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Volumn 3, Issue 8, 2004, Pages 984-987

Complete and limited proteolysis in cell cycle progression

Author keywords

Cathepsin B; Cathepsin L; CDP Cux; Furless mouse; HCF 1; Proteolytic processing; Scc1; Specific proteolysis

Indexed keywords

CATHEPSIN B; CATHEPSIN L PROTEINASE; CDP CUX PROTEIN; COHESIN; COHESIN SCC1 SUBUNIT; HYBRID PROTEIN; PROTEIN SUBUNIT; PROTEINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 13944274870     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.3.8.1025     Document Type: Review
Times cited : (29)

References (63)
  • 1
    • 0030724422 scopus 로고    scopus 로고
    • Roles of ubiquitin-mediated proteolysis in cell cycle control
    • Hershko A. Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr Opin Cell Biol 1997; 9:788-99.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 788-799
    • Hershko, A.1
  • 2
    • 0033995119 scopus 로고    scopus 로고
    • Proteolysis and the cell cycle: With this RING I do thee destroy
    • Tyers M, Jorgensen P. Proteolysis and the cell cycle: with this RING I do thee destroy. Curr Opin Genet Dev 2000; 10:54-64.
    • (2000) Curr Opin Genet Dev , vol.10 , pp. 54-64
    • Tyers, M.1    Jorgensen, P.2
  • 3
    • 0036284778 scopus 로고    scopus 로고
    • The anapbase-promoting complex: Proteolysis in mitosis and beyond
    • Peters JM. The anapbase-promoting complex: proteolysis in mitosis and beyond. Mol Cell 2002; 9:931-43.
    • (2002) Mol Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 4
    • 0033168496 scopus 로고    scopus 로고
    • Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1
    • Uhlmann F, Lottspeich F, Nasmyth K. Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1 [see comments]. Nature 1999; 400:37-42.
    • (1999) Nature , vol.400 , pp. 37-42
    • Uhlmann, F.1    Lottspeich, F.2    Nasmyth, K.3
  • 5
    • 0037311943 scopus 로고    scopus 로고
    • Chromosome cohesion and separation: From men and molecules
    • Uhlmann F. Chromosome cohesion and separation: from men and molecules. Curr Biol 2003; 13:R104-14.
    • (2003) Curr Biol , vol.13
    • Uhlmann, F.1
  • 6
    • 0038242360 scopus 로고    scopus 로고
    • Proteolytic processing is necessary to separate and ensure proper cell growth and cytokinesis functions of HCF-1
    • Julien E, Herr W, Proteolytic processing is necessary to separate and ensure proper cell growth and cytokinesis functions of HCF-1. EMBO J 2003; 22:2360-9.
    • (2003) EMBO J , vol.22 , pp. 2360-2369
    • Julien, E.1    Herr, W.2
  • 7
    • 1942470581 scopus 로고    scopus 로고
    • A Cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor
    • Goulet B, Baruch A, Moon NS, Poirier M, Sansregret LL, Erickson A, Bogyo M, Nepveu A. A Cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol Cell 2004; 14:207-19.
    • (2004) Mol Cell , vol.14 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.S.3    Poirier, M.4    Sansregret, L.L.5    Erickson, A.6    Bogyo, M.7    Nepveu, A.8
  • 8
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown MS, Ye J, Rawson RB, Goldstein JL. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 2000; 100:391-8.
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 9
    • 0035371394 scopus 로고    scopus 로고
    • Membrane-bound transcription factors: Regulated release by RIP or RUP
    • Hoppe T, Rape M, Jentsch S. Membrane-bound transcription factors: regulated release by RIP or RUP. Curr Opin Cell Biol 2001; 13:344-8.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 344-348
    • Hoppe, T.1    Rape, M.2    Jentsch, S.3
  • 10
    • 0032185770 scopus 로고    scopus 로고
    • Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells
    • Sakai J, Rawson RB, Espenshade PJ, Cheng D, Seegmiller AC, Goldstein JL, Brown MS. Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells. Mol Cell 1998; 2:505-14.
