, G., Cardiovascular Research 2006 69 562 573 16405877 10.1016/j.cardiores.2005.12.002
    • (2006) Cardiovascular Research , vol.69 , pp. 562-573
    • Nagase Visse, H.R.1    Murphy, G.2
  • 28
    • 18144384702 scopus 로고    scopus 로고
    • Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting
    • 15713681. 10.1074/jbc.M500897200
    • Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting. MH Lee Rapti, M., Murphy, G., Journal of Biological Chemistry 2005 280 15967 15975 15713681 10.1074/jbc.M500897200
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 15967-15975
    • Lee, M.H.1    Rapti, M.2    Murphy, G.3
  • 30
    • 0042197340 scopus 로고    scopus 로고
    • TIMP-2 mediated inhibition of angiogenesis: An MMP-independent mechanism
    • 12887919. 10.1016/S0092-8674(03)00551-8
    • TIMP-2 mediated inhibition of angiogenesis: an MMP-independent mechanism. DW Seo Li., H., Guedez, L., Wingfield, P.T., Diaz, T., Salloum, R., Wei, B., Stetler-Stevenson, W.G., Cell 2003 114 171 180 12887919 10.1016/S0092-8674(03) 00551-8
    • (2003) Cell , vol.114 , pp. 171-180
    • Seo, D.W.1    Li, H.2    Guedez, L.3    Wingfield, P.T.4    Diaz, T.5    Salloum, R.6    Wei, B.7    Stetler-Stevenson, W.G.8
  • 31
    • 2942676966 scopus 로고    scopus 로고
    • Expression of metalloproteinase-2, metalloproteinase-9, and tissue inhibitor of metalloproteinase-1 in transitional cell carcinoma of upper urinary tract: Correlation with tumor stage and surviva
    • 15028476. 10.1016/j.urology.2003.09.035
    • Expression of metalloproteinase-2, metalloproteinase-9, and tissue inhibitor of metalloproteinase-1 in transitional cell carcinoma of upper urinary tract: correlation with tumor stage and surviva. Y Miyata Kanda, S., Nomata, K., Hayashida, Y., Kanetake, H., Urology 2004 63 602 608 15028476 10.1016/j.urology.2003.09.035
    • (2004) Urology , vol.63 , pp. 602-608
    • Miyata Kanda, Y.S.1    Nomata, K.2    Hayashida, Y.3    Kanetake, H.4
  • 34
    • 0036613237 scopus 로고    scopus 로고
    • Extensive genomic duplication during early chordate evolution
    • 12032567. 10.1038/ng884
    • Extensive genomic duplication during early chordate evolution. A McLysaght Hokamp, K., Wolfe, K.H., Nature Genetics 2002 31 200 204 12032567 10.1038/ng884
    • (2002) Nature Genetics , vol.31 , pp. 200-204
    • McLysaght Hokamp, A.K.1    Wolfe, K.H.2
  • 37
    • 26244444380 scopus 로고    scopus 로고
    • From 2R to 3R: Evidence for a fish-specific genome duplication (FSGD)
    • 16108068. 10.1002/bies.20293
    • From 2R to 3R: evidence for a fish-specific genome duplication (FSGD). A Meyer Van de Peer, Y., BioEssays 2005 27 937 945 16108068 10.1002/bies.20293
    • (2005) BioEssays , vol.27 , pp. 937-945
    • Meyer, A.1    Van De Peer, Y.2
  • 38
    • 21844444108 scopus 로고    scopus 로고
    • The characterisation of six ADAMTS proteases in the basal chordate Ciona intestinalis provides new insights into the vertebrate ADAMTS family
    • 10.1016/j.biocel.2005.03.009
