메뉴 건너뛰기




Volumn 46, Issue 4, 2014, Pages 793-808

Positioning of aminopeptidase inhibitors in next generation cancer therapy

Author keywords

Amino acids; Aminopeptidase inhibitors; Aminopeptidases; Bestatin; Tosedostat

Indexed keywords

AMINOPEPTIDASE; ANTINEOPLASTIC AGENT; ENZYME INHIBITOR;

EID: 84898840991     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-013-1648-0     Document Type: Review
Times cited : (82)

References (116)
  • 2
    • 0017849792 scopus 로고
    • Amastatin, an inhibitor of aminopeptidase A, produced by actinomycetes
    • 681249
    • Aoyagi T, Tobe H, Kojima F, Hamada M (1978) Amastatin, an inhibitor of aminopeptidase A, produced by actinomycetes. J Antibiot 31:636-638
    • (1978) J Antibiot , vol.31 , pp. 636-638
    • Aoyagi, T.1    Tobe, H.2    Kojima, F.3    Hamada, M.4
  • 3
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • 9668046
    • Beninga J, Rock KL, Goldberg A (1998) Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J Biol Chem 273:18734-18742
    • (1998) J Biol Chem , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.3
  • 4
    • 33947164372 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
    • 10.1038/sj.emboj.7601592 1817637 17318184
    • Bhutani N, Venkatraman P, Goldberg A (2007) Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation. EMBO J 26:1385-1396. doi: 10.1038/sj.emboj.7601592
    • (2007) EMBO J , vol.26 , pp. 1385-1396
    • Bhutani, N.1    Venkatraman, P.2    Goldberg, A.3
  • 5
    • 84856935252 scopus 로고    scopus 로고
    • The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing
    • 10.1021/bi201230p 22106953
    • Birtley JR, Saridakis E, Stratikos E, Mavridis IM (2012) The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing. Biochemistry 51:286-295. doi: 10.1021/bi201230p
    • (2012) Biochemistry , vol.51 , pp. 286-295
    • Birtley, J.R.1    Saridakis, E.2    Stratikos, E.3    Mavridis, I.M.4
  • 6
    • 0018346865 scopus 로고
    • Degradation of abnormal proteins in intact mouse reticulocytes: Accumulation of intermediates in the presence of bestatin
    • Botbol V, Scornik O (1979) Degradation of abnormal proteins in intact mouse reticulocytes: accumulation of intermediates in the presence of bestatin. Proc Natl Acad Sci USA 76:703-710
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 703-710
    • Botbol, V.1    Scornik, O.2
  • 7
    • 0025913625 scopus 로고
    • Measurement of instant rates of protein degradation in the livers of intact mice by the accumulation of bestatin-induced peptides
    • 1989975
    • Botbol V, Scornik O (1991) Measurement of instant rates of protein degradation in the livers of intact mice by the accumulation of bestatin-induced peptides. J Biol Chem 266:2151-2157
    • (1991) J Biol Chem , vol.266 , pp. 2151-2157
    • Botbol, V.1    Scornik, O.2
  • 8
    • 67349265997 scopus 로고    scopus 로고
    • Leukocyte lipid bodies - Biogenesis and functions in inflammation
    • 10.1016/j.bbalip.2009.01.005 2693476 19416659
    • Bozza PT, Magalhães KG, Weller PF (2009) Leukocyte lipid bodies - biogenesis and functions in inflammation. Biochim Biophys Acta 1791:540-551. doi: 10.1016/j.bbalip.2009.01.005
    • (2009) Biochim Biophys Acta , vol.1791 , pp. 540-551
    • Bozza, P.T.1    Magalhães, K.G.2    Weller, P.F.3
  • 9
    • 0043095584 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase in rat and human esophageal adenocarcinomas and inhibitory effects of bestatin
    • 12865451
    • Chen X, Li N, Wang S, Wu N, Hong J, Jiao X, Krasna MJ, Beer DG, Yang CS (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    Li, N.2    Wang, S.3    Wu, N.4    Hong, J.5    Jiao, X.6    Krasna, M.J.7    Beer, D.G.8    Yang, C.S.9
  • 10
    • 84864376114 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum aminopeptidases in health and disease: From infection to cancer
    • 10.3390/ijms13078338 3430237 22942706
    • Cifaldi L, Romania P, Lorenzi S, Locatelli F, Fruci D (2012) Role of endoplasmic reticulum aminopeptidases in health and disease: from infection to cancer. Int J Mol Sci 13:8338-8352. doi: 10.3390/ijms13078338
    • (2012) Int J Mol Sci , vol.13 , pp. 8338-8352
    • Cifaldi, L.1    Romania, P.2    Lorenzi, S.3    Locatelli, F.4    Fruci, D.5
  • 11
    • 0028843821 scopus 로고
    • Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization
    • 7592939
    • Constam DB, Tobler AR, Rensing-ehl A, Kemler I, Hersh LB, Fontana A (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    Tobler, A.R.2    Rensing-Ehl, A.3    Kemler, I.4    Hersh, L.B.5    Fontana, A.6