    • (1998) Mol Cell , vol.2 , pp. 505-514
    • Sakai, J.1    Rawson, R.B.2    Espenshade, P.J.3    Cheng, D.4    Seegmiller, A.C.5    Goldstein, J.L.6    Brown, M.S.7
  • 12
    • 0033618342 scopus 로고    scopus 로고
    • Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins
    • Zelenski NG, Rawson RB, Brown MS, Goldstein JL. Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins. J Biol Chem 1999; 274:21973-80.
    • (1999) J Biol Chem , vol.274 , pp. 21973-21980
    • Zelenski, N.G.1    Rawson, R.B.2    Brown, M.S.3    Goldstein, J.L.4
  • 13
    • 0028225462 scopus 로고
    • SREBP-1, a membrane-bound transcription factor released by sterol- regulated proteolysis
    • Wang X, Sato R, Brown MS, Hua X, Goldstein JL. SREBP-1, a membrane-bound transcription factor released by sterol- regulated proteolysis [see comments]. Cell 1994; 77:53-62.
    • (1994) Cell , vol.77 , pp. 53-62
    • Wang, X.1    Sato, R.2    Brown, M.S.3    Hua, X.4    Goldstein, J.L.5
  • 14
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Cell Biol 1999; 10:3787-99.
    • (1999) Mol Cell Biol , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 16
    • 0032555718 scopus 로고    scopus 로고
    • Roles for proteolysis and trafficking in notch maturation and signal transduction
    • Chan YM, Jan YN. Roles for proteolysis and trafficking in notch maturation and signal transduction. Cell 1998; 94:423-6.
    • (1998) Cell , vol.94 , pp. 423-426
    • Chan, Y.M.1    Jan, Y.N.2
  • 17
    • 0033868818 scopus 로고    scopus 로고
    • A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE
    • Brou C, Logeat F, Gupta N, Bessia C, LeBail O, Doedens JR. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol Cell 2000; 5:207-16.
    • (2000) Mol Cell , vol.5 , pp. 207-216
    • Brou, C.1    Logeat, F.2    Gupta, N.3    Bessia, C.4    LeBail, O.5    Doedens, J.R.6
  • 19
    • 0033535508 scopus 로고    scopus 로고
    • Presenilin is required for activity and nuclear access of Notch in Drosophila
    • Srruhl G, Greenwald I. Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature 1999; 398:522-5.
    • (1999) Nature , vol.398 , pp. 522-525
    • Srruhl, G.1    Greenwald, I.2
  • 20
    • 0033536072 scopus 로고    scopus 로고
    • Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations
    • Song W, Nadeau P, Yuan M, Yang X, Shen J, Yankner BA. Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations. Proc Natl Acad Sci USA 1999; 96:6959-63.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6959-6963
    • Song, W.1    Nadeau, P.2    Yuan, M.3    Yang, X.4    Shen, J.5    Yankner, B.A.6
  • 21
    • 0036315042 scopus 로고    scopus 로고
    • Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis
    • Raggo C, Rapin N, Stirling J, Gobeil P, Smith-Windsor E, O'Hare P, Misra V. Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis. Mol Cell Biol 2002; 22:5639-49.
    • (2002) Mol Cell Biol , vol.22 , pp. 5639-5649
    • Raggo, C.1    Rapin, N.2    Stirling, J.3    Gobeil, P.4    Smith-Windsor, E.5    O'Hare, P.6    Misra, V.7
  • 22
    • 0031587830 scopus 로고    scopus 로고
    • Proteolysis that is inhibited by hedgehog targets Cubitus interruptus protein to the nucleus and converts it to a repressor
    • Aza-Blanc P, Ramirez-Weber FA, Laget MP, Schwartz C, Kornberg TB, Proteolysis that is inhibited by hedgehog targets Cubitus interruptus protein to the nucleus and converts it to a repressor. Cell 1997; 89:1043-53.
    • (1997) Cell , vol.89 , pp. 1043-1053
    • Aza-Blanc, P.1    Ramirez-Weber, F.A.2    Laget, M.P.3    Schwartz, C.4    Kornberg, T.B.5
  • 24
    • 0026066613 scopus 로고
    • Generation of p50 subunit of NF-κB by processing of p105 through an ATP-dependent pathway
    • Fan CM, Maniatis T. Generation of p50 subunit of NF-κB by processing of p105 through an ATP-dependent pathway. Nature 1991; 354:395-8.