    • The characterisation of six ADAMTS proteases in the basal chordate Ciona intestinalis provides new insights into the vertebrate ADAMTS family. J Huxley-Jones Apte, S.S., Robertson, D.L., Boot-Handford, R.P., International Journal of Biochemistry and Cell Biology 2005 37 1838 1845 10.1016/j.biocel. 2005.03.009
    • (2005) International Journal of Biochemistry and Cell Biology , vol.37 , pp. 1838-1845
    • Huxley-Jones Apte, J.S.S.1    Robertson, D.L.2    Boot-Handford, R.P.3
  • 39
    • 33846033842 scopus 로고    scopus 로고
    • On the origins of extracellular matrix in vertebrates
    • 10.1016/j.matbio.2006.09.008. 17055232
    • On the origins of extracellular matrix in vertebrates. J Huxley-Jones DL Robertson RP Boot-Handford, Matrix Biology 2007 26 2 11 10.1016/j.matbio.2006. 09.008 17055232
    • (2007) Matrix Biology , vol.26 , pp. 2-11
    • Huxley-Jones, J.1    Robertson, D.L.2    Boot-Handford, R.P.3
  • 40
    • 0026505684 scopus 로고
    • Physical linkage of the A-raf-1, properdin, synapsin I, and TIMP genes on the human and mouse X chromosomes
    • 1572636. 10.1016/0888-7543(92)90286-2
    • Physical linkage of the A-raf-1, properdin, synapsin I, and TIMP genes on the human and mouse X chromosomes. JMJ Derry Barnard, P.J., Genomics 1992 12 632 638 1572636 10.1016/0888-7543(92)90286-2
    • (1992) Genomics , vol.12 , pp. 632-638
    • Derry, J.M.J.1    Barnard, P.J.2
  • 41
    • 0037384351 scopus 로고    scopus 로고
    • Duplication, degeneration and subfunctionalization of the nested synapsin-Timp genes in Fugu
    • 12683968. 10.1016/S0168-9525(03)00048-9
    • Duplication, degeneration and subfunctionalization of the nested synapsin-Timp genes in Fugu. WP Yu Brenner, S., Venkatesh, B., Trends in Genetics 2003 19 180 183 12683968 10.1016/S0168-9525(03)00048-9
    • (2003) Trends in Genetics , vol.19 , pp. 180-183
    • Yu, W.P.1    Brenner, S.2    Venkatesh, B.3
  • 42
    • 0345465698 scopus 로고    scopus 로고
    • Invertebrate Tissue Inhibitor of Metalloproteinase: Structure and nested gene organization within the synapsin locus is conserved from drosophila to human
    • 10198170. 10.1006/geno.1999.5776
    • Invertebrate Tissue Inhibitor of Metalloproteinase: structure and nested gene organization within the synapsin locus is conserved from drosophila to human. N Pohar Godenschwege, T.A., Buchner, E., Genomics 1999 57 293 296 10198170 10.1006/geno.1999.5776
    • (1999) Genomics , vol.57 , pp. 293-296
    • Pohar, N.1    Godenschwege, T.A.2    Buchner, E.3
  • 45
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta
    • 11319869. 10.1006/dbio.2001.0166
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. H Nishimura Cho, C., Branciforte, D.R., Myles, D.G., Primakoff, P., Developmental Biology 2001 233 204 213 11319869 10.1006/dbio.2001.0166
    • (2001) Developmental Biology , vol.233 , pp. 204-213
    • Nishimura Cho, H.C.1    Branciforte, D.R.2    Myles, D.G.3    Primakoff, P.4
  • 46
    • 0030585736 scopus 로고    scopus 로고
    • Chromosomal assignment of four testis-expressed mouse genes from a new family of transmembrane proteins (ADAMs) involved in cell-cell adhesion and fusion
    • 10.1006/geno.1996.0305
