메뉴 건너뛰기




Volumn 386, Issue 1-2, 2007, Pages 98-106

Phylogenetic relationships and gene expression pattern of three different cathepsin L (Ctsl) isoforms in zebrafish: Ctsla is the putative yolk processing enzyme

Author keywords

Expression pattern; Isoforms; Killifish; Yolk syncytial layer

Indexed keywords

CATHEPSIN L; CYSTEINE PROTEINASE; ISOENZYME; MESSENGER RNA; PROTEIN CTSLA; PROTEIN CTSLB; PROTEIN CTSLC;

EID: 33845565360     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2006.08.018     Document Type: Article
Times cited : (64)

References (57)
  • 1
    • 0028923541 scopus 로고
    • Alignment/phylogeny of the papain superfamily of cysteine proteases
    • Berti P.J., and Storer A.C. Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246 (1995) 273-283
    • (1995) J. Mol. Biol. , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 2
    • 8744307040 scopus 로고    scopus 로고
    • Cathepsin L protease (CPL-1) is essential for yolk processing during embryogenesis in Caenorhabditis elegans
    • Britton C., and Murray L. Cathepsin L protease (CPL-1) is essential for yolk processing during embryogenesis in Caenorhabditis elegans. J. Cell Sci. 117 (2004) 5133-5143
    • (2004) J. Cell Sci. , vol.117 , pp. 5133-5143
    • Britton, C.1    Murray, L.2
  • 3
    • 0028566012 scopus 로고
    • A novel family of cathepsin L-like (CTSLL) sequences on human chromosome 10q and related transcripts
    • Bryce S.D., et al. A novel family of cathepsin L-like (CTSLL) sequences on human chromosome 10q and related transcripts. Genomics 24 (1994) 568-576
    • (1994) Genomics , vol.24 , pp. 568-576
    • Bryce, S.D.1
  • 4
    • 18144398616 scopus 로고    scopus 로고
    • PGF2alpha induced differential expression of genes involved in turnover of extracellular matrix in rat decidual cells
    • Callegari E.A., Ferguson-Gottschall S., and Gibori G. PGF2alpha induced differential expression of genes involved in turnover of extracellular matrix in rat decidual cells. Reprod. Biol. Endocrinol. 3 (2005) 3
    • (2005) Reprod. Biol. Endocrinol. , vol.3 , pp. 3
    • Callegari, E.A.1    Ferguson-Gottschall, S.2    Gibori, G.3
  • 5
    • 0032918875 scopus 로고    scopus 로고
    • Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: involvement of two lysosomal proteases
    • Carnevali O., Carletta R., Cambi A., Vita A., and Bromage N. Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: involvement of two lysosomal proteases. 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
    • 0035509860 scopus 로고    scopus 로고
    • Changes of lysosomal enzyme activities in sea bass (Dicentrarchus labrax) eggs and developing embryos
    • Carnevalli O., Mosconi G., Cambi A., Ridolfi S., Zanuy S., and Polzonetti-Magni A.M. Changes of lysosomal enzyme activities in sea bass (Dicentrarchus labrax) eggs and developing embryos. Aquaculture 202 (2001) 249-256
    • (2001) Aquaculture , vol.202 , pp. 249-256
    • Carnevalli, O.1    Mosconi, G.2    Cambi, A.3    Ridolfi, S.4    Zanuy, S.5    Polzonetti-Magni, A.M.6
  • 9
    • 0030199882 scopus 로고    scopus 로고
    • Pattern of vitellogenesis and follicle maturational competence during the ovarian follicular cycle of Fundulus heteroclitus
    • Cerdà J., Calman B.G., LaFleur Jr. G.J., and Limesand S. Pattern of vitellogenesis and follicle maturational competence during the ovarian follicular cycle of Fundulus heteroclitus. Gen. Comp. Endocrinol. 103 (1996) 24-35
    • (1996) Gen. Comp. Endocrinol. , vol.103 , pp. 24-35
    • Cerdà, J.1    Calman, B.G.2    LaFleur Jr., G.J.3    Limesand, S.4
  • 10
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S., and Cygler M. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15 (1996) 5492-5503
    • (1996) EMBO J. , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Menard, R.4    Mort, J.S.5    Cygler, M.6
  • 11