  • 12
    • 80054760140 scopus 로고    scopus 로고
    • Effect of the leukotriene A4 hydrolase aminopeptidase augmentor 4-methoxydiphenylmethane in a pre-clinical model of pulmonary emphysema
    • 10.1016/j.bmcl.2011.09.048.Effect 3209762 21983441
    • De Oliveira E, Wang K, Kong H (2011) Effect of the leukotriene A4 hydrolase aminopeptidase augmentor 4-methoxydiphenylmethane in a pre-clinical model of pulmonary emphysema. Bioorg Med Chem Lett 21:6746-6750. doi: 10.1016/j.bmcl.2011.09.048.Effect
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 6746-6750
    • De Oliveira, E.1    Wang, K.2    Kong, H.3
  • 13
    • 0033961824 scopus 로고    scopus 로고
    • Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells
    • 10605003
    • Dong X, An B, Salvucci Kierstead L, Storkus WJ, Amoscato AA, Salter RD (2000) Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells. J Immunol 164:129-135
    • (2000) J Immunol , vol.164 , pp. 129-135
    • Dong, X.1    An, B.2    Salvucci Kierstead, L.3    Storkus, W.J.4    Amoscato, A.A.5    Salter, R.D.6
  • 14
    • 0034647551 scopus 로고    scopus 로고
    • The human 26 S and 20 S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate
    • 10.1074/jbc.M000740200 10801794
    • Emmerich NP, Nussbaum AK, Stevanovic S, Priemer M, Toes RE, Rammensee HG, Schild H (2000) The human 26 S and 20 S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate. J Biol Chem 275:21140-21148. doi: 10.1074/jbc.M000740200
    • (2000) J Biol Chem , vol.275 , pp. 21140-21148
    • Emmerich, N.P.1    Nussbaum, A.K.2    Stevanovic, S.3    Priemer, M.4    Toes, R.E.5    Rammensee, H.G.6    Schild, H.7
  • 15
    • 77954757238 scopus 로고    scopus 로고
    • Impact of system L amino acid transporter 1 (LAT1) on proliferation of human ovarian cancer cells: A possible target for combination therapy with anti-proliferative aminopeptidase inhibitors
    • 10.1016/j.bcp.2010.05.021 20510678
    • Fan X, Ross DD, Arakawa H, Ganapathy V, Tamai I, Nakanishi T (2010) Impact of system L amino acid transporter 1 (LAT1) on proliferation of human ovarian cancer cells: a possible target for combination therapy with anti-proliferative aminopeptidase inhibitors. Biochem Pharmacol 80:811-818. doi: 10.1016/j.bcp.2010.05.021
    • (2010) Biochem Pharmacol , vol.80 , pp. 811-818
    • Fan, X.1    Ross, D.D.2    Arakawa, H.3    Ganapathy, V.4    Tamai, I.5    Nakanishi, T.6
  • 16
    • 84865501560 scopus 로고    scopus 로고
    • A novel aminopeptidase N inhibitor developed by virtual screening approach
    • 10.1016/j.bmcl.2012.07.086 22901392
    • Feng J, Jin K, Zhu H, Zhang X, Zhang L, Liu J, Xu W (2012) A novel aminopeptidase N inhibitor developed by virtual screening approach. Bioorg Med Chem Lett 22:5863-5869. doi: 10.1016/j.bmcl.2012.07.086
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 5863-5869
    • Feng, J.1    Jin, K.2    Zhu, H.3    Zhang, X.4    Zhang, L.5    Liu, J.6    Xu, W.7
  • 17
    • 0028702667 scopus 로고
    • Suicide inactivation of leukotriene A4 hydrolase/aminopeptidase
    • 7825854
    • Fitzpatrick F, Lepley R, Orning L, Duffin K (1994) Suicide inactivation of leukotriene A4 hydrolase/aminopeptidase. Ann N Y Acad Sci 744:31-38
    • (1994) Ann N y Acad Sci , vol.744 , pp. 31-38
    • Fitzpatrick, F.1    Lepley, R.2    Orning, L.3    Duffin, K.4
  • 18
    • 33645754224 scopus 로고    scopus 로고
    • Expression of endoplasmic reticulum aminopeptidases in EBV-B cell lines from healthy donors and leukemia/lymphoma, carcinoma, and melanoma cell lines
    • 16585582
    • Fruci D, Ferracuti S (2006) Expression of endoplasmic reticulum aminopeptidases in EBV-B cell lines from healthy donors and leukemia/lymphoma, carcinoma, and melanoma cell lines. J Immunol 176:4869-4879
    • (2006) J Immunol , vol.176 , pp. 4869-4879
    • Fruci, D.1    Ferracuti, S.2
  • 19
    • 48749106928 scopus 로고    scopus 로고
    • Altered expression of endoplasmic reticulum aminopeptidases ERAP1 and ERAP2 in transformed non-lymphoid human tissues
    • 10.1002/jcp.21454 18393273
    • Fruci D, Giacomini P, Nicotra MR, Forloni M, Fraioli R, Saveanu L, Van Endert P, Natali PG (2008) Altered expression of endoplasmic reticulum aminopeptidases ERAP1 and ERAP2 in transformed non-lymphoid human tissues. J Cell Physiol 216:742-749. doi: 10.1002/jcp.21454
    • (2008) J Cell Physiol , vol.216 , pp. 742-749
    • Fruci, D.1    Giacomini, P.2    Nicotra, M.R.3    Forloni, M.4    Fraioli, R.5    Saveanu, L.6    Van Endert, P.7    Natali, P.G.8
