메뉴 건너뛰기




Volumn 11, Issue 4, 2012, Pages 545-557

Bestatin inhibits cell growth, cell division, and spore cell differentiation in Dictyostelium discoideum

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; BESTATIN; DRUG DERIVATIVE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; LEUCINE; PROTOZOAL PROTEIN;

EID: 84859132705     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.05311-11     Document Type: Article
Times cited : (18)

References (56)
  • 1
    • 0024696553 scopus 로고
    • A fluorimetric method for the determination of brain aminopeptidases
    • Alba F, Iríbar C, Ramírez M, Arenas C. 1989. A fluorimetric method for the determination of brain aminopeptidases. Arch. Neurobiol. (Madr.) 52:169-173.
    • (1989) Arch. Neurobiol. (Madr.) , vol.52 , pp. 169-173
    • Alba, F.1    Iríbar, C.2    Ramírez, M.3    Arenas, C.4
  • 2
    • 6944252493 scopus 로고    scopus 로고
    • Anti-tumor angiogenesis effect of aminopeptidase inhibitor bestatin against B16-BL6 melanoma cells orthotopically implanted into syngeneic mice
    • Aozuka Y, et al. 2004. Anti-tumor angiogenesis effect of aminopeptidase inhibitor bestatin against B16-BL6 melanoma cells orthotopically implanted into syngeneic mice. Cancer Lett. 216:35-42.
    • (2004) Cancer Lett. , vol.216 , pp. 35-42
    • Aozuka, Y.1
  • 3
    • 33947164372 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
    • Bhutani N, Venkatraman P, Goldberg AL. 2007. Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation. EMBO J. 26:1385-1396.
    • (2007) EMBO J. , vol.26 , pp. 1385-1396
    • Bhutani, N.1    Venkatraman, P.2    Goldberg, A.L.3
  • 4
    • 0242290371 scopus 로고    scopus 로고
    • The Caenorhabditis elegans orthologue of mammalian puromycin-sensitive aminopeptidase has roles in embryogenesis and reproduction
    • Brooks DR, Hooper NM, Isaac RE. 2003. The Caenorhabditis elegans orthologue of mammalian puromycin-sensitive aminopeptidase has roles in embryogenesis and reproduction. J. Biol. Chem. 278:42795-42801.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42795-42801
    • Brooks, D.R.1    Hooper, N.M.2    Isaac, R.E.3
  • 5
    • 0025770253 scopus 로고
    • Leucine aminopeptidase: Bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysis
    • Burley SK, David PR, Lipscomb WN. 1991. Leucine aminopeptidase: Bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysis. Proc. Natl. Acad. Sci. U. S. A. 88:6916-6920.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 6916-6920
    • Burley, S.K.1    David, P.R.2    Lipscomb, W.N.3
  • 6
    • 79955936156 scopus 로고    scopus 로고
    • Nucleolar localization and identification of nuclear/nucleolar localization signals of the calmodulin-binding protein nucleomorphin during growth and mitosis in Dictyostelium
    • Catalano A, O'Day DH. 2011. Nucleolar localization and identification of nuclear/nucleolar localization signals of the calmodulin-binding protein nucleomorphin during growth and mitosis in Dictyostelium. Histochem. Cell Biol. 135:239-249.
    • (2011) Histochem. Cell Biol. , vol.135 , pp. 239-249
    • Catalano, A.1    O'Day, D.H.2
  • 7
    • 84855227022 scopus 로고    scopus 로고
    • Dictyostelium puromycinsensitive aminopeptidase A is a nucleoplasmic nucleomorphin-binding protein that relocates to the cytoplasm during mitosis
    • Catalano A, Poloz Y, O'Day DH. 2011. Dictyostelium puromycinsensitive aminopeptidase A is a nucleoplasmic nucleomorphin-binding protein that relocates to the cytoplasm during mitosis. Histochem. Cell Biol. 136:677-688.
    • (2011) Histochem. Cell Biol. , vol.136 , pp. 677-688
    • Catalano, A.1    Poloz, Y.2    O'Day, D.H.3
  • 9
    • 0043095584 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase in rat and human esophageal adenocarcinomas and inhibitory effects of bestatin
    • Chen X, et al. 2003. Leukotriene A4 hydrolase in rat and human esophageal adenocarcinomas and inhibitory effects of bestatin. J. Natl. Cancer Inst. 95:1053-1061.