    • 0942265428 scopus 로고    scopus 로고
    • Ovarian cysteine proteases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation
    • Fabra M., and Cerdà J. Ovarian cysteine proteases 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    Cerdà, J.2
  • 12
    • 33746008840 scopus 로고    scopus 로고
    • Yolk proteolysis and aquaporin-1o play essential roles to regulate fish oocyte hydration during meiosis resumption
    • Fabra M., Raldúa D., Bozzo M.G., Deen P.M.T., Lubzens E., and Cerdà J. Yolk proteolysis and aquaporin-1o play essential roles to regulate fish oocyte hydration during meiosis resumption. Dev. Biol. 295 (2006) 250-262
    • (2006) Dev. Biol. , vol.295 , pp. 250-262
    • Fabra, M.1    Raldúa, D.2    Bozzo, M.G.3    Deen, P.M.T.4    Lubzens, E.5    Cerdà, J.6
  • 13
    • 0029583839 scopus 로고
    • Regulation of yolk degradation, or how to make sleepy lysosomes
    • Fagotto F. Regulation of yolk degradation, or how to make sleepy lysosomes. J. Cell Sci. 108 (1995) 3645-3647
    • (1995) J. Cell Sci. , vol.108 , pp. 3645-3647
    • Fagotto, F.1
  • 14
    • 0023778543 scopus 로고
    • Isolation and sequence of a cDNA for human pro-(cathepsin L)
    • Gal S., and Gottesman M.M. Isolation and sequence of a cDNA for human pro-(cathepsin L). Biochem. J. 253 (1988) 303-306
    • (1988) Biochem. J. , vol.253 , pp. 303-306
    • Gal, S.1    Gottesman, M.M.2
  • 15
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/N
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/N. Nucleic Acids Symp. Ser. 41 (1999) 95-98
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 16
    • 77956813833 scopus 로고
    • Yolk absorption in embryonic and larval fishes
    • Hoar W.S., and Randall D.J. (Eds), Academic Press, New York
    • Heming T.A., and Buddington R.K. Yolk absorption in embryonic and larval fishes. In: Hoar W.S., and Randall D.J. (Eds). Fish Physiology vol. 11A (1988), Academic Press, New York 407-446
    • (1988) Fish Physiology , vol.11 A , pp. 407-446
    • Heming, T.A.1    Buddington, R.K.2
  • 17
    • 0036006819 scopus 로고    scopus 로고
    • Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids
    • Hiramatsu N., Ichikawa N., Fukada H., Fujita T., Sullivan C.V., and Hara A. Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids. J. Exp. Zool. 292 (2002) 11-25
    • (2002) J. Exp. Zool. , vol.292 , pp. 11-25
    • Hiramatsu, N.1    Ichikawa, N.2    Fukada, H.3    Fujita, T.4    Sullivan, C.V.5    Hara, A.6
  • 18
    • 26244445000 scopus 로고    scopus 로고
    • The lysosomal cysteine proteases in MHC class II antigen presentation
    • Hsing L.C., and Rudensky A.Y. The lysosomal cysteine proteases in MHC class II antigen presentation. Immunol. Rev. 207 (2005) 229-241
    • (2005) Immunol. Rev. , vol.207 , pp. 229-241
    • Hsing, L.C.1    Rudensky, A.Y.2
  • 19
    • 28244490929 scopus 로고    scopus 로고
    • Duplication events and the evolution of segmental identity
    • Hurley I., Hale M.E., and Prince V.E. Duplication events and the evolution of segmental identity. Evol. Dev. 7 (2005) 556-567
    • (2005) Evol. Dev. , vol.7 , pp. 556-567
    • Hurley, I.1    Hale, M.E.2    Prince, V.E.3
  • 20
    • 0033616978 scopus 로고    scopus 로고
    • Genomic organization and chromosomal localization of the human cathepsin L2 gene
    • Itoh R., Kawamoto S., Adachi W., Kinoshita S., and Okubo K. Genomic organization and chromosomal localization of the human cathepsin L2 gene. DNA Res. 6 (1999) 137-140
    • (1999) DNA Res. , vol.6 , pp. 137-140
    • Itoh, R.1    Kawamoto, S.2    Adachi, W.3    Kinoshita, S.4    Okubo, K.5
  • 21
    • 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 431 (2004) 946-957
    • (2004) Nature , vol.431 , pp. 946-957
    • Jaillon, O.1
  • 22
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer K.M., Peiffer S.L., and DiTomas M.E. Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 3063-3067