  • 20
    • 79959698334 scopus 로고    scopus 로고
    • LYP, a novel bestatin derivative, inhibits cell growth and suppresses APN/CD13 activity in human ovarian carcinoma cells more potently than bestatin
    • 10.1007/s10637-010-9391-9 20111888
    • Gao J-J, Gao Z-H, Zhao C-R, Yuan Y, Cui S-X, Zhang X-F, Cheng Y-N, Xu W-F, Tang W, Qu X-J (2011) LYP, a novel bestatin derivative, inhibits cell growth and suppresses APN/CD13 activity in human ovarian carcinoma cells more potently than bestatin. Invest New Drugs 29:574-582. doi: 10.1007/s10637-010- 9391-9
    • (2011) Invest New Drugs , vol.29 , pp. 574-582
    • Gao, J.-J.1    Gao, Z.-H.2    Zhao, C.-R.3    Yuan, Y.4    Cui, S.-X.5    Zhang, X.-F.6    Cheng, Y.-N.7    Xu, W.-F.8    Tang, W.9    Qu, X.-J.10
  • 21
    • 0027994297 scopus 로고
    • Serum leucine aminopeptidase in head and neck cancer
    • 7930914
    • Garg LN, Yadav SP, Lal H (1994) Serum leucine aminopeptidase in head and neck cancer. J Laryngol Otol 108:660-662
    • (1994) J Laryngol Otol , vol.108 , pp. 660-662
    • Garg, L.N.1    Yadav, S.P.2    Lal, H.3
  • 22
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • 10.1152/physrev.00027.2001 11917093
    • Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82:373-428. doi: 10.1152/physrev.00027.2001
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 23
    • 79952774855 scopus 로고    scopus 로고
    • Intracellular amino acid sensing and mTORC1-regulated growth: New ways to block an old target?
    • 3044466 21154118
    • Goberdhan D (2010) Intracellular amino acid sensing and mTORC1-regulated growth: new ways to block an old target? Curr Opin Investig Drugs 11:1360-1367
    • (2010) Curr Opin Investig Drugs , vol.11 , pp. 1360-1367
    • Goberdhan, D.1
  • 24
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • 10.1038/nature02263 14685250
    • Goldberg AL (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426:895-899. doi: 10.1038/nature02263
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 25
    • 0036364467 scopus 로고    scopus 로고
    • Multidrug resistance in cancer: Role of ATP-dependent transporters
    • 10.1038/nrc706 11902585
    • Gottesman MM, Fojo T, Bates SE (2002) Multidrug resistance in cancer: role of ATP-dependent transporters. Nat Rev Cancer 2:48-58. doi: 10.1038/nrc706
    • (2002) Nat Rev Cancer , vol.2 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 26
    • 0030248766 scopus 로고    scopus 로고
    • Peptide antigen production by the proteasome: Complexity provides efficiency
    • 8854562
    • Groettrup M, Soza A, Kuckelkorn U, Kloetzel P (1996) Peptide antigen production by the proteasome: complexity provides efficiency. Immunol Today 17:429-435
    • (1996) Immunol Today , vol.17 , pp. 429-435
    • Groettrup, M.1    Soza, A.2    Kuckelkorn, U.3    Kloetzel, P.4
  • 27
    • 0037190118 scopus 로고    scopus 로고
    • Aminopeptidase inhibitors bestatin and actinonin inhibit cell proliferation of myeloma cells predominantly by intracellular interactions
    • 12048155
    • Grujić M, Renko M (2002) Aminopeptidase inhibitors bestatin and actinonin inhibit cell proliferation of myeloma cells predominantly by intracellular interactions. Cancer Lett 182:113-119
    • (2002) Cancer Lett , vol.182 , pp. 113-119
    • Grujić, M.1    Renko, M.2
  • 28
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • 10.1016/j.ccr.2007.05.008 17613433
    • Guertin DA, Sabatini DM (2007) Defining the role of mTOR in cancer. Cancer Cell 12:9-22. doi: 10.1016/j.ccr.2007.05.008
    • (2007) Cancer Cell , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 29
    • 10944253095 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis
    • 10.1074/jbc.R400027200 15339917
    • Haeggström JZ (2004) Leukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis. J Biol Chem 279:50639-50642. doi: 10.1074/jbc.R400027200
    • (2004) J Biol Chem , vol.279 , pp. 50639-50642
    • Haeggström, J.Z.1
  • 30
    • 2142812860 scopus 로고    scopus 로고
    • Functional properties and molecular architecture of leukotriene A4 hydrolase, a pivotal catalyst of chemotactic leukotriene formation
    • 10.1100/tsw.2002.810
    • Haeggström JZ, Nordlund P, Thunnissen MMGM (2002) Functional properties and molecular architecture of leukotriene A4 hydrolase, a pivotal catalyst of chemotactic leukotriene formation. Sci World J 2:1734-1749. doi: 10.1100/tsw.2002.810
    • (2002) Sci World J , vol.2 , pp. 1734-1749
