메뉴 건너뛰기




Volumn 49, Issue 2, 1999, Pages 272-281

The evolution of the calpain family as reflected in paralogous chromosome regions

Author keywords

Calpain; Chordate evolution; Gene duplication; Paralogous chromosome regions; Tetraploidization

Indexed keywords

CALPAIN;

EID: 0032783288     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00006549     Document Type: Article
Times cited : (39)

References (61)
  • 1
    • 0031010579 scopus 로고    scopus 로고
    • Evidence for a clade of nematodes, arthropods and other moulting animals
    • Aguinaldo AM, Turbeville JM, Linford LS, et al. (1997) Evidence for a clade of nematodes, arthropods and other moulting animals. Nature 387:489-493
    • (1997) Nature , vol.387 , pp. 489-493
    • Aguinaldo, A.M.1    Turbeville, J.M.2    Linford, L.S.3
  • 2
    • 0025837971 scopus 로고
    • Characterization of cDNA clones encoding a novel calcium-activated neutral proteinase from Schistosoma mansoni
    • Andresen K, Tom TD, Strand M (1991) Characterization of cDNA clones encoding a novel calcium-activated neutral proteinase from Schistosoma mansoni. J Biol Chem 266:15085-15090
    • (1991) J Biol Chem , vol.266 , pp. 15085-15090
    • Andresen, K.1    Tom, T.D.2    Strand, M.3
  • 3
    • 0025948202 scopus 로고
    • Signal convergence on protein kinase A as a molecular correlate of learning
    • Aszödi A, Müller U, Friedrich P, Spatz HC (1991) Signal convergence on protein kinase A as a molecular correlate of learning. Proc Natl Acad Sci USA 88:5832-5836
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5832-5836
    • Aszödi, A.1    Müller, U.2    Friedrich, P.3    Spatz, H.C.4
  • 4
    • 0031930042 scopus 로고    scopus 로고
    • Origin of the metazoan phyla: Molecular docks confirm paleontological estimates
    • Ayala FJ, Rzhetsky A, Ayala FJ (1998) Origin of the metazoan phyla: Molecular docks confirm paleontological estimates. Proc Natl Acad Sci USA 95:606-611
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 606-611
    • Ayala, F.J.1    Rzhetsky, A.2    Ayala, F.J.3
  • 5
    • 0028972095 scopus 로고
    • Selective proteolysis of arrestin by calpain. Molecular characteristics and its effect on rhodopsin dephosphorylation
    • Azarian SM, King AJ, Hallett MA, Williams DS (1995) Selective proteolysis of arrestin by calpain. Molecular characteristics and its effect on rhodopsin dephosphorylation. J Biol Chem 270:24375-24384
    • (1995) J Biol Chem , vol.270 , pp. 24375-24384
    • Azarian, S.M.1    King, A.J.2    Hallett, M.A.3    Williams, D.S.4
  • 7
    • 0029834118 scopus 로고    scopus 로고
    • The tra-3 sex determination gene of Caenorhabditis elegans encodes a member of the calpain regulatory protease family
    • Barnes TM, Hodgkin J (1996) The tra-3 sex determination gene of Caenorhabditis elegans encodes a member of the calpain regulatory protease family. EMBO J 15:4477-4484
    • (1996) EMBO J , vol.15 , pp. 4477-4484
    • Barnes, T.M.1    Hodgkin, J.2
  • 8
    • 2642713364 scopus 로고    scopus 로고
    • The ParaHox gene cluster is an evolutionary sister of the Hox gene cluster
    • Brooke NM, Garcia-Fernandez J, Holland PW (1998) The ParaHox gene cluster is an evolutionary sister of the Hox gene cluster. Nature 392:920-922
    • (1998) Nature , vol.392 , pp. 920-922
    • Brooke, N.M.1    Garcia-Fernandez, J.2    Holland, P.W.3
  • 9
    • 0031259933 scopus 로고    scopus 로고
    • A new subfamily of vertebrate calpains lacking a calmodulin-like domain: Implications for calpain regulation and evolution