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    DiTomas, M.E.3
  • 23
    • 0001808598 scopus 로고    scopus 로고
    • Cathepsin L in eggs and larvae of perch Perca fluviatilis: variations with developmental stage and spawning period
    • Kestemont P., Cooremans J., Abi-Ayad A., and Mélardet C. Cathepsin L in eggs and larvae of perch Perca fluviatilis: variations with developmental stage and spawning period. Fish Physiol. Biochem. 21 (1999) 59-64
    • (1999) Fish Physiol. Biochem. , vol.21 , pp. 59-64
    • Kestemont, P.1    Cooremans, J.2    Abi-Ayad, A.3    Mélardet, C.4
  • 24
    • 0035184222 scopus 로고    scopus 로고
    • Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss)
    • Kwon J.Y., Prat F., Randall C., and Tyler C.R. Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss). Biol. Reprod. 65 (2001) 1701-1709
    • (2001) Biol. Reprod. , vol.65 , pp. 1701-1709
    • Kwon, J.Y.1    Prat, F.2    Randall, C.3    Tyler, C.R.4
  • 25
    • 25144498370 scopus 로고    scopus 로고
    • Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus
    • LaFleur Jr. G.J., et al. 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 Jr., G.J.1
  • 26
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille F., Kaleta J., and Bromme D. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 102 (2002) 4459-4488
    • (2002) Chem. Rev. , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Bromme, D.3
  • 27
    • 0033199056 scopus 로고    scopus 로고
    • Two forms of vitellogenin, yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs
    • Matsubara T., Ohkubo N., Andoh T., Sullivan C.V., and Hara A. Two forms of vitellogenin, yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs. Dev. Biol. 213 (1999) 18-32
    • (1999) Dev. Biol. , vol.213 , pp. 18-32
    • Matsubara, T.1    Ohkubo, N.2    Andoh, T.3    Sullivan, C.V.4    Hara, A.5
  • 28
    • 8844283297 scopus 로고    scopus 로고
    • Multiple vitellogenins and their unique roles in marine teleosts
    • Matsubara T., et al. Multiple vitellogenins and their unique roles in marine teleosts. Fish Physiol. Biochem. 28 (2003) 295-299
    • (2003) Fish Physiol. Biochem. , vol.28 , pp. 295-299
    • Matsubara, T.1
  • 30
    • 0031030808 scopus 로고    scopus 로고
    • Crystal structure of human cathepsin K complexed with a potent inhibitor
    • McGrath M.E., Klaus J.L., Barnes M.G., and Brömme D. Crystal structure of human cathepsin K complexed with a potent inhibitor. Nat. Struct. Biol. 4 (1997) 105-109
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 105-109
    • McGrath, M.E.1    Klaus, J.L.2    Barnes, M.G.3    Brömme, D.4
  • 31
    • 0030897758 scopus 로고    scopus 로고
    • Inhibition of gastrulation in Xenopus embryos by an antibody against a cathepsin L-like protease
    • Miyata S., and Kubo T. Inhibition of gastrulation in Xenopus embryos by an antibody against a cathepsin L-like protease. Dev. Growth Differ. 39 (1997) 111-115
    • (1997) Dev. Growth Differ. , vol.39 , pp. 111-115
    • Miyata, S.1    Kubo, T.2
  • 32
    • 0025637072 scopus 로고
    • Yolk phosphoprotein metabolism during early development of the fish, Oryzias latipes
    • Murakami M., Iuchi I., and Yamagami K. Yolk phosphoprotein metabolism during early development of the fish, Oryzias latipes. Dev. Growth Differ. 32 (1990) 619-627
    • (1990) Dev. Growth Differ. , vol.32 , pp. 619-627
    • Murakami, M.1    Iuchi, I.2    Yamagami, K.3
  • 33
    • 0037767281 scopus 로고    scopus 로고
    • Genome size evolution in pufferfish: a comparative analysis of diodontid and tetraodontid pufferfish genomes
    • Neafsey D.E., and Palumbi S.R. Genome size evolution in pufferfish: a comparative analysis of diodontid and tetraodontid pufferfish genomes. Genome Res. 13 (2003) 821-830
    • (2003) Genome Res. , vol.13 , pp. 821-830
    • Neafsey, D.E.1    Palumbi, S.R.2