    • (2003) J. Natl. Cancer Inst. , vol.95 , pp. 1053-1061
    • Chen, X.1
  • 10
    • 0028843821 scopus 로고
    • Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization
    • Constam DB, et al. 1995. Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization. J. Biol. Chem. 270:26931-26939.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26931-26939
    • Constam, D.B.1
  • 11
    • 0029781804 scopus 로고    scopus 로고
    • Induction of apoptosis by ubenimex (Bestatin) in human non-small-cell lung cancer cell lines
    • Ezawa K, Minato K, Dobashi K. 1996. Induction of apoptosis by ubenimex (Bestatin) in human non-small-cell lung cancer cell lines. Biomed. Pharmacother. 50:283-289.
    • (1996) Biomed. Pharmacother. , vol.50 , pp. 283-289
    • Ezawa, K.1    Minato, K.2    Dobashi, K.3
  • 13
    • 0015309518 scopus 로고
    • Partial characterization of several protein and amino acid metabolizing enzymes in the cellular slime mold Dictyostelium discoideum
    • Firtel RA, Brackenbury RW. 1972. Partial characterization of several protein and amino acid metabolizing enzymes in the cellular slime mold Dictyostelium discoideum. Dev. Biol. 27:307-321.
    • (1972) Dev. Biol. , vol.27 , pp. 307-321
    • Firtel, R.A.1    Brackenbury, R.W.2
  • 14
    • 0033924129 scopus 로고    scopus 로고
    • Dictyostelium: A model for regulated cell movement during morphogenesis
    • Firtel RA, Meili R. 2000. Dictyostelium: a model for regulated cell movement during morphogenesis. Curr. Opin. Genet. Dev. 10:421-427.
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 421-427
    • Firtel, R.A.1    Meili, R.2
  • 15
    • 0038392597 scopus 로고    scopus 로고
    • Bestatin selectively suppresses the growth of leukemic stem/progenitor cells with BCR/ABL mRNA transcript in patients with chronic myelogenous leukemia
    • Fujisaki T, et al. 2003. Bestatin selectively suppresses the growth of leukemic stem/progenitor cells with BCR/ABL mRNA transcript in patients with chronic myelogenous leukemia. Int. Immunopharmacol. 3:901-907.
    • (2003) Int. Immunopharmacol. , vol.3 , pp. 901-907
    • Fujisaki, T.1
  • 16
    • 0014238667 scopus 로고
    • Use of a fluorescent brightener to demonstrate cellulose in the cellular slime molds
    • Harrington BJ, Raper KB. 1968. Use of a fluorescent brightener to demonstrate cellulose in the cellular slime molds. Appl. Microbiol. 16:106-113.
    • (1968) Appl. Microbiol. , vol.16 , pp. 106-113
    • Harrington, B.J.1    Raper, K.B.2
  • 17
    • 80052493969 scopus 로고    scopus 로고
    • Nucleocytoplasmic transfer of cyclin dependent kinase 5 and its binding partner puromycin-sensitive aminopeptidase in Dictyostelium discoideum
    • Huber RJ, O'Day DH. 2011. Nucleocytoplasmic transfer of cyclin dependent kinase 5 and its binding partner puromycin-sensitive aminopeptidase in Dictyostelium discoideum. Histochem. Cell Biol. 136:177-189.
    • (2011) Histochem. Cell Biol. , vol.136 , pp. 177-189
    • Huber, R.J.1    O'Day, D.H.2
  • 18
    • 84857557770 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor roscovitine inhibits kinase activity, cell proliferation, multicellular development, and Cdk5 nuclear translocation in Dictyostelium discoideum
    • Huber RJ, O'Day DH. 2011. The cyclin-dependent kinase inhibitor roscovitine inhibits kinase activity, cell proliferation, multicellular development, and Cdk5 nuclear translocation in Dictyostelium discoideum. J. Cell. Biochem. 113:868-876.
    • (2011) J. Cell. Biochem. , vol.113 , pp. 868-876
    • Huber, R.J.1    O'Day, D.H.2
  • 19
    • 0032553422 scopus 로고    scopus 로고
    • A novel neuron-specific aminopeptidase in rat brain synaptosomes. Its identification, purification, and characterization
    • Hui K, Saito M, Hui M. 1998. A novel neuron-specific aminopeptidase in rat brain synaptosomes. Its identification, purification, and characterization. J. Biol. Chem. 273:31053-31060.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31053-31060
    • Hui, K.1    Saito, M.2    Hui, M.3
  • 20
    • 0038364080 scopus 로고    scopus 로고
    • Randomized double-blind placebo-controlled trial of bestatin in patients with resected state I squamous-cell lung carcinoma
    • Ichinose Y, et al. 2003. Randomized double-blind placebo-controlled trial of bestatin in patients with resected state I squamous-cell lung carcinoma. J. Natl. Cancer Inst. 95:605-610.
