메뉴 건너뛰기




Volumn 149, Issue 4, 2008, Pages 541-551

Cloning and expression of carp cathepsin Z: Possible involvement in yolk metabolism

Author keywords

Carp; Cathepsin Z; Cortical granule; Fertilization envelope; Oocyte maturation; Vitellogenin

Indexed keywords

CATHEPSIN; CATHEPSIN Z; COMPLEMENTARY DNA; MESSENGER RNA; PAPAIN; PROTEINASE; UNCLASSIFIED DRUG;

EID: 39849103861     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2006.05.017     Document Type: Article
Times cited : (15)

References (69)
  • 1
    • 0142225776 scopus 로고    scopus 로고
    • Lysis of pathogenic bacteria by epidermal cathepsin L and B in the Japanese eel
    • Aranishi F. Lysis of pathogenic bacteria by epidermal cathepsin L and B in the Japanese eel Fish Physiol. Biochem. 20 1999 37 41
    • (1999) Fish Physiol. Biochem. , vol.20 , pp. 37-41
    • Aranishi, F.1
  • 2
    • 0028325357 scopus 로고
    • Unique cleavage specificity of ‘prohormone thiol protease’ related to proenkephalin processing
    • Azaryan A.V. Hook V.Y. Unique cleavage specificity of ‘prohormone thiol protease’ related to proenkephalin processing FEBS Lett. 341 1994 197 202
    • (1994) FEBS Lett. , vol.341 , pp. 197-202
    • Azaryan, A.V.1    Hook, V.Y.2
  • 3
    • 0013771494 scopus 로고
    • Lysosomal enzymes in the rat ovary and endometrium during the estrous cycle
    • Banon P. Brandes D. Frost J.K. Lysosomal enzymes in the rat ovary and endometrium during the estrous cycle Acta Cytol. 8 1964 416 425
    • (1964) Acta Cytol. , vol.8 , pp. 416-425
    • Banon, P.1    Brandes, D.2    Frost, J.K.3
  • 4
    • 0030814882 scopus 로고    scopus 로고
    • Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss
    • Brooks S. Tyler C.R. Carnevali O. Coward K. Sumpter J.P. Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss Gene 201 1997 45 54
    • (1997) Gene , vol.201 , pp. 45-54
    • Brooks, S.1    Tyler, C.R.2    Carnevali, O.3    Coward, K.4    Sumpter, J.P.5
  • 5
    • 0032918875 scopus 로고    scopus 로고
    • Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: involvement of two lysosomal proteinases
    • Carnevali O. Carletta R. Cambi A. Vita A. Bromage N. Yolk formation and degradation during oocyte maturation in seabream Sparus aurata : involvement of two lysosomal proteinases Biol. Reprod. 60 1999 140 146
    • (1999) Biol. Reprod. , vol.60 , pp. 140-146
    • Carnevali, O.1    Carletta, R.2    Cambi, A.3    Vita, A.4    Bromage, N.5
  • 6
    • 0026327404 scopus 로고
    • Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease
    • Cataldo A.M. Paskevich P.A. Kominami E. Nixon R.A. Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease Proc. Natl. Acad. Sci. U. S. A. 88 1991 10998 11002
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10998-11002
    • Cataldo, A.M.1    Paskevich, P.A.2    Kominami, E.3    Nixon, R.A.4
  • 7
    • 0000249898 scopus 로고
    • Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs
    • Chan S.J. San S.B. McCormick M.B. Steiner D.F. Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs Proc. Natl. Acad. Sci. U. S. A. 33 1986 7721 7725
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.33 , pp. 7721-7725
    • Chan, S.J.1    San, S.B.2    McCormick, M.B.3    Steiner, D.F.4
  • 8
    • 0036015203 scopus 로고    scopus 로고
    • Fibroin-like substance is a major component of the outer layer of fertilization envelope via which carp egg adheres to the substratum
    • Chang Y.S. Huang F.L. Fibroin-like substance is a major component of the outer layer of fertilization envelope via which carp egg adheres to the substratum Mol. Reprod. Dev. 62 2002 397 406
    • (2002) Mol. Reprod. Dev. , vol.62 , pp. 397-406
    • Chang, Y.S.1    Huang, F.L.2
  • 9
    • 0029747210 scopus 로고    scopus 로고