    • (1991) Nature , vol.354 , pp. 395-398
    • Fan, C.M.1    Maniatis, T.2
  • 25
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 1994; 78:773-85.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 26
    • 0032588390 scopus 로고    scopus 로고
    • C/EBPα regulates generation of C/EBPβ isoforms through activation of specific proteolytic cleavage
    • Welm AL, Timchenko NA, Darlington GJ. C/EBPα regulates generation of C/EBPβ isoforms through activation of specific proteolytic cleavage. Mol Cell Biol 1999; 19:1695-704.
    • (1999) Mol Cell Biol , vol.19 , pp. 1695-1704
    • Welm, A.L.1    Timchenko, N.A.2    Darlington, G.J.3
  • 27
    • 0030793345 scopus 로고    scopus 로고
    • Functionally distinct isoforms of STAT5 are generated by protein processing
    • Azam M, Lee C, Strehlow I, Schindler C. Functionally distinct isoforms of STAT5 are generated by protein processing. Immunity 1997; 6:691-701.
    • (1997) Immunity , vol.6 , pp. 691-701
    • Azam, M.1    Lee, C.2    Strehlow, I.3    Schindler, C.4
  • 28
    • 0034663045 scopus 로고    scopus 로고
    • Myeloid differentiation of FdCP1 cells is dependent on Stat5 processing
    • Piazza F, Valens J, Lagasse E, Schindler C. Myeloid differentiation of FdCP1 cells is dependent on Stat5 processing. Blood 2000; 96:1358-65.
    • (2000) Blood , vol.96 , pp. 1358-1365
    • Piazza, F.1    Valens, J.2    Lagasse, E.3    Schindler, C.4
  • 29
    • 0032520260 scopus 로고    scopus 로고
    • Carboxyl-truncated STAT5β is generated by a nucleus-associated serine protease in early hematopoietic progenitors
    • Meyer J, Jucker M, Ostertag W, Stocking C. Carboxyl-truncated STAT5β is generated by a nucleus-associated serine protease in early hematopoietic progenitors. Blood 1998; 91:1901-8.
    • (1998) Blood , vol.91 , pp. 1901-1908
    • Meyer, J.1    Jucker, M.2    Ostertag, W.3    Stocking, C.4
  • 31
    • 0036785569 scopus 로고    scopus 로고
    • IL-4 induces the proteolytic processing of mast cell STAT6
    • Sherman MA, Powell DR, Brown MA. IL-4 induces the proteolytic processing of mast cell STAT6. J Immunol 2002; 169:3811-8.
    • (2002) J Immunol , vol.169 , pp. 3811-3818
    • Sherman, M.A.1    Powell, D.R.2    Brown, M.A.3
  • 32
    • 0042877024 scopus 로고    scopus 로고
    • Lineage-specific negative regulation of STAT-mediated signaling by proteolytic processing
    • Nakajima H, Suzuki K, Iwamoto I. Lineage-specific negative regulation of STAT-mediated signaling by proteolytic processing. Cytokine Growth Factor Rev 2003; 14:375-80.
    • (2003) Cytokine Growth Factor Rev , vol.14 , pp. 375-380
    • Nakajima, H.1    Suzuki, K.2    Iwamoto, I.3
  • 33
    • 0026696338 scopus 로고
    • Inducible processing of interferon regulatory factor-2
    • Palombella VJ, Maniatis T. Inducible processing of interferon regulatory factor-2. Mol Cell Biol 1992; 12:3325-36.
    • (1992) Mol Cell Biol , vol.12 , pp. 3325-3336
    • Palombella, V.J.1    Maniatis, T.2
  • 34
    • 0028004110 scopus 로고
    • A truncated form of the IRF-2 transcription factor has the properties of a postinduction repressor of interferon-beta gene expression
    • Whiteside ST, King P, Goodbourn S. A truncated form of the IRF-2 transcription factor has the properties of a postinduction repressor of interferon-beta gene expression. J Biol Chem 1994; 269:27059-65.