    • Chromosomal assignment of four testis-expressed mouse genes from a new family of transmembrane proteins (ADAMs) involved in cell-cell adhesion and fusion. C Cho Primakoff, P., White, J.M., Myles, D.G., Genomics 1996 3 413 417 10.1006/geno.1996.0305
    • (1996) Genomics , vol.3 , pp. 413-417
    • Cho Primakoff, C.P.1    White, J.M.2    Myles, D.G.3
  • 47
    • 1942533493 scopus 로고    scopus 로고
    • Positive selection at reproductive ADAM genes with potential interceulluar binding activity
    • 10.1093/molbev/msh080
    • Positive selection at reproductive ADAM genes with potential interceulluar binding activity. B Glassey Civetta, A., Molecular Biology and Evolution 2004 21 851 859 10.1093/molbev/msh080
    • (2004) Molecular Biology and Evolution , vol.21 , pp. 851-859
    • Glassey, B.1    Civetta, A.2
  • 48
    • 0033178820 scopus 로고    scopus 로고
    • Transcripts encoding the sperm surface protein tMDC II are non-functional in the human
    • 10417343. 10.1042/0264-6021:3410771
    • Transcripts encoding the sperm surface protein tMDC II are non-functional in the human. J Frayne Dimsey, E.A., Jury, J.A., Hall, L., Biochemical Journal 1999 341 771 775 10417343 10.1042/0264-6021:3410771
    • (1999) Biochemical Journal , vol.341 , pp. 771-775
    • Frayne Dimsey, J.E.A.1    Jury, J.A.2    Hall, L.3
  • 51
    • 0033527442 scopus 로고    scopus 로고
    • Isolation of Two Novel Metalloproteinase- Disintegrin (ADAM) cDNAs That Show Testis-Specific Gene Expression
    • 10.1006/bbrc.1999.1322
    • Isolation of Two Novel Metalloproteinase- Disintegrin (ADAM) cDNAs That Show Testis-Specific Gene Expression. DP Cerretti DuBose, R. F., Black, R.A., Nelson, N., Biochemistry and Biophysics Research Communications 1999 263 810 815 10.1006/bbrc.1999.1322
    • (1999) Biochemistry and Biophysics Research Communications , vol.263 , pp. 810-815
    • Cerretti, D.P.1    Dubose, R.F.2    Black, R.A.3    Nelson, N.4
  • 52
    • 0037227364 scopus 로고    scopus 로고
    • Positive selection within sperm-egg adhesion domains of fertilin: An ADAM gene with a potential role in fertilization
    • Positive selection within sperm-egg adhesion domains of fertilin: an ADAM gene with a potential role in fertilization. A Civetta, Molecular Biology and Evolution 2003 20 21-29
    • (2003) Molecular Biology and Evolution , vol.20 , Issue.21-29
    • Civetta, A.1
  • 54
    • 34248187237 scopus 로고    scopus 로고
    • Sea urchin metalloproteases: A genomic survey of the BMP-1/tolloid-like, MMP and ADAM families
    • 17059814. 10.1016/j.ydbio.2006.07.046
    • Sea urchin metalloproteases: A genomic survey of the BMP-1/tolloid-like, MMP and ADAM families. L Angerer Hussain, S., Wei, Z., Livingstone, B.T., Developmental Biology 2006 300 267 281 17059814 10.1016/j.ydbio.2006.07.046
    • (2006) Developmental Biology , vol.300 , pp. 267-281
    • Angerer Hussain, L.S.1    Wei, Z.2    Livingstone, B.T.3
  • 55
    • 34248530454 scopus 로고    scopus 로고
    • Interpro. http://www.ebi.ac.uk/interpro
    • Interpro
  • 56
    • 0037321822 scopus 로고    scopus 로고
    • Fibrillar collagen: The key to vertebrate evolution? a tale of molecular incest.