  • 34
    • 0020460737 scopus 로고
    • A major developmental transition in early Xenopus embryos: II Control of the onset of transcription
    • Newport J., and Kirschner M. A major developmental transition in early Xenopus embryos: II Control of the onset of transcription. Cell 30 (1982) 687-696
    • (1982) Cell , vol.30 , pp. 687-696
    • Newport, J.1    Kirschner, M.2
  • 35
    • 0023661275 scopus 로고
    • Specific proteolysis regulated fusion between endocytic compartments in Xenopus oocytes
    • Opresko L.K., and Karpf R.A. Specific proteolysis regulated 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.A.2
  • 37
    • 33845591487 scopus 로고    scopus 로고
    • Submission and Curation of Gene Expression Data
    • Rauch G.J., et al. Submission and Curation of Gene Expression Data. ZFIN Direct Data Submission (2003)
    • (2003) ZFIN Direct Data Submission
    • Rauch, G.J.1
  • 38
    • 0033810653 scopus 로고    scopus 로고
    • Cathepsin L deficiency as molecular defect of furless: hyperproliferation of keratinocytes and pertubation of hair follicle cycling
    • Roth W., et al. Cathepsin L deficiency as molecular defect of furless: hyperproliferation of keratinocytes and pertubation of hair follicle cycling. FASEB J. 14 (2000) 2075-2086
    • (2000) FASEB J. , vol.14 , pp. 2075-2086
    • Roth, W.1
  • 39
    • 0035421972 scopus 로고    scopus 로고
    • Bafilomycin A1 inhibits proteolytic cleavage and hydration but not yolk crystal disassembly or meiosis during maturation of sea bass oocytes
    • Selman K., Wallace R.A., and Cerdà J. Bafilomycin A1 inhibits proteolytic cleavage and hydration but not yolk crystal disassembly or meiosis during maturation of sea bass oocytes. J. Exp. Zool. 290 (2001) 265-278
    • (2001) J. Exp. Zool. , vol.290 , pp. 265-278
    • Selman, K.1    Wallace, R.A.2    Cerdà, J.3
  • 40
    • 0028095918 scopus 로고
    • Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout
    • Sire M.F., Babin P.J., and Vernier J.M. Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout. J. Exp. Zool. 269 (1994) 69-83
    • (1994) J. Exp. Zool. , vol.269 , pp. 69-83
    • Sire, M.F.1    Babin, P.J.2    Vernier, J.M.3
  • 41
    • 0037168586 scopus 로고    scopus 로고
    • Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
    • Strausberg R.L., et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 16899-16903
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16899-16903
    • Strausberg, R.L.1
  • 42
    • 32644482495 scopus 로고    scopus 로고
    • Expression of the zebrafish genome during embryogenesis (NIH R01 RR15402)
    • Thisse B. Expression of the zebrafish genome during embryogenesis (NIH R01 RR15402). ZFIN Direct Data Submission (2001)
    • (2001) ZFIN Direct Data Submission
    • Thisse, B.1
  • 43
    • 3342981522 scopus 로고    scopus 로고
    • Expression patterns of three estrogen receptor genes during zebrafish (Danio rerio) development: evidence for high expression in neuromasts
    • Tingaud-Sequeira A., Forgue J.A.M., Barthe C., and Babin P.J. Expression patterns of three estrogen receptor genes during zebrafish (Danio rerio) development: evidence for high expression in neuromasts. Gene Expr. Patterns 4 (2004) 561-568
    • (2004) Gene Expr. Patterns , vol.4 , pp. 561-568
    • Tingaud-Sequeira, A.1    Forgue, J.A.M.2    Barthe, C.3    Babin, P.J.4
  • 44
    • 0036097449 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin L is an important regulator of keratinocyte and melanocyte differentiation during hair follicle morphogenesis and cycling
    • Tobin D.J., et al. The lysosomal protease cathepsin L is an important regulator of keratinocyte and melanocyte differentiation during hair follicle morphogenesis and cycling. Am. J. Pathol. 160 (2002) 1807-1821
    • (2002) Am. J. Pathol. , vol.160 , pp. 1807-1821
    • Tobin, D.J.1
  • 45