    • Haeggström, J.Z.1    Nordlund, P.2    Thunnissen, M.3
  • 31
    • 84898880103 scopus 로고    scopus 로고
    • Adipocyte-derived leucine aminopeptidase genotype and response to antihypertensive therapy
    • Hallberg L, Michaëlsson K (2003) Adipocyte-derived leucine aminopeptidase genotype and response to antihypertensive therapy. BMC cardiovasc Disord 6:7-12
    • (2003) BMC Cardiovasc Disord , vol.6 , pp. 7-12
    • Hallberg, L.1    Michaëlsson, K.2
  • 32
    • 0036161112 scopus 로고    scopus 로고
    • Aminopeptidase N is involved in cell motility and angiogenesis: Its clinical significance in human colon cancer
    • 10.1053/gast.2002.31095 11832452
    • Hashida H, Takabayashi A, Kanai M, Adachi M, Kondo K, Kohno N, Yamaoka Y, Miyake M (2002) Aminopeptidase N is involved in cell motility and angiogenesis: its clinical significance in human colon cancer. Gastroenterology 122:376-386. doi: 10.1053/gast.2002.31095
    • (2002) Gastroenterology , vol.122 , pp. 376-386
    • Hashida, H.1    Takabayashi, A.2    Kanai, M.3    Adachi, M.4    Kondo, K.5    Kohno, N.6    Yamaoka, Y.7    Miyake, M.8
  • 33
    • 14044255662 scopus 로고    scopus 로고
    • Processing of antigenic peptides by aminopeptidases
    • 15187416
    • Hattori A, Tsujimoto M (2004) Processing of antigenic peptides by aminopeptidases. Biol Pharm Bull 27:777-780
    • (2004) Biol Pharm Bull , vol.27 , pp. 777-780
    • Hattori, A.1    Tsujimoto, M.2
  • 34
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • 10.1101/gad.1212704 15314020
    • Hay N, Sonenberg N (2004) Upstream and downstream of mTOR. Genes Dev 18:1926-1945. doi: 10.1101/gad.1212704
    • (2004) Genes Dev , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 35
    • 23944471680 scopus 로고    scopus 로고
    • The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle
    • 10.1038/sj.cdd.4401702 16094395
    • Hershko A (2005) The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle. Cell Death Differ 12:1191-1197. doi: 10.1038/sj.cdd.4401702
    • (2005) Cell Death Differ , vol.12 , pp. 1191-1197
    • Hershko, A.1
  • 36
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • 10.1146/annurev.bi.61.070192.003553 1323239
    • Hershko A, Ciechanover A (1992) The ubiquitin system for protein degradation. Annu Rev Biochem 61:761-807. doi: 10.1146/annurev.bi.61.070192. 003553
    • (1992) Annu Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 37
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • 10.1146/annurev.biochem.67.1.425 9759494
    • Hershko A, Ciechanover A (1998) The ubiquitin system. Annu Rev Biochem 67:425-479. doi: 10.1146/annurev.biochem.67.1.425
    • (1998) Annu Rev Biochem , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 38
    • 56149108905 scopus 로고    scopus 로고
    • The role of LTA4H and ALOX5AP polymorphism in asthma and allergy susceptibility
    • 10.1111/j.1398-9995.2008.01667.x 18547289
    • Holloway JW, Barton SJ, Holgate ST, Rose-Zerilli MJ, Sayers I (2008) The role of LTA4H and ALOX5AP polymorphism in asthma and allergy susceptibility. Allergy 63:1046-1053. doi: 10.1111/j.1398-9995.2008.01667.x
    • (2008) Allergy , vol.63 , pp. 1046-1053
    • Holloway, J.W.1    Barton, S.J.2    Holgate, S.T.3    Rose-Zerilli, M.J.4    Sayers, I.5
  • 39
    • 34548488989 scopus 로고    scopus 로고
    • Brain-specific aminopeptidase: From enkephalinase to protector against neurodegeneration
    • 10.1007/s11064-007-9356-3 17476590
    • Hui K-S (2007) Brain-specific aminopeptidase: from enkephalinase to protector against neurodegeneration. Neurochem Res 32:2062-2071. doi: 10.1007/s11064-007-9356-3
    • (2007) Neurochem Res , vol.32 , pp. 2062-2071
    • Hui, K.-S.1
  • 40
    • 0038364080 scopus 로고    scopus 로고
    • Randomized double-blind placebo-controlled trial of bestatin in patients with resected stage i squamous-cell lung carcinoma
    • 12697853
    • Ichinose Y, Genka K, Koike T, Kato H, Watanabe Y, Mori T, Iioka S, Sakuma A, Ohta M (2003) Randomized double-blind placebo-controlled trial of bestatin in patients with resected stage 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    Genka, K.2    Koike, T.3    Kato, H.4    Watanabe, Y.5    Mori, T.6    Iioka, S.7    Sakuma, A.8    Ohta, M.9
  • 41
    • 0032753156 scopus 로고    scopus 로고
    • Serum leucine aminopeptidase as an activity indicator in systemic lupus erythematosus: A study of 46 consecutive cases
    • 10501415