    • 12539240. 10.1002/bies.10230
    • Fibrillar collagen: the key to vertebrate evolution? A tale of molecular incest. RP Boot-Handford Tuckwell, D.S., BioEssays 2003 25 142 151 12539240 10.1002/bies.10230
    • (2003) BioEssays , vol.25 , pp. 142-151
    • Boot-Handford, R.P.1    Tuckwell, D.S.2
  • 57
    • 26444603772 scopus 로고    scopus 로고
    • Two rounds of whole genome duplication in the ancestral vertebrate
    • 10.1371/journal.pbio.0030314
    • Two rounds of whole genome duplication in the ancestral vertebrate. P Dehal Boore, J.L., PLoS Biology 2005 3 1700 1708 10.1371/journal.pbio.0030314
    • (2005) PLoS Biology , vol.3 , pp. 1700-1708
    • Dehal, P.1    Boore, J.L.2
  • 58
    • 0038817812 scopus 로고    scopus 로고
    • New evidence for genome-wide duplications at the origin of vertebrates using an amphioxus gene set and completed animal genomes
    • 12799346. 10.1101/gr.874803
    • New evidence for genome-wide duplications at the origin of vertebrates using an amphioxus gene set and completed animal genomes. G Panopoulou Hennig, S., Groth, D., Krause, A., Poutska, A.J., Herwid, R., Vingron, M., Lehrach, H., Genome Research 2003 13 1056 1066 12799346 10.1101/gr.874803
    • (2003) Genome Research , vol.13 , pp. 1056-1066
    • Panopoulou Hennig, G.S.1    Groth, D.2    Krause, A.3    Poutska, A.J.4    Herwid, R.5    Vingron, M.6    Lehrach, H.7
  • 60
    • 33745067419 scopus 로고    scopus 로고
    • The gain and loss of genes during 600 million years of vertebrate evolution
    • 16723033. 10.1186/gb-2006-7-5-r43
    • The gain and loss of genes during 600 million years of vertebrate evolution. T Blomme Vandepoele, K., De Bodt, S., Simillion, C., Maere, S., Van de Peer, Y., Genome Biology 2006 7 R43 16723033 10.1186/gb-2006-7-5-r43
    • (2006) Genome Biology , vol.7 , pp. 43
    • Blomme Vandepoele, T.K.1    De Bodt, S.2    Simillion, C.3    Maere, S.4    Van De Peer, Y.5
  • 61
    • 0345016262 scopus 로고    scopus 로고
    • Evolution and diversity of fish genomes
    • 10.1016/j.gde.2003.09.001
    • Evolution and diversity of fish genomes. B Venkatesh, Current Opinion in Genetics and Development 2003 13 1 5 10.1016/j.gde.2003.09.001
    • (2003) Current Opinion in Genetics and Development , vol.13 , pp. 1-5
    • Venkatesh, B.1
  • 62
    • 15544377813 scopus 로고    scopus 로고
    • Genome evolution and biodiversity in teleost fish
    • 15674378. 10.1038/sj.hdy.6800635
    • Genome evolution and biodiversity in teleost fish. JN Volff, Heredity 2005 94 280 294 15674378 10.1038/sj.hdy.6800635
    • (2005) Heredity , vol.94 , pp. 280-294
    • Volff, J.N.1
  • 63
  • 64
    • 0037351989 scopus 로고    scopus 로고
    • Genome duplication, a trait shared by 22000 species of ray-finned fish
    • 12618368. 10.1101/gr.640303
    • Genome duplication, a trait shared by 22000 species of ray-finned fish. JS Taylor Braasch, I., Frickey, T., Meyer, A., Van de Peer, Y., Genome Research 2003 13 382 390 12618368 10.1101/gr.640303
    • (2003) Genome Research , vol.13 , pp. 382-390
    • Taylor, J.S.1    Braasch, I.2    Frickey, T.3    Meyer, A.4    Van De Peer, Y.5
  • 66
    • 15344342865 scopus 로고    scopus 로고
    • Functional evolution of ADAMTS genes: Evidence from analyses of phylogeny and gene organization
    • 15693998. 10.1186/1471-2148-5-11
    • Functional evolution of ADAMTS genes: Evidence from analyses of phylogeny and gene organization. AC Nicholson Malik, S-B., Logsdon Jr, J.M., Van Meir, E.G., BMC Evolutionary Biology 2005 5 11 15693998 10.1186/1471-2148-5-11
    • (2005) BMC Evolutionary Biology , vol.5 , pp. 11