    • Dear N, Matena K, Vingron M, Boehm T (1997) A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution. Genomics 45:175-184
    • (1997) Genomics , vol.45 , pp. 175-184
    • Dear, N.1    Matena, K.2    Vingron, M.3    Boehm, T.4
  • 10
    • 0025915708 scopus 로고
    • Molecular cloning and analysis of small optic lobes, a structural brain gene of Drosophila melanogaster
    • Delaney SJ, Hayward DC, Barleben F, Fischbach KF, Miklos GI. (1991) Molecular cloning and analysis of small optic lobes, a structural brain gene of Drosophila melanogaster. Proc Natl Acad Sci USA 88:7214-7218
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7214-7218
    • Delaney, S.J.1    Hayward, D.C.2    Barleben, F.3    Fischbach, K.F.4    Miklos, G.I.5
  • 11
    • 0032561502 scopus 로고    scopus 로고
    • A physical map of 30,000 human genes
    • Deloukas P, Schuler GD, Gyapay G, et al. (1998) A physical map of 30,000 human genes. Science 282:744-746
    • (1998) Science , vol.282 , pp. 744-746
    • Deloukas, P.1    Schuler, G.D.2    Gyapay, G.3
  • 12
    • 0028892964 scopus 로고
    • Signaling of ambient pH in Aspergillus involves a cysteine protease
    • Denison SH, Orejas M, Arst HNJ (1995) Signaling of ambient pH in Aspergillus involves a cysteine protease. J Biol Chem 270:28519-28522
    • (1995) J Biol Chem , vol.270 , pp. 28519-28522
    • Denison, S.H.1    Orejas, M.2    Arst, H.N.J.3
  • 13
    • 0029017620 scopus 로고
    • Specific degradation of troponin T and I by μ-calpain and its modulation by substrate phosphorylation
    • Di Lisa F, De Tullio R, Salamino F, et al. (1995) Specific degradation of troponin T and I by μ-calpain and its modulation by substrate phosphorylation. Biochem J 308:57-61
    • (1995) Biochem J , vol.308 , pp. 57-61
    • Di Lisa, F.1    De Tullio, R.2    Salamino, F.3
  • 14
    • 0030023247 scopus 로고    scopus 로고
    • Determining divergence times of the major kingdoms of living organisms with a protein clock
    • Doolittle RF, Feng DF, Tsang S, Cho G, Little E (1996) Determining divergence times of the major kingdoms of living organisms with a protein clock. Science 271:470-477
    • (1996) Science , vol.271 , pp. 470-477
    • Doolittle, R.F.1    Feng, D.F.2    Tsang, S.3    Cho, G.4    Little, E.5
  • 15
    • 0027985149 scopus 로고
    • Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila
    • Emori Y, Saigo K (1994) Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila. J Biol Chem 269:25137-25142
    • (1994) J Biol Chem , vol.269 , pp. 25137-25142
    • Emori, Y.1    Saigo, K.2
  • 16
    • 0031946862 scopus 로고    scopus 로고
    • Mechanisms of developmental regulation in globin loci
    • Fraser P, Gribnau J, Trimborn T (1998) Mechanisms of developmental regulation in globin loci. Curr Opin Hematol 5:139-144
    • (1998) Curr Opin Hematol , vol.5 , pp. 139-144
    • Fraser, P.1    Gribnau, J.2    Trimborn, T.3
  • 17
    • 0031003129 scopus 로고    scopus 로고
    • Positive cross-regulation and enhancer sharing: Two mechanisms for specifying overlapping Hox expression patterns
    • Gould A, Morrison A, Sproat G, White RA, Krumlauf R (1997) Positive cross-regulation and enhancer sharing: two mechanisms for specifying overlapping Hox expression patterns. Genes Dev 11: 900-913
    • (1997) Genes Dev , vol.11 , pp. 900-913
    • Gould, A.1    Morrison, A.2    Sproat, G.3    White, R.A.4    Krumlauf, R.5
  • 18
    • 0032212158 scopus 로고    scopus 로고
    • Lampetra fluviatilis neurotrophin homolog, descendant of a neurotrophin ancestor, discloses the early molecular evolution of neurotrophins in the vertebrate subphylum