    • Molecular cloning, structural analysis, and expression of carp ZP3 gene
    • Chang Y.S. Wang S.C. Tsao C.C. Huang F.L. Molecular cloning, structural analysis, and expression of carp ZP3 gene Mol. Reprod. Dev. 44 1996 295 304
    • (1996) Mol. Reprod. Dev. , vol.44 , pp. 295-304
    • Chang, Y.S.1    Wang, S.C.2    Tsao, C.C.3    Huang, F.L.4
  • 10
    • 0031735393 scopus 로고    scopus 로고
    • Identification of cystatin as a component of carp chorion
    • Chang Y.S. Weng J.W. Li C.C. Huang F.L. Identification of cystatin as a component of carp chorion Mol. Reprod. Dev. 51 1998 430 435
    • (1998) Mol. Reprod. Dev. , vol.51 , pp. 430-435
    • Chang, Y.S.1    Weng, J.W.2    Li, C.C.3    Huang, F.L.4
  • 11
    • 0034712886 scopus 로고    scopus 로고
    • Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization
    • Deussing J. von Olshausen I. Peters C. Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization Biochim. Biophys. Acta 1491 2000 93 106
    • (2000) Biochim. Biophys. Acta , vol.1491 , pp. 93-106
    • Deussing, J.1    von Olshausen, I.2    Peters, C.3
  • 12
    • 0024312845 scopus 로고
    • Biosynthesis of lysosomal endopeptidases
    • Erickson A. Biosynthesis of lysosomal endopeptidases J. Cell. Biochem. 40 1989 31 41
    • (1989) J. Cell. Biochem. , vol.40 , pp. 31-41
    • Erickson, A.1
  • 13
    • 0022998829 scopus 로고
    • Cloning and DNA sequence analysis of the cDNA for the precursor of the beta chain of bovine follicle stimulating hormone
    • Esch F.S. Mason A.J. Cooksey K. Mercado M. Shimasaki S. Cloning and DNA sequence analysis of the cDNA for the precursor of the beta chain of bovine follicle stimulating hormone Proc. Natl. Acad. Sci. U. S. A. 83 1986 6618 6621
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6618-6621
    • Esch, F.S.1    Mason, A.J.2    Cooksey, K.3    Mercado, M.4    Shimasaki, S.5
  • 16
    • 0942265428 scopus 로고    scopus 로고
    • Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation
    • Fabra M. Cerda J. Ovarian cysteine proteinases in the teleost Fundulus heteroclitus : molecular cloning and gene expression during vitellogenesis and oocyte maturation Mol. Reprod. Dev. 67 2004 282 294
    • (2004) Mol. Reprod. Dev. , vol.67 , pp. 282-294
    • Fabra, M.1    Cerda, J.2
  • 17
    • 0034106414 scopus 로고    scopus 로고
    • The new subfamily of cathepsin-Z-like protease genes includes Tc-cpz-1, a cysteine protease gene expressed in Toxocara canis adults and infective stage larvae
    • Falcone F.H. Tetteh K.K. Hunt P. Blaxter M.L. Loukas A. Maizels R.M. The new subfamily of cathepsin-Z-like protease genes includes Tc-cpz-1, a cysteine protease gene expressed in Toxocara canis adults and infective stage larvae Exp. Parasitol. 94 2000 201 207
    • (2000) Exp. Parasitol. , vol.94 , pp. 201-207
    • Falcone, F.H.1    Tetteh, K.K.2    Hunt, P.3    Blaxter, M.L.4    Loukas, A.5    Maizels, R.M.6
  • 18
    • 0024310890 scopus 로고
    • Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase
    • Fuchs R. Gassen H.G. Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase Nucleic Acids Res. 17 1989 9471
    • (1989) Nucleic Acids Res. , vol.17 , pp. 9471
    • Fuchs, R.1    Gassen, H.G.2
  • 20
    • 0017058840 scopus 로고
    • Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 2. Evidence for identical subunits catalysing the two activities
    • Gething M.J. Davidson B.E. Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 2. Evidence for identical subunits catalysing the two activities Eur. J. Biochem. 71 1976 327 336
    • (1976) Eur. J. Biochem. , vol.71 , pp. 327-336
    • Gething, M.J.1    Davidson, B.E.2
  • 21
    • 0033168970 scopus 로고    scopus 로고