    • (2003) J. Natl. Cancer Inst. , vol.95 , pp. 605-610
    • Ichinose, Y.1
  • 21
    • 0029563918 scopus 로고
    • Aminopeptidase inhibitor ubenimex (bestatin) inhibits the growth of human choriocarcinoma in nude mice through its direct cytostatic activity
    • Inoi K, et al. 1995. Aminopeptidase inhibitor ubenimex (bestatin) inhibits the growth of human choriocarcinoma in nude mice through its direct cytostatic activity. Anticancer Res. 15:2081-2087.
    • (1995) Anticancer Res. , vol.15 , pp. 2081-2087
    • Inoi, K.1
  • 22
    • 0034118442 scopus 로고    scopus 로고
    • Dictyostelium, a model organism for microtubulebased transport
    • Koonce MP. 2000. Dictyostelium, a model organism for microtubulebased transport. Protist 151:17-25.
    • (2000) Protist , vol.151 , pp. 17-25
    • Koonce, M.P.1
  • 23
    • 77957001690 scopus 로고    scopus 로고
    • Dictyostelium discoideum. A model system for ultrastructural analyses of cell motility and development
    • Koonce MP, Gräf R. 2010. Dictyostelium discoideum. A model system for ultrastructural analyses of cell motility and development. Methods Cell Biol. 96:197-216.
    • (2010) Methods Cell Biol. , vol.96 , pp. 197-216
    • Koonce, M.P.1    Gräf, R.2
  • 24
    • 79954492611 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase (PSA/ NPEPPS) impedes development of neuropathology in HPSA/TAUP301L double-transgenic mice
    • Kudo LC, et al. 2011. Puromycin-sensitive aminopeptidase (PSA/ NPEPPS) impedes development of neuropathology in HPSA/TAUP301L double-transgenic mice. Hum. Mol. Genet. 20:1820-1833.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1820-1833
    • Kudo, L.C.1
  • 25
    • 33745585591 scopus 로고    scopus 로고
    • Aminopeptidase inhibitor Bestatin induces HL-60 cell apoptosis through activating caspase 3
    • Lin M, He J, Cai Z, Qian W. 2001. Aminopeptidase inhibitor Bestatin induces HL-60 cell apoptosis through activating caspase 3. Zhonghua Xue Ye Xue Za Zhi. 22:348-350.
    • (2001) Zhonghua Xue Ye Xue Za Zhi. , vol.22 , pp. 348-350
    • Lin, M.1    He, J.2    Cai, Z.3    Qian, W.4
  • 26
    • 57449101615 scopus 로고    scopus 로고
    • Bestatin, an inhibitor for aminopeptidases, modulates the production of cytokines and chemokines by activated monocytes and macrophages
    • Lkhagvaa B, et al. 2008. Bestatin, an inhibitor for aminopeptidases, modulates the production of cytokines and chemokines by activated monocytes and macrophages. Cytokine 44:386-391.
    • (2008) Cytokine , vol.44 , pp. 386-391
    • Lkhagvaa, B.1
  • 27
    • 33751538073 scopus 로고    scopus 로고
    • The puromycin-sensitive aminopeptidase PAM-1 is required for meiotic exit and anteroposterior polarity in the one-cell Caenorhabditis elegans embryo
    • Lyczak R, et al. 2006. The puromycin-sensitive aminopeptidase PAM-1 is required for meiotic exit and anteroposterior polarity in the one-cell Caenorhabditis elegans embryo. Development (Camb.) 133:4281-4292.
    • (2006) Development (Camb.) , vol.133 , pp. 4281-4292
    • Lyczak, R.1
  • 28
    • 0025900047 scopus 로고
    • Relationship between nucleolar size and growth characteristics in small cell lung cancer cell lines
    • Matsumoto T, et al. 1991. Relationship between nucleolar size and growth characteristics in small cell lung cancer cell lines. Japan. J. Cancer Res. 82:820-828.