    • Hallböök F, Lundin LG, Kullander K (1998) Lampetra fluviatilis neurotrophin homolog, descendant of a neurotrophin ancestor, discloses the early molecular evolution of neurotrophins in the vertebrate subphylum. J Neurosci 18:8700-8711
    • (1998) J Neurosci , vol.18 , pp. 8700-8711
    • Hallböök, F.1    Lundin, L.G.2    Kullander, K.3
  • 19
    • 0030943108 scopus 로고    scopus 로고
    • Molecular evolution of the vertebrate troponin I gene family
    • Hastings KE (1997) Molecular evolution of the vertebrate troponin I gene family. Cell Struct Funct 22:205-211
    • (1997) Cell Struct Funct , vol.22 , pp. 205-211
    • Hastings, K.E.1
  • 21
    • 0032514704 scopus 로고    scopus 로고
    • Role of calpain in skeletal-muscle protein degradation
    • Huang J, Forsberg NE (1998) Role of calpain in skeletal-muscle protein degradation. Proc Natl Acad Sci USA 95:12100-12105
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12100-12105
    • Huang, J.1    Forsberg, N.E.2
  • 22
    • 0032528020 scopus 로고    scopus 로고
    • SOLH, a human homologue of the Drosophila melanogaster small optic lobes gene is a member of the calpain and zinc-finger gene families and maps to human chromosome 16p13.3 near CATM (cataract with microphthalmia)
    • Kamei M, Webb GC, Young IG, Campbell HD (1998) SOLH, a human homologue of the Drosophila melanogaster small optic lobes gene is a member of the calpain and zinc-finger gene families and maps to human chromosome 16p13.3 near CATM (cataract with microphthalmia). Genomics 51:197-206
    • (1998) Genomics , vol.51 , pp. 197-206
    • Kamei, M.1    Webb, G.C.2    Young, I.G.3    Campbell, H.D.4
  • 23
  • 24
    • 0030902728 scopus 로고    scopus 로고
    • Chromosomal duplication and the emergence of the adaptive immune system
    • Kasahara M, Nakaya J, Satta Y, Takahata N (1997) Chromosomal duplication and the emergence of the adaptive immune system. Trends Genet 13:90-92
    • (1997) Trends Genet , vol.13 , pp. 90-92
    • Kasahara, M.1    Nakaya, J.2    Satta, Y.3    Takahata, N.4
  • 25
    • 18144445733 scopus 로고    scopus 로고
    • Purification of native p94, a muscle-specific calpain, and characterization of its autolysis
    • Kinbara K, Ishiura S, Tomioka S, et al. (1998a) Purification of native p94, a muscle-specific calpain, and characterization of its autolysis. Biochem J 335:589-596
    • (1998) Biochem J , vol.335 , pp. 589-596
    • Kinbara, K.1    Ishiura, S.2    Tomioka, S.3
  • 26
    • 0031696884 scopus 로고    scopus 로고
    • Skeletal muscle-specific calpain, p94: Structure and physiological function
    • Kinbara K, Sorimachi H, Ishiura S, Suzuki K (1998b) Skeletal muscle-specific calpain, p94: structure and physiological function. Biochem Pharmacol 56:415-420
    • (1998) Biochem Pharmacol , vol.56 , pp. 415-420
    • Kinbara, K.1    Sorimachi, H.2    Ishiura, S.3    Suzuki, K.4
  • 27
    • 0031025671 scopus 로고    scopus 로고
    • Evolution of chordate actin genes: Evidence from genomic organization and amino acid sequences
    • Kusakabe T, Araki I, Satoh N, Jeffery WR (1997) Evolution of chordate actin genes: Evidence from genomic organization and amino acid sequences. J Mol Evol 44:289-298
    • (1997) J Mol Evol , vol.44 , pp. 289-298
    • Kusakabe, T.1    Araki, I.2    Satoh, N.3    Jeffery, W.R.4
  • 28
    • 0031883959 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract
    • Lee HJ, Sorimachi H, Jeong SY, Ishiura S, Suzuki K (1998) Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract. Biol Chem 379:175-183