    • The cortical granule serine protease CGSP1 of the sea urchin, Strongylocentrotus purpuratus, is autocatalytic and contains a low-density lipoprotein receptor-like domain
    • Haley S.A. Wessel G.M. The cortical granule serine protease CGSP1 of the sea urchin, Strongylocentrotus purpuratus , is autocatalytic and contains a low-density lipoprotein receptor-like domain Dev. Biol. 211 1999 1 10
    • (1999) Dev. Biol. , vol.211 , pp. 1-10
    • Haley, S.A.1    Wessel, G.M.2
  • 23
    • 1242316967 scopus 로고    scopus 로고
    • The Caenorhabditis elegans cathepsin Z-like cysteine protease, Ce-CPZ-1, has a multifunctional role during the worms' development
    • Hashmi S. Zhang J. Oksov Y. Lustigman S. The Caenorhabditis elegans cathepsin Z-like cysteine protease, Ce-CPZ-1, has a multifunctional role during the worms' development J. Biol. Chem. 279 2004 6035 6045
    • (2004) J. Biol. Chem. , vol.279 , pp. 6035-6045
    • Hashmi, S.1    Zhang, J.2    Oksov, Y.3    Lustigman, S.4
  • 25
    • 0029991462 scopus 로고    scopus 로고
    • The house dust mite allergen Der p1 catalytically inactivates alpha 1-antitrypsin by specific reactive centre loop cleavage: a mechanism that promotes airway inflammation and asthma
    • Kalsheker N.A. Deam S. Chambers L. Sreedharan S. Brocklehurst K. Lomas D.A. The house dust mite allergen Der p1 catalytically inactivates alpha 1-antitrypsin by specific reactive centre loop cleavage: a mechanism that promotes airway inflammation and asthma Biochem. Biophys. Res. Commun. 221 1996 59 61
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 59-61
    • Kalsheker, N.A.1    Deam, S.2    Chambers, L.3    Sreedharan, S.4    Brocklehurst, K.5    Lomas, D.A.6
  • 26
    • 0023069331 scopus 로고
    • Abnormal expression of lysosomal cysteine proteinases in muscle wasting diseases
    • Katunuma N. Kominami E. Abnormal expression of lysosomal cysteine proteinases in muscle wasting diseases Rev. Physiol., Biochem. Pharmacol. 108 1987 1 20
    • (1987) Rev. Physiol., Biochem. Pharmacol. , vol.108 , pp. 1-20
    • Katunuma, N.1    Kominami, E.2
  • 28
    • 1342265418 scopus 로고    scopus 로고
    • Myxobolus cerebralis: identification of a cathepsin Z-like protease gene (MyxCP-1) expressed during parasite development in rainbow trout, Oncorhynchus mykiss
    • Kelley G.O. Adkison M.A. Leutenegger C.M. Hedrick R.P. Myxobolus cerebralis : identification of a cathepsin Z-like protease gene (MyxCP-1) expressed during parasite development in rainbow trout, Oncorhynchus mykiss Exp. Parasitol. 105 2003 201 210
    • (2003) Exp. Parasitol. , vol.105 , pp. 201-210
    • Kelley, G.O.1    Adkison, M.A.2    Leutenegger, C.M.3    Hedrick, R.P.4
  • 30
    • 0024814219 scopus 로고
    • Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins
    • Kirschke H. Wiederanders B. Brommed D. Rinne A. Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins Biochem. J. 264 1989 467 473
    • (1989) Biochem. J. , vol.264 , pp. 467-473
    • Kirschke, H.1    Wiederanders, B.2    Brommed, D.3    Rinne, A.4
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 32
    • 25144498370 scopus 로고    scopus 로고
    • Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus
    • LaFleur G.J. Jr. Raldua D. Fabra M. Carnevali O. Denslow N. Wallace R.A. Cerda J. Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus Biol. Reprod. 73 2005 815 824
    • (2005) Biol. Reprod. , vol.73 , pp. 815-824
    • LaFleur, G.J.1    Raldua, D.2    Fabra, M.3    Carnevali, O.4    Denslow, N.5    Wallace, R.A.6    Cerda, J.7
  • 33
    • 0030890614 scopus 로고    scopus 로고
    • Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes
    • Linnevers C. Smeekens S.P. Bromme D. Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes FEBS Lett. 405 1997 253 259
    • (1997) FEBS Lett. , vol.405 , pp. 253-259