    • (1994) J Biol Chem , vol.269 , pp. 27059-27065
    • Whiteside, S.T.1    King, P.2    Goodbourn, S.3
  • 35
    • 0034662905 scopus 로고    scopus 로고
    • Autocatalytic proteolysis of the transcription factor-coactivator C1 (HCF): A potential role for proteolytic regulation of coactivator function
    • Vogel JL, Kristie TM. Autocatalytic proteolysis of the transcription factor-coactivator C1 (HCF): a potential role for proteolytic regulation of coactivator function. Proc Nat Acad Sci USA 2000; 97:9425-30.
    • (2000) Proc Nat Acad Sci USA , vol.97 , pp. 9425-9430
    • Vogel, J.L.1    Kristie, T.M.2
  • 36
    • 0035724764 scopus 로고    scopus 로고
    • S phase-specific proteolytic cleavage is required to activate stable DNA binding by the CDP/Cut homeodomain protein
    • Moon NS, Premdas P, Truscott M, Leduy L, Berube G, Nepveu A. S phase-specific proteolytic cleavage is required to activate stable DNA binding by the CDP/Cut homeodomain protein. Mol Cell Biol 2001; 21:6332-45.
    • (2001) Mol Cell Biol , vol.21 , pp. 6332-6345
    • Moon, N.S.1    Premdas, P.2    Truscott, M.3    Leduy, L.4    Berube, G.5    Nepveu, A.6
  • 38
    • 0034613176 scopus 로고    scopus 로고
    • CCAAT displacement activity involves Cut repeats 1 and 2, not the Cut homeodomain
    • Moon NS, Berube G, Nepveu A. CCAAT displacement activity involves Cut repeats 1 and 2, not the Cut homeodomain. J Biol Chem 2000; 275:31325-34.
    • (2000) J Biol Chem , vol.275 , pp. 31325-31334
    • Moon, N.S.1    Berube, G.2    Nepveu, A.3
  • 39
    • 0032541492 scopus 로고    scopus 로고
    • The mammalian Cut homeodomain protein functions as a cell-cycle dependent transcriptional repressor which downmodulates p21WAF1/CIP1/SDI1 in S phase
    • Coqueret O, Berube G, Nepveu A. The mammalian Cut homeodomain protein functions as a cell-cycle dependent transcriptional repressor which downmodulates p21WAF1/CIP1/SDI1 in S phase. EMBO J 1998; 17:4680-94.
    • (1998) EMBO J , vol.17 , pp. 4680-4694
    • Coqueret, O.1    Berube, G.2    Nepveu, A.3
  • 41
    • 0024431313 scopus 로고
    • Human H4 histone gene transcription requires the proliferation-specific nuclear factor HiNF-D. Auxiliary roles for HiNF-C (Sp1-like) and HiNF-A (high mobility group-like)
    • van Wijnen AJ, Wright KL, Lian JB, Stein JL, Stein GS. Human H4 histone gene transcription requires the proliferation-specific nuclear factor HiNF-D. Auxiliary roles for HiNF-C (Sp1-like) and HiNF-A (high mobility group-like). J Biol Chem 1989; 264:15034-42.
    • (1989) J Biol Chem , vol.264 , pp. 15034-15042
    • Van Wijnen, A.J.1    Wright, K.L.2    Lian, J.B.3    Stein, J.L.4    Stein, G.S.5
  • 47
    • 0030039974 scopus 로고    scopus 로고
    • Appearance of nuclear protease activity after embryonal carcinoma cells undergo differentiation
    • Scholtz B, Lamb K, Rosfjord E, Kingsley M, Rizzino A. Appearance of nuclear protease activity after embryonal carcinoma cells undergo differentiation. Dev Biol 1996; 173:420-7.
    • (1996) Dev Biol , vol.173 , pp. 420-427
    • Scholtz, B.1    Lamb, K.2    Rosfjord, E.3    Kingsley, M.4    Rizzino, A.5
  • 48
    • 0032472245 scopus 로고    scopus 로고
    • A retinoblastoma susceptibility gene product, RB, targeting protease is regulated through the cell cycle
    • Fu YH, Nishinaka T, Yokoyama K, Chiu R. A retinoblastoma susceptibility gene product, RB, targeting protease is regulated through the cell cycle. FEBS Lett 1998; 421:89-93.