    • (1991) Japan. J. Cancer Res. , vol.82 , pp. 820-828
    • Matsumoto, T.1
  • 29
    • 77956533673 scopus 로고    scopus 로고
    • Dictyostelium possesses highly diverged presenilin/γ-secretase that regulates growth and cell-fate specification and can accurately process human APP: A system for functional studies of the presenilin/γ-secretase complex. DNMDis
    • McMains VC, Myre M, Kreppel L, Kimmel AR. 2010. Dictyostelium possesses highly diverged presenilin/γ-secretase that regulates growth and cell-fate specification and can accurately process human APP: a system for functional studies of the presenilin/γ-secretase complex. DNMDis. Models Mech. 3:581-594.
    • (2010) Models Mech. , vol.3 , pp. 581-594
    • McMains, V.C.1    Myre, M.2    Kreppel, L.3    Kimmel, A.R.4
  • 30
    • 0041836274 scopus 로고    scopus 로고
    • Bestatin results in pathophysiological changes similar to preeclampsia in rats via induction of placental apoptosis
    • Murata Y, et al. 2003. Bestatin results in pathophysiological changes similar to preeclampsia in rats via induction of placental apoptosis. Horm. Metab. Res. 35:343-348.
    • (2003) Horm. Metab. Res. , vol.35 , pp. 343-348
    • Murata, Y.1
  • 31
    • 79955571230 scopus 로고    scopus 로고
    • Deficiency of huntingtin has pleiotropic effects in the social amoeba Dictyostelium discoideum
    • Myre MA, et al. 2011. Deficiency of huntingtin has pleiotropic effects in the social amoeba Dictyostelium discoideum. PLoS Genet. 7:e1002052.
    • (2011) PLoS Genet. , vol.7
    • Myre, M.A.1
  • 32
    • 0037205488 scopus 로고    scopus 로고
    • Nucleomorphin. A novel, acidic, nuclear calmodulin-binding protein from Dictyostelium that regulates nuclear number
    • Myre MA, O'Day DH. 2002. Nucleomorphin. A novel, acidic, nuclear calmodulin-binding protein from Dictyostelium that regulates nuclear number. J. Biol. Chem. 277:19735-19744.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19735-19744
    • Myre, M.A.1    O'Day, D.H.2
  • 33
    • 7744235662 scopus 로고    scopus 로고
    • Dictyostelium nucleomorphin is a member of the BRCT-domain family of cell cycle checkpoint proteins
    • Myre MA, O'Day DH. 2004. Dictyostelium nucleomorphin is a member of the BRCT-domain family of cell cycle checkpoint proteins. Biochim. Biophys. Acta Gen. Subj. 1675:192-197.
    • (2004) Biochim. Biophys. Acta Gen. Subj. , vol.1675 , pp. 192-197
    • Myre, M.A.1    O'Day, D.H.2
  • 34
    • 6044261548 scopus 로고    scopus 로고
    • Dictyostelium calcium-binding protein 4a interacts with nucleomorphin, a BRCT-domain protein that regulates nuclear number
    • Myre MA, O'Day DH. 2004. Dictyostelium calcium-binding protein 4a interacts with nucleomorphin, a BRCT-domain protein that regulates nuclear number. Biochem. Biophys. Res. Commun. 322:665-671.
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 665-671
    • Myre, M.A.1    O'Day, D.H.2
  • 35
    • 0031040142 scopus 로고    scopus 로고
    • Clathrin heavy chain is required for spore cell but not stalk cell differentiation in Dictyostelium discoideum
    • Niswonger ML, O'Halloran TJ. 1997. Clathrin heavy chain is required for spore cell but not stalk cell differentiation in Dictyostelium discoideum. Development 124:443-451.
    • (1997) Development , vol.124 , pp. 443-451
    • Niswonger, M.L.1    O'Halloran, T.J.2
  • 36
    • 0020455308 scopus 로고
    • Proteolytic activities in Dictyostelium discoideum detected with chromogenic peptide substrates
    • North MJ. 1982. Proteolytic activities in Dictyostelium discoideum detected with chromogenic peptide substrates. Exp. Mycol. 6:345-352.
    • (1982) Exp. Mycol. , vol.6 , pp. 345-352
    • North, M.J.1
  • 37
    • 57649158941 scopus 로고    scopus 로고
    • Differentiation inducing factor-1 (DIF-1) induces gene and protein expression of the Dictyostelium nuclear calmodulin-binding protein nucleomorphin
    • O'Day DH, Poloz Y, Myre MA. 2009. Differentiation inducing factor-1 (DIF-1) induces gene and protein expression of the Dictyostelium nuclear calmodulin-binding protein nucleomorphin. Cell. Signal. 21:317-323.