    • (1998) Biol Chem , vol.379 , pp. 175-183
    • Lee, H.J.1    Sorimachi, H.2    Jeong, S.Y.3    Ishiura, S.4    Suzuki, K.5
  • 29
    • 0033080358 scopus 로고    scopus 로고
    • Characterization of a human digestive tract-specific calpain, nCL-4, expressed in the baculovirus system
    • Lee HJ, Tomioka S, Kinbara K, et al. (1999) Characterization of a human digestive tract-specific calpain, nCL-4, expressed in the baculovirus system. Arch Biochem Biophys 362:22-31
    • (1999) Arch Biochem Biophys , vol.362 , pp. 22-31
    • Lee, H.J.1    Tomioka, S.2    Kinbara, K.3
  • 30
    • 0031984447 scopus 로고    scopus 로고
    • An antisense oligodeoxyribonucleotide to m-calpain mRNA inhibits secretion from alveolar epithelial type II cells
    • Li HL, Feinstein SI, Liu L, Zimmerman UJ (1998) An antisense oligodeoxyribonucleotide to m-calpain mRNA inhibits secretion from alveolar epithelial type II cells. Cell Signal 10:137-142
    • (1998) Cell Signal , vol.10 , pp. 137-142
    • Li, H.L.1    Feinstein, S.I.2    Liu, L.3    Zimmerman, U.J.4
  • 31
    • 0027284770 scopus 로고
    • Evolution of the vertebrate genome as reflected in paralogous chromosomal regions in man and the house mouse
    • Lundin LG (1993) Evolution of the vertebrate genome as reflected in paralogous chromosomal regions in man and the house mouse, Genomics 16:1-19
    • (1993) Genomics , vol.16 , pp. 1-19
    • Lundin, L.G.1
  • 32
    • 0009631372 scopus 로고    scopus 로고
    • Paralogous genes and metazoan macroevolution
    • Hadronic Press, Palm Harbor
    • Lundin LG (1996) Paralogous genes and metazoan macroevolution. In: New frontiers in theoretical biology. Hadronic Press, Palm Harbor, pp 3-51
    • (1996) New Frontiers in Theoretical Biology , pp. 3-51
    • Lundin, L.G.1
  • 33
    • 0031466228 scopus 로고    scopus 로고
    • Tissue-specific alternative splicing of ascidian troponin I isoforms. Redesign of a protein isoform-generating mechanism during chordate evolution
    • MacLean DW, Meedel TH, Hastings KE (1997) Tissue-specific alternative splicing of ascidian troponin I isoforms. Redesign of a protein isoform-generating mechanism during chordate evolution. J Biol Chem 272:32115-32120
    • (1997) J Biol Chem , vol.272 , pp. 32115-32120
    • MacLean, D.W.1    Meedel, T.H.2    Hastings, K.E.3
  • 34
    • 0031936364 scopus 로고    scopus 로고
    • Genomic organization of mouse Capn5 and Capn6 genes confirms that they are a distinct calpain subfamily
    • Matena K, Boehm T, Dear N (1998) Genomic organization of mouse Capn5 and Capn6 genes confirms that they are a distinct calpain subfamily. Genomics 48:117-120
    • (1998) Genomics , vol.48 , pp. 117-120
    • Matena, K.1    Boehm, T.2    Dear, N.3
  • 35
    • 8544240102 scopus 로고    scopus 로고
    • Overview of the yeast genome
    • Mewes HW, Albermann K, Bahr M, et al. (1997) Overview of the yeast genome. Nature 387:7-65
    • (1997) Nature , vol.387 , pp. 7-65
    • Mewes, H.W.1    Albermann, K.2    Bahr, M.3
  • 36
    • 8544277996 scopus 로고    scopus 로고
    • An estimate of divergence time of Parazoa and Eumetazoa and that of Cephalochordata and Vertebrata by aldolase and triose phosphate isomerase clocks
    • Nikoh N, Iwabe N, Kuma K, et al. (1997) An estimate of divergence time of Parazoa and Eumetazoa and that of Cephalochordata and Vertebrata by aldolase and triose phosphate isomerase clocks. J Mol Evol 45:97-106
    • (1997) J Mol Evol , vol.45 , pp. 97-106
    • Nikoh, N.1    Iwabe, N.2    Kuma, K.3
  • 37
    • 0021749729 scopus 로고
    • Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?