    • (1998) FEBS Lett , vol.421 , pp. 89-93
    • Fu, Y.H.1    Nishinaka, T.2    Yokoyama, K.3    Chiu, R.4
  • 49
    • 0032509203 scopus 로고    scopus 로고
    • Intracellular proteolytic cleavage of 9-cis-retinoic acid receptor alpha by cathepsin L-type protease is a potential mechanism for modulating thyroid hormone action
    • Nagaya T, Murata Y, Yamaguchi S, Nomura Y, Ohmori S, Fujieda M, Katunuma N, Yen PM, Chin WW, Seo H. Intracellular proteolytic cleavage of 9-cis-retinoic acid receptor alpha by cathepsin L-type protease is a potential mechanism for modulating thyroid hormone action. J Biol Chem 1998; 273:33166-73.
    • (1998) J Biol Chem , vol.273 , pp. 33166-33173
    • Nagaya, T.1    Murata, Y.2    Yamaguchi, S.3    Nomura, Y.4    Ohmori, S.5    Fujieda, M.6    Katunuma, N.7    Yen, P.M.8    Chin, W.W.9    Seo, H.10
  • 50
    • 0030990586 scopus 로고    scopus 로고
    • A unique cathepsin-like protease isolated from CV-1 cells is involved in rapid degradation of retinoblastoma susceptibility gene product, RB, and transcription factor SP1
    • Nishinaka T, Fu YH, Chen LI, Yokoyama K, Chiu R. A unique cathepsin-like protease isolated from CV-1 cells is involved in rapid degradation of retinoblastoma susceptibility gene product, RB, and transcription factor SP1. Biochim Biophys Acta 1997; 1351:274-86.
    • (1997) Biochim Biophys Acta , vol.1351 , pp. 274-286
    • Nishinaka, T.1    Fu, Y.H.2    Chen, L.I.3    Yokoyama, K.4    Chiu, R.5
  • 52
    • 0035971742 scopus 로고    scopus 로고
    • Nuclear cathepsin B-like protease cleaves transcription factor YY1 in differentiated cells
    • Pizzorno MC. Nuclear cathepsin B-like protease cleaves transcription factor YY1 in differentiated cells. Biochim Biophys Acta 2001; 1536:31-42.
    • (2001) Biochim Biophys Acta , vol.1536 , pp. 31-42
    • Pizzorno, M.C.1
  • 53
    • 0030032833 scopus 로고    scopus 로고
    • Nuclear localization of procathepsin L/MEP in ras-transformed mouse fibroblasts
    • Hiwasa T, Sakiyama S. Nuclear localization of procathepsin L/MEP in ras-transformed mouse fibroblasts. Cancer Lett 1996; 99:87-91.
    • (1996) Cancer Lett , vol.99 , pp. 87-91
    • Hiwasa, T.1    Sakiyama, S.2
  • 54
    • 0035862167 scopus 로고    scopus 로고
    • Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonus epilepsy (EPM1)
    • Riccio M, Di Giaimo R, Pianetti S, Palmieri PP, Melli M, Santi S. Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonus epilepsy (EPM1). Exp Cell Res 2001; 262:84-94.
    • (2001) Exp Cell Res , vol.262 , pp. 84-94
    • Riccio, M.1    Di Giaimo, R.2    Pianetti, S.3    Palmieri, P.P.4    Melli, M.5    Santi, S.6
  • 55
    • 0027319177 scopus 로고
    • Characterization of the cathepsin B gene and multiple mRNAs in human tissues: Evidence for alternative splicing of cathepsin B pre-mRNA
    • Gong Q, Chan SJ, Bajkowski AS, Steiner DF, Frankfater A. Characterization of the cathepsin B gene and multiple mRNAs in human tissues: evidence for alternative splicing of cathepsin B pre-mRNA. DNA Cell Biol 1993; 12:299-309.