    • (2009) Cell. Signal. , vol.21 , pp. 317-323
    • O'Day, D.H.1    Poloz, Y.2    Myre, M.A.3
  • 38
    • 0034987779 scopus 로고    scopus 로고
    • Male reproductive defects caused by puromycinsensitive aminopeptidase deficiency in mice
    • Osada T, et al. 2001. Male reproductive defects caused by puromycinsensitive aminopeptidase deficiency in mice. Mol. Endocrinol. 15:960-971.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 960-971
    • Osada, T.1
  • 39
    • 0034982609 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase is essential for the maternal recognition of pregnancy in mice
    • Osada T, Watanabe G, Sakaki Y, Takeuchi T. 2001. Puromycin-sensitive aminopeptidase is essential for the maternal recognition of pregnancy in mice. Mol. Endocrinol. 15:882-893.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 882-893
    • Osada, T.1    Watanabe, G.2    Sakaki, Y.3    Takeuchi, T.4
  • 40
    • 79956081199 scopus 로고    scopus 로고
    • The role of multifunctional M1 metallopeptidases in cell cycle progression
    • Peer WA. 2011. The role of multifunctional M1 metallopeptidases in cell cycle progression. Ann. Bot. 107:1171-1181.
    • (2011) Ann. Bot. , vol.107 , pp. 1171-1181
    • Peer, W.A.1
  • 41
    • 84857381075 scopus 로고    scopus 로고
    • Colchicine affects cell motility, pattern formation and stalk cell differentiation in Dictyostelium by altering calcium signaling
    • Poloz Y, O'Day DH. 2012. Colchicine affects cell motility, pattern formation and stalk cell differentiation in Dictyostelium by altering calcium signaling. Differentiation 83:185-199.
    • (2012) Differentiation , vol.83 , pp. 185-199
    • Poloz, Y.1    O'Day, D.H.2
  • 42
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings ND, Barrett AJ. 1995. Evolutionary families of metallopeptidases. Methods Enzymol. 248:183-228.
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 43
    • 16644376470 scopus 로고    scopus 로고
    • A puromycin-sensitive aminopeptidase is essential for meiosis in Arabidopsis thaliana
    • Sánchez-Morán E, Jones GH, Franklin FCH, Santos JL. 2004. A puromycin-sensitive aminopeptidase is essential for meiosis in Arabidopsis thaliana. Plant Cell 16:2895-2909.
    • (2004) Plant Cell , vol.16 , pp. 2895-2909
    • Sánchez-Morán, E.1    Jones, G.H.2    Franklin, F.C.H.3    Santos, J.L.4
  • 44
    • 0035709639 scopus 로고    scopus 로고
    • Genetic analysis of dPsa, the Drosophila orthologue of puromycin-sensitive aminopeptidase, suggests redundancy of aminopeptidases
    • Schulz C, Perezgasga L, Fuller MT. 2001. Genetic analysis of dPsa, the Drosophila orthologue of puromycin-sensitive aminopeptidase, suggests redundancy of aminopeptidases. Dev. Genes Evol. 211:581-588.
    • (2001) Dev. Genes Evol. , vol.211 , pp. 581-588
    • Schulz, C.1    Perezgasga, L.2    Fuller, M.T.3
  • 45
    • 0033046028 scopus 로고    scopus 로고
    • Induction of apoptosis by bestatin (ubenimex) in human leukemic cell lines
    • Sekine K, Fujii H, Abe F. 1999. Induction of apoptosis by bestatin (ubenimex) in human leukemic cell lines. Leukemia 13:729-734.
    • (1999) Leukemia , vol.13 , pp. 729-734
    • Sekine, K.1    Fujii, H.2    Abe, F.3
  • 46
    • 0036083190 scopus 로고    scopus 로고
    • The Cdk5 homologue, Crp, regulates endocytosis and secretion in Dictyostelium and is necessary for optimum growth and differentiation
    • Sharma SK, et al. 2002. The Cdk5 homologue, Crp, regulates endocytosis and secretion in Dictyostelium and is necessary for optimum growth and differentiation. Dev. Biol. 247:1-10.