    • Linnevers, C.1    Smeekens, S.P.2    Bromme, D.3
  • 34
    • 8844224148 scopus 로고    scopus 로고
    • RNA interference targeting cathepsin L and Z-like cysteine proteases of Onchocerca volvulus confirmed their essential function during L3 molting
    • Lustigman S. Zhang J. Liu J. Oksov Y. Hashmi S. RNA interference targeting cathepsin L and Z-like cysteine proteases of Onchocerca volvulus confirmed their essential function during L3 molting Mol. Biochem. Parasitol. 138 2004 165 170
    • (2004) Mol. Biochem. Parasitol. , vol.138 , pp. 165-170
    • Lustigman, S.1    Zhang, J.2    Liu, J.3    Oksov, Y.4    Hashmi, S.5
  • 35
    • 0019324038 scopus 로고
    • Multiple forms of the asclepains. Cysteinyl proteases from milkweed
    • Lynn K.R. Brockbank W.J. Clevette N.A. Multiple forms of the asclepains. Cysteinyl proteases from milkweed Biochim. Biophys. Acta 612 1980 119 125
    • (1980) Biochim. Biophys. Acta , vol.612 , pp. 119-125
    • Lynn, K.R.1    Brockbank, W.J.2    Clevette, N.A.3
  • 37
    • 8444249345 scopus 로고    scopus 로고
    • Salmon spawning migration and muscle protein metabolism: the August Krogh principle at work
    • Mommsen T.P. Salmon spawning migration and muscle protein metabolism: the August Krogh principle at work Comp. Biochem. Physiol. B 139 2004 383 400
    • (2004) Comp. Biochem. Physiol. B , vol.139 , pp. 383-400
    • Mommsen, T.P.1
  • 38
    • 0001674593 scopus 로고
    • Sites and pattern of protein and amino acid utilization during the spawning migration of salmon
    • Mommsen T.P. French C.J. Hochachka P.W. Sites and pattern of protein and amino acid utilization during the spawning migration of salmon Can. J. Zool. 58 1980 1785 1799
    • (1980) Can. J. Zool. , vol.58 , pp. 1785-1799
    • Mommsen, T.P.1    French, C.J.2    Hochachka, P.W.3
  • 39
    • 0028853165 scopus 로고
    • Delivery of nascent MHC class II-invariant chain complexes to lysosomal compartments and proteolysis of invariant chain by cysteine proteases precedes peptide binding in B-lymphoblastoid cells
    • Morton P.A. Zacheis M.L. Giacoletto K.S. Manning J.A. Schwartz B.D. Delivery of nascent MHC class II-invariant chain complexes to lysosomal compartments and proteolysis of invariant chain by cysteine proteases precedes peptide binding in B-lymphoblastoid cells J. Immunol. 154 1995 137 150
    • (1995) J. Immunol. , vol.154 , pp. 137-150
    • Morton, P.A.1    Zacheis, M.L.2    Giacoletto, K.S.3    Manning, J.A.4    Schwartz, B.D.5
  • 40
    • 0040234054 scopus 로고    scopus 로고
    • Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions
    • Nagler D.K. Menard R. Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions FEBS Lett. 434 1998 135 139
    • (1998) FEBS Lett. , vol.434 , pp. 135-139
    • Nagler, D.K.1    Menard, R.2
  • 41
    • 0040366645 scopus 로고    scopus 로고
    • Human cathepsin X: a cysteine protease with unique carboxypeptidase activity
    • Nagler D.K. Zhang R. Tam W. Sulea T. Purisima E.O. Menard R. Human cathepsin X: a cysteine protease with unique carboxypeptidase activity Biochemistry 38 1999 12648 12654
    • (1999) Biochemistry , vol.38 , pp. 12648-12654
    • Nagler, D.K.1    Zhang, R.2    Tam, W.3    Sulea, T.4    Purisima, E.O.5    Menard, R.6
  • 43
    • 0023661275 scopus 로고
    • Specific proteolysis regulates fusion between endocytic compartments in Xenopus oocytes
    • Opresko L.K. Karpf R. Specific proteolysis regulates fusion between endocytic compartments in Xenopus oocytes Cell 51 1987 557 568
    • (1987) Cell , vol.51 , pp. 557-568
    • Opresko, L.K.1    Karpf, R.2
  • 45
    • 0020416069 scopus 로고
    • Study on a proteolytic enzyme from Trypanosoma congolense. Purification and some biochemical properties