    • Inokuma S, Setoguchi K, Ohta T, Matsuzaki Y, Yoshida A (1999) Serum leucine aminopeptidase as an activity indicator in systemic lupus erythematosus: a study of 46 consecutive cases. Rheumatology 38:705-708
    • (1999) Rheumatology , vol.38 , pp. 705-708
    • Inokuma, S.1    Setoguchi, K.2    Ohta, T.3    Matsuzaki, Y.4    Yoshida, A.5
  • 44
    • 2642559772 scopus 로고    scopus 로고
    • Specific nonpeptide inhibitors of puromycin-sensitive aminopeptidase with a 2,4(1H,3H)-quinazolinedione skeleton
    • 14600372
    • Kakuta H, Tanatani A, Nagasawa K, Hashimoto Y (2003) Specific nonpeptide inhibitors of puromycin-sensitive aminopeptidase with a 2,4(1H,3H)- quinazolinedione skeleton. Chem Pharm Bull 51:1273-1282
    • (2003) Chem Pharm Bull , vol.51 , pp. 1273-1282
    • Kakuta, H.1    Tanatani, A.2    Nagasawa, K.3    Hashimoto, Y.4
  • 46
    • 0347626098 scopus 로고    scopus 로고
    • Biological significance of aminopeptidase N/CD13 in thyroid carcinomas
    • 14679016
    • Kehlen A, Lendeckel U, Dralle H (2003) Biological significance of aminopeptidase N/CD13 in thyroid carcinomas. Cancer Res 63:8500-8506
    • (2003) Cancer Res , vol.63 , pp. 8500-8506
    • Kehlen, A.1    Lendeckel, U.2    Dralle, H.3
  • 47
    • 73349135008 scopus 로고    scopus 로고
    • Cytosolic aminopeptidases influence MHC class I-mediated antigen presentation in an allele-dependent manner
    • 10.4049/jimmunol.0901489 19917696
    • Kim E, Kwak H, Ahn K (2009) Cytosolic aminopeptidases influence MHC class I-mediated antigen presentation in an allele-dependent manner. J Immunol 183:7379-7387. doi: 10.4049/jimmunol.0901489
    • (2009) J Immunol , vol.183 , pp. 7379-7387
    • Kim, E.1    Kwak, H.2    Ahn, K.3
  • 48
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • 9442034
    • Kisselev A, Akopian T, Goldberg A (1998) Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J Biol Chem 273:1982-1989
    • (1998) J Biol Chem , vol.273 , pp. 1982-1989
    • Kisselev, A.1    Akopian, T.2    Goldberg, A.3
  • 49
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes
    • 9920878
    • Kisselev A, Akopian T, Woo K, AL G (1999) The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. J Biol Chem 274:3363-3371
    • (1999) J Biol Chem , vol.274 , pp. 3363-3371
    • Kisselev, A.1    Akopian, T.2    Woo, K.3    Al, G.4
  • 51
    • 70350418625 scopus 로고    scopus 로고
    • MTOR signaling at a glance
    • 10.1242/jcs.051011 2758797 19812304
    • Laplante M, Sabatini DM (2009) mTOR signaling at a glance. J Cell Sci 122:3589-3594. doi: 10.1242/jcs.051011
    • (2009) J Cell Sci , vol.122 , pp. 3589-3594
    • Laplante, M.1    Sabatini, D.M.2
  • 52
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • 10.1016/j.cell.2012.03.017 3331679 22500797
    • Laplante M, Sabatini DM (2012) mTOR signaling in growth control and disease. Cell 149:274-293. doi: 10.1016/j.cell.2012.03.017
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 53
    • 0030036617 scopus 로고    scopus 로고
    • T cell responses affected by aminopeptidase N (CD13)-mediated trimming of major histocompatibility complex class II-bound peptides
    • 8691132
    • Larsen SL, Pedersen LO, Buus S, Stryhn A (1996) T cell responses affected by aminopeptidase N (CD13)-mediated trimming of major histocompatibility complex class II-bound peptides. J Exp Med 184:183-189
    • (1996) J Exp Med , vol.184 , pp. 183-189
    • Larsen, S.L.1    Pedersen, L.O.2    Buus, S.3    Stryhn, A.4
  • 54
    • 33745816760 scopus 로고    scopus 로고
    • Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
    • 10.1681/ASN.2006010083 16738015
    • Lecker SH, Goldberg AL, Mitch WE (2006) Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. J Am Soc Nephrol 17:1807-1819. doi: 10.1681/ASN.2006010083
    • (2006) J Am Soc Nephrol , vol.17 , pp. 1807-1819
    • Lecker, S.H.1    Goldberg, A.L.2    Mitch, W.E.3
  • 55
    • 67649432959 scopus 로고    scopus 로고
    • Cobalt chloride-induced downregulation of puromycin-sensitive aminopeptidase suppresses the migration and invasion of PC-3 Cells
    • 10.4014/jmb.0807.438 19494703
    • Lee S (2009) Cobalt chloride-induced downregulation of puromycin-sensitive aminopeptidase suppresses the migration and invasion of PC-3 Cells. J Microbiol Biotechnol 19:530-536. doi: 10.4014/jmb.0807.438
    • (2009) J Microbiol Biotechnol , vol.19 , pp. 530-536
    • Lee, S.1
  • 56
    • 0037316065 scopus 로고    scopus 로고
    • Acute leukemia with myeloid, B-, and natural killer cell differentiation
    • Lee P, Lin C, Liu C (2003) Acute leukemia with myeloid, B-, and natural killer cell differentiation. Arch Pathol Lab Med 127:93-95