    • (2002) Dev. Biol. , vol.247 , pp. 1-10
    • Sharma, S.K.1
  • 47
    • 0022370746 scopus 로고
    • Bestatin, a microbial aminopeptidase inhibitor, inhibits DNA synthesis induced by insulin or epidermal growth factor in primary cultured rat hepatocytes
    • Takahashi S, Kato H, Seki T. 1985. Bestatin, a microbial aminopeptidase inhibitor, inhibits DNA synthesis induced by insulin or epidermal growth factor in primary cultured rat hepatocytes. J. Antibiot. 38:1767-1773.
    • (1985) J. Antibiot. , vol.38 , pp. 1767-1773
    • Takahashi, S.1    Kato, H.2    Seki, T.3
  • 48
    • 0024428352 scopus 로고
    • The effects of bestatin, a microbial aminopeptidase inhibitor, on epidermal growth factor-induced DNA synthesis and cell division in primary cultured hepatocytes of rats
    • Takahashi S, et al. 1989. The effects of bestatin, a microbial aminopeptidase inhibitor, on epidermal growth factor-induced DNA synthesis and cell division in primary cultured hepatocytes of rats. Exp. Cell Res. 183: 399-412.
    • (1989) Exp. Cell Res. , vol.183 , pp. 399-412
    • Takahashi, S.1
  • 49
    • 0027479013 scopus 로고
    • Aminopeptidases: Structure and function
    • Taylor A. 1993. Aminopeptidases: structure and function. FASEB J. 7:290-298.
    • (1993) FASEB J. , vol.7 , pp. 290-298
    • Taylor, A.1
  • 50
    • 79960327525 scopus 로고    scopus 로고
    • Identifying an uptake mechanism for the antiepileptic and bipolar disorder treatment valproic acid using the simple biomedical model Dictyostelium
    • Terbach N, et al. 2011. Identifying an uptake mechanism for the antiepileptic and bipolar disorder treatment valproic acid using the simple biomedical model Dictyostelium. J. Cell Sci. 124:2267-2276.
    • (2011) J. Cell Sci. , vol.124 , pp. 2267-2276
    • Terbach, N.1
  • 51
    • 0030668026 scopus 로고    scopus 로고
    • Inhibitory effects of ubenimex (bestatin) on the invasion of uterine cervical carcinoma cells and their production and activation of gelatinase A
    • Ueda M, Ueki M, Fujii H, Yoshizawa K, Nakajima M. 1997. Inhibitory effects of ubenimex (bestatin) on the invasion of uterine cervical carcinoma cells and their production and activation of gelatinase A. J. Med. 28:175-190.
    • (1997) J. Med. , vol.28 , pp. 175-190
    • Ueda, M.1    Ueki, M.2    Fujii, H.3    Yoshizawa, K.4    Nakajima, M.5
  • 52
    • 0017236348 scopus 로고
    • Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes
    • Umezawa H, Aoyagi T, Suda H, Hamada M, Takeuchi T. 1976. Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes. J. Antibiot. 29:97-99.
    • (1976) J. Antibiot. , vol.29 , pp. 97-99
    • Umezawa, H.1    Aoyagi, T.2    Suda, H.3    Hamada, M.4    Takeuchi, T.5
  • 53
    • 78349285170 scopus 로고    scopus 로고
    • Dictyostelium finds new roles to model
    • Williams JG. 2010. Dictyostelium finds new roles to model. Genetics 185: 717-726.
    • (2010) Genetics , vol.185 , pp. 717-726
    • Williams, J.G.1
  • 54
    • 33745602760 scopus 로고    scopus 로고
    • Transcriptional regulation of Dictyostelium pattern formation
    • Williams JG. 2006. Transcriptional regulation of Dictyostelium pattern formation. EMBO J. 7:694-698.
    • (2006) EMBO J. , vol.7 , pp. 694-698
    • Williams, J.G.1
  • 55
    • 0037368335 scopus 로고    scopus 로고
    • Effect of bestatin on leukemic cells in acute leukemia and myelodysplastic syndromes
    • Yamada S, et al. 2003. Effect of bestatin on leukemic cells in acute leukemia and myelodysplastic syndromes. Biotherapy (Japan) 17:161-166.
    • (2003) Biotherapy (Japan) , vol.17 , pp. 161-166
    • Yamada, S.1
  • 56
    • 0036177032 scopus 로고    scopus 로고
    • Axonal transport of puromycin-sensitive aminopeptidase in rat sciatic nerves
    • Yamamoto M, et al. 2002. Axonal transport of puromycin-sensitive aminopeptidase in rat sciatic nerves. Neurosci. Res. 42:133-140.
    • (2002) Neurosci. Res. , vol.42 , pp. 133-140
    • Yamamoto, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.