    • Rautenberg P. Schadler R. Reinwald E. Risse H.J. Study on a proteolytic enzyme from Trypanosoma congolense . Purification and some biochemical properties Mol. Cell. Biochem. 47 1982 151 159
    • (1982) Mol. Cell. Biochem. , vol.47 , pp. 151-159
    • Rautenberg, P.1    Schadler, R.2    Reinwald, E.3    Risse, H.J.4
  • 46
    • 0026437443 scopus 로고
    • Molecular cloning and functional characterization of chicken cathepsin D, a key enzyme for yolk formation
    • Retzek H. Steyrer E. Sanders E.J. Nimpf J. Schneider W.J. Molecular cloning and functional characterization of chicken cathepsin D, a key enzyme for yolk formation DNA Cell Biol. 11 1992 661 672
    • (1992) DNA Cell Biol. , vol.11 , pp. 661-672
    • Retzek, H.1    Steyrer, E.2    Sanders, E.J.3    Nimpf, J.4    Schneider, W.J.5
  • 48
    • 0037036926 scopus 로고    scopus 로고
    • Oestrogen-induced expression of a novel liver-specific aspartic proteinase in Danio rerio (zebrafish)
    • Riggio M. Scudiero R. Filosa S. Parisi E. Oestrogen-induced expression of a novel liver-specific aspartic proteinase in Danio rerio (zebrafish) Gene 295 2002 241 246
    • (2002) Gene , vol.295 , pp. 241-246
    • Riggio, M.1    Scudiero, R.2    Filosa, S.3    Parisi, E.4
  • 50
    • 0032522413 scopus 로고    scopus 로고
    • Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas
    • Santamaria I. Velasco G. Cazorla M. Fueyo A. Campo E. Lopez-Otin C. Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas Cancer Res. 58 1998 1624 1630
    • (1998) Cancer Res. , vol.58 , pp. 1624-1630
    • Santamaria, I.1    Velasco, G.2    Cazorla, M.3    Fueyo, A.4    Campo, E.5    Lopez-Otin, C.6
  • 51
    • 0032479144 scopus 로고    scopus 로고
    • Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location
    • Santamaria I. Velasco G. Pendas A.M. Fueyo A. Lopez-Otin C. Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location J. Biol. Chem. 273 1998 16816 16823
    • (1998) J. Biol. Chem. , vol.273 , pp. 16816-16823
    • Santamaria, I.1    Velasco, G.2    Pendas, A.M.3    Fueyo, A.4    Lopez-Otin, C.5
  • 52
    • 0026630108 scopus 로고
    • Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease
    • Shi G.P. Munger J.S. Meara J.P. Rich D.H. Chapman H.A. Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease J. Biol. Chem. 267 1992 7258 7262
    • (1992) J. Biol. Chem. , vol.267 , pp. 7258-7262
    • Shi, G.P.1    Munger, J.S.2    Meara, J.P.3    Rich, D.H.4    Chapman, H.A.5
  • 53
    • 0034723144 scopus 로고    scopus 로고
    • Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine
    • Sivaraman J. Nagler D.K. Zhang R. Menard R. Cygler M. Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine J. Mol. Biol. 295 2000 939 951
    • (2000) J. Mol. Biol. , vol.295 , pp. 939-951
    • Sivaraman, J.1    Nagler, D.K.2    Zhang, R.3    Menard, R.4    Cygler, M.5
  • 57
    • 0032835452 scopus 로고    scopus 로고
    • Cathepsin J, a novel murine cysteine protease of the papain family with a placenta-restricted expression
    • Tisljar K. Deussing J. Peters C. Cathepsin J, a novel murine cysteine protease of the papain family with a placenta-restricted expression FEBS Lett. 459 1999 299 304
    • (1999) FEBS Lett. , vol.459 , pp. 299-304
    • Tisljar, K.1    Deussing, J.2    Peters, C.3
  • 58
    • 0023656232 scopus 로고
    • Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin
    • Troen B.R. Gal S. Gottesman M.M. Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin Biochem. J. 246 1987 731 735
    • (1987) Biochem. J. , vol.246 , pp. 731-735
    • Troen, B.R.1    Gal, S.2    Gottesman, M.M.3
  • 60
    • 0028072096 scopus 로고
    • Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in human tissues