    • Ohno S, Emori Y, Imajoh S, Kawasaki H, Kisaragi M, Suzuki K (1984) Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein? Nature 312:566-570
    • (1984) Nature , vol.312 , pp. 566-570
    • Ohno, S.1    Emori, Y.2    Imajoh, S.3    Kawasaki, H.4    Kisaragi, M.5    Suzuki, K.6
  • 38
    • 0025936264 scopus 로고
    • Multigene families and the evolution of complexity
    • Ohta T (1991) Multigene families and the evolution of complexity. J Mol Evol 33:34-41
    • (1991) J Mol Evol , vol.33 , pp. 34-41
    • Ohta, T.1
  • 40
    • 0032169330 scopus 로고    scopus 로고
    • Muscle-specific locus control region activity associated with the human desmin gene
    • Raguz S, Hobbs C, Yague E, Ioannou PA, Walsh FS, Antoniou M (1998) Muscle-specific locus control region activity associated with the human desmin gene. Dev Biol 201:26-42
    • (1998) Dev Biol , vol.201 , pp. 26-42
    • Raguz, S.1    Hobbs, C.2    Yague, E.3    Ioannou, P.A.4    Walsh, F.S.5    Antoniou, M.6
  • 41
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
    • Richard I, Broux O, Allamand V, et al. (1995) Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell 81:27-40
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3
  • 42
    • 0031016034 scopus 로고    scopus 로고
    • Cloning and analysis of an HMG gene from the lamprey Lampetra fluviatilis: Gene duplication in vertebrate evolution
    • Sharman AC, Hay-Schmidt A, Holland PW (1997) Cloning and analysis of an HMG gene from the lamprey Lampetra fluviatilis: Gene duplication in vertebrate evolution. Gene 184:99-105
    • (1997) Gene , vol.184 , pp. 99-105
    • Sharman, A.C.1    Hay-Schmidt, A.2    Holland, P.W.3
  • 43
    • 0032536818 scopus 로고    scopus 로고
    • Selectivity, sharing and competitive interactions in the regulation of Hoxb genes
    • Sharpe J, Nonchev S, Gould A, Whiting J, Krumlauf R (1998) Selectivity, sharing and competitive interactions in the regulation of Hoxb genes. EMBO J 17:1788-1798
    • (1998) EMBO J , vol.17 , pp. 1788-1798
    • Sharpe, J.1    Nonchev, S.2    Gould, A.3    Whiting, J.4    Krumlauf, R.5
  • 46
    • 0024369426 scopus 로고
    • Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m-and μ-types. Specific expression of the mRNA in skeletal muscle
    • Sorimachi H, Imajoh-Ohmi S, Emori Y, et al. (1989) Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m-and μ-types. Specific expression of the mRNA in skeletal muscle. J Biol Chem 264:20106-20111
    • (1989) J Biol Chem , vol.264 , pp. 20106-20111
    • Sorimachi, H.1    Imajoh-Ohmi, S.2    Emori, Y.3
  • 48
    • 0027276561 scopus 로고
    • Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle
    • Sorimachi H, Toyama-Sorimachi N, Saido TC, et al. (1993b) Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. J Biol Chem 268:10593-10605
    • (1993) J Biol Chem , vol.268 , pp. 10593-10605
    • Sorimachi, H.1    Toyama-Sorimachi, N.2    Saido, T.C.3
  • 49
    • 0028347283 scopus 로고
    • New error of calpain research. Discovery of tissue-specific calpains
    • Sorimachi H, Saido TC, Suzuki K (1994) New error of calpain research. Discovery of tissue-specific calpains. FEBS Lett 343:1-5
    • (1994) FEBS Lett , vol.343 , pp. 1-5
    • Sorimachi, H.1    Saido, T.C.2    Suzuki, K.3
  • 50
    • 13344285357 scopus 로고
    • Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence
    • Sorimachi H, Kinbara K, Kimura S, et al. (1995a) Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J Biol Chem 270:31158-31162
    • (1995) J Biol Chem , vol.270 , pp. 31158-31162
    • Sorimachi, H.1    Kinbara, K.2    Kimura, S.3
  • 51
    • 0028959934 scopus 로고
    • Identification of a third ubiquitous calpain species: Chicken muscle expresses four distinct calpains