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: more than scavengers
    • Turk B., Turk D., and Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta 1477 (2000) 98-111
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 46
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: facts and opportunities
    • Turk V., Turk B., and Turk D. Lysosomal cysteine proteases: facts and opportunities. EMBO J. 20 (2001) 4629-4633
    • (2001) EMBO J. , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 47
    • 0344484133 scopus 로고    scopus 로고
    • Oocyte growth and development in teleosts
    • Tyler C.R., and Sumpter J.P. Oocyte growth and development in teleosts. Rev. Fish Biol. Fish. 6 (1996) 287-318
    • (1996) Rev. Fish Biol. Fish. , vol.6 , pp. 287-318
    • Tyler, C.R.1    Sumpter, J.P.2
  • 48
    • 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
  • 49
    • 0001001066 scopus 로고    scopus 로고
    • Expression of a zebrafish cathepsin L gene in anterior mesendoderm and hatching gland
    • Vogel A.M., and Gerster T. Expression of a zebrafish cathepsin L gene in anterior mesendoderm and hatching gland. Dev. Genes Evol. 206 (1997) 477-479
    • (1997) Dev. Genes Evol. , vol.206 , pp. 477-479
    • Vogel, A.M.1    Gerster, T.2
  • 50
    • 0022163146 scopus 로고
    • Vitellogenesis and oocyte growth in non-mammalian vertebrates
    • Browder L.W. (Ed), Plenum Press, New York
    • Wallace R.A. Vitellogenesis and oocyte growth in non-mammalian vertebrates. In: Browder L.W. (Ed). Developmental Biology vol. 1 (1985), Plenum Press, New York 127-177
    • (1985) Developmental Biology , vol.1 , pp. 127-177
    • Wallace, R.A.1
  • 51
    • 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., and Brömme 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    Brömme, D.6
  • 53
    • 0034470261 scopus 로고    scopus 로고
    • Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like cysteine proteases
    • Wex T., Levy B., Wex H., and Bromme D. Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like cysteine proteases. Adv. Exp. Med. Biol. 477 (2000) 271-280
    • (2000) Adv. Exp. Med. Biol. , vol.477 , pp. 271-280
    • Wex, T.1    Levy, B.2    Wex, H.3    Bromme, D.4
  • 54
    • 0042924384 scopus 로고    scopus 로고
    • Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter
    • Yasothornsrikul S., et al. Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 9590-9595
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9590-9595
    • Yasothornsrikul, S.1
  • 55
    • 0028023542 scopus 로고
    • Cathepsin D activity in the vitellogenesis of Xenopus laevis
    • Yoshizaki N., and Yonezawa S. Cathepsin D activity in the vitellogenesis of Xenopus laevis. Dev. Growth Differ. 36 (1994) 299-306
    • (1994) Dev. Growth Differ. , vol.36 , pp. 299-306
    • Yoshizaki, N.1    Yonezawa, S.2
  • 56
    • 0031761930 scopus 로고    scopus 로고
    • Cysteine protease plays a key role for the initiation of yolk digestion during development of Xenopus laevis
    • Yoshizaki N., and Yonezawa S. Cysteine protease plays a key role for the initiation of yolk digestion during development of Xenopus laevis. Dev. Growth Differ. 40 (1998) 659-667
    • (1998) Dev. Growth Differ. , vol.40 , pp. 659-667
    • Yoshizaki, N.1    Yonezawa, S.2
  • 57
    • 0031903727 scopus 로고    scopus 로고
    • Purification and properties of embryonic cysteine protease which participates in yolk-lysis of Xenopus laevis
    • Yoshizaki N., Moriyama A., and Yonezawa S. Purification and properties of embryonic cysteine protease which participates in yolk-lysis of Xenopus laevis. Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. 119 (1998) 571-576
    • (1998) Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. , vol.119 , pp. 571-576
    • Yoshizaki, N.1    Moriyama, A.2    Yonezawa, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.