    • (1993) DNA Cell Biol , vol.12 , pp. 299-309
    • Gong, Q.1    Chan, S.J.2    Bajkowski, A.S.3    Steiner, D.F.4    Frankfater, A.5
  • 56
    • 0029048724 scopus 로고
    • Identification of two new exons and multiple transcription start points in the 5′-untranslated region of the human cathepsin-B-encoding gene
    • Berquin IM, Cao L, Fong D, Sloane BF. Identification of two new exons and multiple transcription start points in the 5′-untranslated region of the human cathepsin-B-encoding gene. Gene 1995; 159:143-9.
    • (1995) Gene , vol.159 , pp. 143-149
    • Berquin, I.M.1    Cao, L.2    Fong, D.3    Sloane, B.F.4
  • 57
    • 0032557529 scopus 로고    scopus 로고
    • In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B. Subcellular distribution of the truncated enzyme in COS cells
    • Mehtani S, Gong Q, Panella J, Subbiah S, Peffley DM, Franktater A. In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B. Subcellular distribution of the truncated enzyme in COS cells. J Biol Chem 1998; 273:13236-44.
    • (1998) J Biol Chem , vol.273 , pp. 13236-13244
    • Mehtani, S.1    Gong, Q.2    Panella, J.3    Subbiah, S.4    Peffley, D.M.5    Franktater, A.6
  • 58
    • 0036479227 scopus 로고    scopus 로고
    • Cathepsin L is essential for embryogenesis and development of Caenorhabditis elegans
    • Hashmi S, Britton C, Liu J, Guiliano DB, Oksov Y, Lustigman S. Cathepsin L is essential for embryogenesis and development of Caenorhabditis elegans. J Biol Chem 2002; 277:3477-86.
    • (2002) J Biol Chem , vol.277 , pp. 3477-3486
    • Hashmi, S.1    Britton, C.2    Liu, J.3    Guiliano, D.B.4    Oksov, Y.5    Lustigman, S.6
  • 59
    • 0346157317 scopus 로고    scopus 로고
    • Shrimp cathepsin L encoded by an intronless gene has predominant expression in hepatopancreas, and occurs in the nucleus of oocyte
    • Hu KJ, Leung PC. Shrimp cathepsin L encoded by an intronless gene has predominant expression in hepatopancreas, and occurs in the nucleus of oocyte. Comp Biochem Physiol B Biochem Mol Biol 2004; 137:21-33.
    • (2004) Comp Biochem Physiol B Biochem Mol Biol , vol.137 , pp. 21-33
    • Hu, K.J.1    Leung, P.C.2
  • 60
    • 0025733588 scopus 로고
    • Transformation of sensory organ identity by ectopic expression of Cut in Drosophila
    • Blochlinger K, Jan LY, Jan YN. Transformation of sensory organ identity by ectopic expression of Cut in Drosophila. Genes Dev 1991; 5:1124-35.
    • (1991) Genes Dev , vol.5 , pp. 1124-1135
    • Blochlinger, K.1    Jan, L.Y.2    Jan, Y.N.3
  • 61
    • 0023663120 scopus 로고
    • Transformation of sensory organs by mutations of the cut locus of D. melanogaster
    • Bodmer R, Barbel S, Shepherd S, Jack JW, Jan LY, Jan YN. Transformation of sensory organs by mutations of the cut locus of D. melanogaster. Cell 1987; 51:293-307.
    • (1987) Cell , vol.51 , pp. 293-307
    • Bodmer, R.1    Barbel, S.2    Shepherd, S.3    Jack, J.W.4    Jan, L.Y.5    Jan, Y.N.6
  • 62
    • 0036968842 scopus 로고    scopus 로고
    • Impaired hair follicle morphogenesis and cycling with abnormal epidermal differentiation in nackt mice, a cathepsin L-deficient mutation
    • Benavides F, Starost MF, Flores M, Gimenez-Conti IB, Guenet JL, Conti CJ. Impaired hair follicle morphogenesis and cycling with abnormal epidermal differentiation in nackt mice, a cathepsin L-deficient mutation. Am J Pathol 2002; 161:693-703.
    • (2002) Am J Pathol , vol.161 , pp. 693-703
    • Benavides, F.1    Starost, M.F.2    Flores, M.3    Gimenez-Conti, I.B.4    Guenet, J.L.5    Conti, C.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.