    • Sorimachi H, Tsukahara T, Okada-Ban M, Sugita H, Ishiura S, Suzuki K (1995b) Identification of a third ubiquitous calpain species: Chicken muscle expresses four distinct calpains. Biochim Biophys Acta 1261:381-393
    • (1995) Biochim Biophys Acta , vol.1261 , pp. 381-393
    • Sorimachi, H.1    Tsukahara, T.2    Okada-Ban, M.3    Sugita, H.4    Ishiura, S.5    Suzuki, K.6
  • 52
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H, Ishiura S, Suzuki K (1997) Structure and physiological function of calpains. Biochem J 328:721-732
    • (1997) Biochem J , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 53
    • 0030785498 scopus 로고    scopus 로고
    • Lactate dehydrogenase (LDH) gene duplication during chordate evolution: The cDNA sequence of the LDH of the tunicate Styela plicata
    • Stock DW, Quattro JM, Whitt GS, Powers DA (1997) Lactate dehydrogenase (LDH) gene duplication during chordate evolution: the cDNA sequence of the LDH of the tunicate Styela plicata. Mol Biol Evol 14:1273-1284
    • (1997) Mol Biol Evol , vol.14 , pp. 1273-1284
    • Stock, D.W.1    Quattro, J.M.2    Whitt, G.S.3    Powers, D.A.4
  • 54
    • 0029836454 scopus 로고    scopus 로고
    • Quartet puzzling: A quartet maximum likelihood method for reconstructing tree topologies
    • Strimmer K, Haeseler VA (1996) Quartet puzzling: A quartet maximum likelihood method for reconstructing tree topologies. Mol Biol Evol 13:964-969
    • (1996) Mol Biol Evol , vol.13 , pp. 964-969
    • Strimmer, K.1    Haeseler, V.A.2
  • 55
    • 0028851344 scopus 로고
    • CalpA. a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells
    • Theopold U, Pintér M, Daffre S, et al. (1995) CalpA. a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells. Mol Cell Biol 15:824-834
    • (1995) Mol Cell Biol , vol.15 , pp. 824-834
    • Theopold, U.1    Pintér, M.2    Daffre, S.3
  • 56
    • 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 JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 57
    • 0033521532 scopus 로고    scopus 로고
    • Dividing the empire: Boundary chromatin elements delimit the territory of enhancers
    • Udvardy A (1999) Dividing the empire: Boundary chromatin elements delimit the territory of enhancers. EMBO J 18:1-8
    • (1999) EMBO J , vol.18 , pp. 1-8
    • Udvardy, A.1
  • 58
    • 0027441185 scopus 로고
    • Specific cleavage of transcription factors by the thiol protease, m-calpain
    • Watt F, Molloy PL (1993) Specific cleavage of transcription factors by the thiol protease, m-calpain. Nucleic Acids Res 21:5092-5100
    • (1993) Nucleic Acids Res , vol.21 , pp. 5092-5100
    • Watt, F.1    Molloy, P.L.2
  • 59
    • 0028295681 scopus 로고
    • 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans
    • Wilson R, Ainscough R, Anderson K, et al. (1994) 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 368:32-38
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1    Ainscough, R.2    Anderson, K.3
  • 60
    • 0024471787 scopus 로고
    • 2+-dependent proteinase (calpain) activity in a plant species, Elodea densa
    • 2+-dependent proteinase (calpain) activity in a plant species, Elodea densa. Life Sci 45:2093-2101
    • (1989) Life Sci , vol.45 , pp. 2093-2101
    • Wolfe, F.H.1    Szpacenko, A.2    McGee, K.3    Goll, D.E.4
  • 61
    • 0031587952 scopus 로고    scopus 로고
    • Cytoplasmic processing of human profilaggrin by active μ-calpain
    • Yamazaki M, Ishidoh K, Suga Y, et al. (1997) Cytoplasmic processing of human profilaggrin by active μ-calpain. Biochem Biophys Res Commun 235:652-656
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 652-656
    • Yamazaki, M.1    Ishidoh, K.2    Suga, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.