    • Velasco G. Ferrando A.A. Puente X.S. Sanchez L.M. Lopez-Otin C. Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli , and expression analysis in human tissues J. Biol. Chem. 269 1994 27136 27142
    • (1994) J. Biol. Chem. , vol.269 , pp. 27136-27142
    • Velasco, G.1    Ferrando, A.A.2    Puente, X.S.3    Sanchez, L.M.4    Lopez-Otin, C.5
  • 62
    • 0030790341 scopus 로고    scopus 로고
    • Degradation of mouse invariant chain: roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism
    • Villadangos J.A. Riese R.J. Peters C. Chapman H.A. Ploegh H.L. Degradation of mouse invariant chain: roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism J. Exp. Med. 186 1997 549 560
    • (1997) J. Exp. Med. , vol.186 , pp. 549-560
    • Villadangos, J.A.1    Riese, R.J.2    Peters, C.3    Chapman, H.A.4    Ploegh, H.L.5
  • 63
    • 0026586805 scopus 로고
    • Physiological changes of skeletal muscle by maturation-spawning of non-migrating female Atlantic salmon, Salmo salar
    • von der Decken A. Physiological changes of skeletal muscle by maturation-spawning of non-migrating female Atlantic salmon, Salmo salar Comp. Biochem. Physiol. B 101 1992 299 301
    • (1992) Comp. Biochem. Physiol. B , vol.101 , pp. 299-301
    • von der Decken, A.1
  • 64
    • 0022416087 scopus 로고
    • Major protein changes during vitellogenesis and maturation of Fundulus oocytes
    • Wallace R.A. Selman K. Major protein changes during vitellogenesis and maturation of Fundulus oocytes Dev. Biol. 110 1985 492 498
    • (1985) Dev. Biol. , vol.110 , pp. 492-498
    • Wallace, R.A.1    Selman, K.2
  • 65
    • 0036233580 scopus 로고    scopus 로고
    • Carp ovarian cystatin binds and agglutinates spermatozoa via electrostatic interaction
    • Wang S.C. Huang F.L. Carp ovarian cystatin binds and agglutinates spermatozoa via electrostatic interaction Biol. Reprod. 66 2002 1318 1327
    • (2002) Biol. Reprod. , vol.66 , pp. 1318-1327
    • Wang, S.C.1    Huang, F.L.2
  • 66
    • 0033610817 scopus 로고    scopus 로고
    • Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization
    • Wang B. Shi G.P. Yao P.M. Li Z. Chapman H.A. Bromme D. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization J. Biol. Chem. 273 1998 32000 32008
    • (1998) J. Biol. Chem. , vol.273 , pp. 32000-32008
    • Wang, B.1    Shi, G.P.2    Yao, P.M.3    Li, Z.4    Chapman, H.A.5    Bromme, D.6
  • 67
    • 0025186654 scopus 로고
    • High activities of cathepsin B, D, H, and L in the white muscle of chum salmon in spawning migration
    • Yamashita M. Konagaya S. High activities of cathepsin B, D, H, and L in the white muscle of chum salmon in spawning migration Comp. Biochem. Physiol. B 95 1990 149 152
    • (1990) Comp. Biochem. Physiol. B , vol.95 , pp. 149-152
    • Yamashita, M.1    Konagaya, S.2
  • 68
    • 0026001169 scopus 로고
    • Increase in catheptic activity and appearance of phagocytes in the white muscle of chum salmon during spawning migration
    • Yamashita M. Konagaya S. Increase in catheptic activity and appearance of phagocytes in the white muscle of chum salmon during spawning migration Biomed. Biochem. Acta 50 1991 565 567
    • (1991) Biomed. Biochem. Acta , vol.50 , pp. 565-567
    • Yamashita, M.1    Konagaya, S.2
  • 69
    • 0031903727 scopus 로고    scopus 로고
    • Purification and properties of embryonic cysteine proteinase which participates in yolk-lysis of Xenopus laevis
    • Yoshizaki N. Moriyama A. Yoneyawa S. Purification and properties of embryonic cysteine proteinase which participates in yolk-lysis of Xenopus laevis Comp. Biochem. Physiol. B 119 1998 571 576
    • (1998) Comp. Biochem. Physiol. B , vol.119 , pp. 571-576
    • Yoshizaki, N.1    Moriyama, A.2    Yoneyawa, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.