    • (2003) Arch Pathol Lab Med , vol.127 , pp. 93-95
    • Lee, P.1    Lin, C.2    Liu, C.3
  • 59
    • 0036882401 scopus 로고    scopus 로고
    • Metalloaminopeptidases: Common functional themes in disparate structural surroundings
    • 12475202
    • Lowther WT, Matthews BW (2002) Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chem Rev 102:4581-4608
    • (2002) Chem Rev , vol.102 , pp. 4581-4608
    • Lowther, W.T.1    Matthews, B.W.2
  • 63
    • 65349123542 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms in antigen processing machinery component ERAP1 significantly associate with clinical outcome in cervical carcinoma
    • 10.1002/gcc 19202550
    • Mehta A, Jordanova E, Corver W, Van Wezel T, Uh H, Kenter G, Fleuren GJ (2009) Single nucleotide polymorphisms in antigen processing machinery component ERAP1 significantly associate with clinical outcome in cervical carcinoma. Genes Chromosom Cancer 48:410-418. doi: 10.1002/gcc
    • (2009) Genes Chromosom Cancer , vol.48 , pp. 410-418
    • Mehta, A.1    Jordanova, E.2    Corver, W.3    Van Wezel, T.4    Uh, H.5    Kenter, G.6    Fleuren, G.J.7
  • 64
    • 0027461740 scopus 로고
    • Biochemical and functional characterization of aminopeptidase N expressed by human melanoma cells
    • 8095183
    • Menrad A, Speicher D, Wacker J, Herlyn M (1993) Biochemical and functional characterization of aminopeptidase N expressed by human melanoma cells. Cancer Res 53:1450-1455
    • (1993) Cancer Res , vol.53 , pp. 1450-1455
    • Menrad, A.1    Speicher, D.2    Wacker, J.3    Herlyn, M.4
  • 65
    • 48149111676 scopus 로고    scopus 로고
    • The moonlighting enzyme CD13: Old and new functions to target
    • 10.1016/j.molmed.2008.06.003 18603472
    • Mina-Osorio P (2008) The moonlighting enzyme CD13: old and new functions to target. Trends Mol Med 14:361-371. doi: 10.1016/j.molmed.2008.06.003
    • (2008) Trends Mol Med , vol.14 , pp. 361-371
    • Mina-Osorio, P.1
  • 68
    • 78649927272 scopus 로고    scopus 로고
    • Resveratrol, a red wine polyphenol, suppresses pancreatic cancer by inhibiting leukotriene ahydrolase
    • 10.1158/0008-5472.CAN-10-2858 20952510
    • Oi N, Jeong C-H, Nadas J, Cho Y-Y, Pugliese A, Bode AM, Dong Z (2010) Resveratrol, a red wine polyphenol, suppresses pancreatic cancer by inhibiting leukotriene ahydrolase. Cancer Res 70:9755-9764. doi: 10.1158/0008-5472.CAN-10- 2858
    • (2010) Cancer Res , vol.70 , pp. 9755-9764
    • Oi, N.1    Jeong, C.-H.2    Nadas, J.3    Cho, Y.-Y.4    Pugliese, A.5    Bode, A.M.6    Dong, Z.7
  • 69
    • 0033950895 scopus 로고    scopus 로고
    • Aminopeptidase N Is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis
    • 10676659
    • Pasqualini R, Koivunen E, Kain R (2000) Aminopeptidase N Is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis. Cancer Res 60:722-727
    • (2000) Cancer Res , vol.60 , pp. 722-727
    • Pasqualini, R.1    Koivunen, E.2    Kain, R.3
  • 70
    • 84859788826 scopus 로고    scopus 로고
    • CIP-13F, a novel aminopeptidase N (APN/CD13) inhibitor, inhibits Lewis lung carcinoma growth and metastasis in mice
    • 10.1007/s00280-011-1799-1 22186885
    • Pei K-L, Yuan Y, Qin S-H, Wang Y, Zhou L, Zhang H-L, Qu X-J, Cui S-X (2012) CIP-13F, a novel aminopeptidase N (APN/CD13) inhibitor, inhibits Lewis lung carcinoma growth and metastasis in mice. Cancer Chemother Pharmacol 69:1029-1038. doi: 10.1007/s00280-011-1799-1
    • (2012) Cancer Chemother Pharmacol , vol.69 , pp. 1029-1038
    • Pei, K.-L.1    Yuan, Y.2    Qin, S.-H.3    Wang, Y.4    Zhou, L.5    Zhang, H.-L.6    Qu, X.-J.7    Cui, S.-X.8
  • 71
    • 70349331392 scopus 로고    scopus 로고
    • Increased APN/CD13 and acid aminopeptidase activities in head and neck squamous cell carcinoma
    • 10.1002/h
    • Pérez I, Varona A, Blanco L, Gil J (2009) Increased APN/CD13 and acid aminopeptidase activities in head and neck squamous cell carcinoma. Head Neck 10:1335-1340. doi: 10.1002/h
    • (2009) Head Neck , vol.10 , pp. 1335-1340
    • Pérez, I.1    Varona, A.2    Blanco, L.3    Gil, J.4
  • 72
    • 0000828960 scopus 로고    scopus 로고
    • Antimetabolites
    • R.L. Souhami I. Tannock Hohenberger J.C. Horiot (eds) 2 Oxford University Press Oxford
    • Peters GJ, Jansen G (2001) Antimetabolites. In: Souhami RL, Tannock I, Hohenberger P, Horiot JC (eds) Oxford textbook of oncology, vol 1, chapter 4.16, 2nd edn. Oxford University Press, Oxford, pp 663-713
    • (2001) Oxford Textbook of Oncology, Vol 1, Chapter 4.16 , pp. 663-713