    • Nicholson, A.C.1    Malik, S.-B.2    Logsdon Jr., J.M.3    Van Meir, E.G.4
  • 68
  • 69
    • 0025259313 scopus 로고
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
    • 10.1073/pnas.87.6.2264
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes. S Karlin Altchul, S.F., Proceedings of the Nation Academy of Sciences of the United States of America 1990 87 2264 2268 10.1073/pnas.87.6.2264
    • (1990) Proceedings of the Nation Academy of Sciences of the United States of America , vol.87 , pp. 2264-2268
    • Karlin, S.1    Altchul, S.F.2
  • 70
    • 34248572658 scopus 로고    scopus 로고
    • JGI, http://genome.jgi-psf.org/
    • Jgi1
  • 71
    • 34248532452 scopus 로고    scopus 로고
    • TIGR, http://www.tigr.org/tdb
    • Tigr1
  • 72
    • 34248523225 scopus 로고    scopus 로고
    • NCBI-zebrafish, http://www.ncbi.nlm.nih.gov/genome/guide/zebrafish
    • Ncbi-Zebrafish1
  • 73
    • 0035861990 scopus 로고    scopus 로고
    • Automatic clustering of orthologs and In-paralogs from Pairwise Species Comparisons
    • 11743721. 10.1006/jmbi.2000.5197
    • Automatic clustering of orthologs and In-paralogs from Pairwise Species Comparisons. M Remm Storm, C.E.V., Ell, S., Journal of Molecular Biology 2001 314 1041 1052 11743721 10.1006/jmbi.2000.5197
    • (2001) Journal of Molecular Biology , vol.314 , pp. 1041-1052
    • Remm Storm, M.C.E.V.1    Ell, S.2
  • 74
    • 34248593421 scopus 로고    scopus 로고
    • InParanoid, http://inparanoid.sbc.su.se/
    • Inparanoid1
  • 75
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • 15223320. 10.1016/j.jmb.2004.05.028
    • Improved prediction of signal peptides: SignalP 3.0. JD Bendtsen Nielsen, H., von Heijne, G., Brunak, S., Journal of Molecular Biology 2004 340 783 795 15223320 10.1016/j.jmb.2004.05.028
    • (2004) Journal of Molecular Biology , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 76
    • 2442713832 scopus 로고    scopus 로고
    • GeneWise and GenomeWise
    • 15123596. 10.1101/gr.1865504
    • GeneWise and GenomeWise. E Birney Clamp, M., Durbin, R., Genome Research 2004 14 988 995 15123596 10.1101/gr.1865504
    • (2004) Genome Research , vol.14 , pp. 988-995
    • Birney Clamp, E.M.1    Durbin, R.2
  • 77
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTALX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • The CLUSTALX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. JD Thompson Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., Nucleic Acids Research 1997 24 4877 4882
    • (1997) Nucleic Acids Research , vol.24 , pp. 4877-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 78
    • 34248587119 scopus 로고    scopus 로고
    • Ensembl, http://www.ensembl.org/Danio_rerio/index.html
    • Ensembl1
  • 79
    • 0004287108 scopus 로고
    • Department of Genetics, University of Washington, Seattle , Distributed by the author Version 3.5c
    • PHYLIP. J Felsenstein, Department of Genetics, University of Washington, Seattle, Distributed by the author Version 3.5c 1993
    • (1993) PHYLIP
    • Felsenstein, J.1
  • 80
    • 0029836454 scopus 로고    scopus 로고
    • Quartet puzzling: A quartet maximum likelihood method for reconstructing tree topologies
    • http://mbe.oxfordjournals.org/cgi/reprint/13/7/964
    • Quartet puzzling: A quartet maximum likelihood method for reconstructing tree topologies. K Strimmer von Haeseler, A., Molecular Biology and Evolution 1996 13 964 969 http://mbe.oxfordjournals.org/cgi/reprint/13/7/964
    • (1996) Molecular Biology and Evolution , vol.13 , pp. 964-969
    • Strimmer, K.1    Von Haeseler, A.2
  • 81


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.