    • Peters, G.J.1    Jansen, G.2
  • 73
    • 80051679604 scopus 로고    scopus 로고
    • Aminopeptidase-N/CD13 is a potential proapoptotic target in human myeloid tumor cells
    • 10.1096/fj.11-181396 21566207
    • Piedfer M, Dauzonne D, Tang R, N'Guyen J, Billard C, Bauvois B (2011) Aminopeptidase-N/CD13 is a potential proapoptotic target in human myeloid tumor cells. FASEB J 25:2831-2842. doi: 10.1096/fj.11-181396
    • (2011) FASEB J , vol.25 , pp. 2831-2842
    • Piedfer, M.1    Dauzonne, D.2    Tang, R.3    N'Guyen, J.4    Billard, C.5    Bauvois, B.6
  • 74
    • 0031465286 scopus 로고    scopus 로고
    • Bestatin-mediated inhibition of leucine aminopeptidase may hinder HIV infection
    • 9477117
    • Pulido-Cejudo G, Conway B, Proulx P, Brown R, Izaguirre C (1997) Bestatin-mediated inhibition of leucine aminopeptidase may hinder HIV infection. Antiviral Res 36:167-177
    • (1997) Antiviral Res , vol.36 , pp. 167-177
    • Pulido-Cejudo, G.1    Conway, B.2    Proulx, P.3    Brown, R.4    Izaguirre, C.5
  • 76
    • 0021770929 scopus 로고
    • Leukotriene A4 hydrolase in human leukocytes. Purification and properties
    • 6490615
    • Radmark O, Shimizus T, Jornvall H, Samuelsson B (1984) Leukotriene A4 hydrolase in human leukocytes. Purification and properties. J Biol Chem 259:12339-12345
    • (1984) J Biol Chem , vol.259 , pp. 12339-12345
    • Radmark, O.1    Shimizus, T.2    Jornvall, H.3    Samuelsson, B.4
  • 77
    • 79960565694 scopus 로고    scopus 로고
    • A new aminopeptidase inhibitor from streptomyces strain HCCB10043 found by UPLC-MS
    • 10.1007/s00216-011-5093-1 21626195
    • Rao M, Li Q, Feng L, Xia X, Ruan L, Sheng X, Ge M (2011) A new aminopeptidase inhibitor from streptomyces strain HCCB10043 found by UPLC-MS. Anal Bioanal Chem 401:699-706. doi: 10.1007/s00216-011-5093-1
    • (2011) Anal Bioanal Chem , vol.401 , pp. 699-706
    • Rao, M.1    Li, Q.2    Feng, L.3    Xia, X.4    Ruan, L.5    Sheng, X.6    Ge, M.7
  • 78
    • 68049128092 scopus 로고    scopus 로고
    • A first-in-man phase i and pharmacokinetic study on CHR-2797 (Tosedostat), an inhibitor of M1 aminopeptidases, in patients with advanced solid tumors
    • 10.1158/1078-0432.CCR-09-0306 19638462
    • Reid AHM, Protheroe A, Attard G, Hayward N, Vidal L, Spicer J, Shaw HM, Bone EA, Carter J, Hooftman L, Harris A, De Bono JS (2009) A first-in-man phase I and pharmacokinetic study on CHR-2797 (Tosedostat), an inhibitor of M1 aminopeptidases, in patients with advanced solid tumors. Clin Cancer Res 15:4978-4985. doi: 10.1158/1078-0432.CCR-09-0306
    • (2009) Clin Cancer Res , vol.15 , pp. 4978-4985
    • Reid, A.H.M.1    Protheroe, A.2    Attard, G.3    Hayward, N.4    Vidal, L.5    Spicer, J.6    Shaw, H.M.7    Bone, E.A.8    Carter, J.9    Hooftman, L.10    Harris, A.11    De Bono, J.S.12
  • 80
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • 10.1146/annurev.immunol.17.1.739 10358773
    • Rock K, Goldberg A (1999) Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu Rev Immunol 17:739-779. doi: 10.1146/annurev.immunol.17.1.739
    • (1999) Annu Rev Immunol , vol.17 , pp. 739-779
    • Rock, K.1    Goldberg, A.2
  • 81
    • 3242807547 scopus 로고    scopus 로고
    • Post-proteasomal antigen processing for major histocompatibility complex class i presentation
    • 10.1038/ni1089 15224092
    • Rock K, York I, Goldberg A (2004) Post-proteasomal antigen processing for major histocompatibility complex class I presentation. Nat Immunol 5:670-677. doi: 10.1038/ni1089
    • (2004) Nat Immunol , vol.5 , pp. 670-677
    • Rock, K.1    York, I.2    Goldberg, A.3
  • 82
    • 2342613168 scopus 로고
    • Leucine aminopeptidase activity; Observations in patients with cancer of the pancreas and other diseases
    • 13578084
    • Rutenburg A, Goldbarg J, Pineda E (1958) Leucine aminopeptidase activity; observations in patients with cancer of the pancreas and other diseases. N Engl J Med 259:469-472
    • (1958) N Engl J Med , vol.259 , pp. 469-472
    • Rutenburg, A.1    Goldbarg, J.2    Pineda, E.3
  • 83
    • 45849105156 scopus 로고    scopus 로고
    • The rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • 10.1126/science.1157535 2475333 18497260
    • Sancak Y, Peterson TR, Shaul YD, Lindquist RA, Thoreen CC, Bar-Peled L, Sabatini DM (2008) The rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 320(5882):1496-1501. doi: 10.1126/science.1157535
    • (2008) Science , vol.320 , Issue.5882 , pp. 1496-1501
    • Sancak, Y.1    Peterson, T.R.2    Shaul, Y.D.3    Lindquist, R.A.4    Thoreen, C.C.5    Bar-Peled, L.6    Sabatini, D.M.7
  • 85
    • 0034630350 scopus 로고    scopus 로고
    • Aminopeptidase N/CD13 is directly linked to signal transduction pathways in monocytes
    • 10.1006/cimm.2000.1629 10805970
    • Santos A, Langner J, Herrmann M, Riemann D (2000) Aminopeptidase N/CD13 is directly linked to signal transduction pathways in monocytes. Cell Immunol 201:22-32. doi: 10.1006/cimm.2000.1629
    • (2000) Cell Immunol , vol.201 , pp. 22-32
    • Santos, A.1    Langner, J.2    Herrmann, M.3    Riemann, D.4
  • 86
    • 0036902105 scopus 로고    scopus 로고
    • An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides
    • 10.1038/ni859 12436109
    • Saric T, Chang S-C, Hattori A, York IA, Markant S, Rock KL, Tsujimoto M, Goldberg AL (2002) An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat Immunol 3:1169-1176. doi: 10.1038/ni859
    • (2002) Nat Immunol , vol.3 , pp. 1169-1176
    • Saric, T.1    Chang, S.-C.2    Hattori, A.3    York, I.A.4    Markant, S.5    Rock, K.L.6    Tsujimoto, M.7    Goldberg, A.L.8
  • 87
    • 8744237281 scopus 로고    scopus 로고
    • Pathway for degradation of peptides generated by proteasomes: A key role for thimet oligopeptidase and other metallopeptidases
    • 10.1074/jbc.M406537200 15328361
    • Saric T, Graef CI, Goldberg AL (2004) Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases. J Biol Chem 279:46723-46732. doi: 10.1074/jbc.M406537200
    • (2004) J Biol Chem , vol.279 , pp. 46723-46732
    • Saric, T.1    Graef, C.I.2    Goldberg, A.L.3
  • 88
    • 16644386079 scopus 로고    scopus 로고
    • Role of aminopeptidase in angiogenesis
    • 15187415
    • Sato Y (2004) Role of aminopeptidase in angiogenesis. Biol Pharm Bull 27:772-776
    • (2004) Biol Pharm Bull , vol.27 , pp. 772-776
    • Sato, Y.1
  • 90
    • 0242635646 scopus 로고    scopus 로고
    • Aminopeptidase inhibitors inhibit proliferation and induce apoptosis of K562 and STI571-resistant K562 cell lines through the MAPK and GSK-3beta pathways
    • 10.1080/1042819031000122033 14738154
    • Sawafuji K, Miyakawa Y, Weisberg E, Griffin JD, Ikeda Y, Kizaki M (2003) Aminopeptidase inhibitors inhibit proliferation and induce apoptosis of K562 and STI571-resistant K562 cell lines through the MAPK and GSK-3beta pathways. Leuk Lymphoma 44:1987-1996. doi: 10.1080/1042819031000122033
    • (2003) Leuk Lymphoma , vol.44 , pp. 1987-1996
    • Sawafuji, K.1    Miyakawa, Y.2    Weisberg, E.3    Griffin, J.D.4    Ikeda, Y.5    Kizaki, M.6
  • 91
    • 0035041649 scopus 로고    scopus 로고
    • Bestatin as an experimental tool in mammals
    • 11465152
    • Scornik O, Botbol V (2001) Bestatin as an experimental tool in mammals. Curr Drug Metab 2:67-85
    • (2001) Curr Drug Metab , vol.2 , pp. 67-85
    • Scornik, O.1    Botbol, V.2
  • 92
    • 0033822017 scopus 로고    scopus 로고
    • Single amino acid (arginine) deprivation: Rapid and selective death of cultured transformed and malignant cells
    • 10.1054/bjoc.2000.1353 2363527 10952786
    • Scott L, Lamb J, Smith S, Wheatley DN (2000) Single amino acid (arginine) deprivation: rapid and selective death of cultured transformed and malignant cells. Br J Cancer 83:800-810. doi: 10.1054/bjoc.2000.1353
    • (2000) Br J Cancer , vol.83 , pp. 800-810
    • Scott, L.1    Lamb, J.2    Smith, S.3    Wheatley, D.N.4
  • 94
    • 0037015624 scopus 로고    scopus 로고
    • ERAAP customizes peptides for MHC class i molecules in the endoplasmic reticulum
    • 10.1038/nature01074 12368856
    • Serwold T, Gonzalez F, Kim J, Jacob R, Shastri N (2002) ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 419:480-483. doi: 10.1038/nature01074
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 96
    • 84871256917 scopus 로고    scopus 로고
    • Development of synthetic aminopeptidase N/CD13 inhibitors to overcome cancer metastasis and angiogenesis
    • 10.1021/ml3000758
    • Su L, Cao J, Jia Y, Zhang X, Fang H, Xu W (2012a) Development of synthetic aminopeptidase N/CD13 inhibitors to overcome cancer metastasis and angiogenesis. ACS Med Chem Lett 3:959-964. doi: 10.1021/ml3000758
    • (2012) ACS Med Chem Lett , vol.3 , pp. 959-964
    • Su, L.1    Cao, J.2    Jia, Y.3    Zhang, X.4    Fang, H.5    Xu, W.6
  • 97
    • 84861580001 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of novel amino acid ureido derivatives as aminopeptidase N/CD13 inhibitors
    • 10.1016/j.bmc.2012.04.035 22607877
    • Su L, Jia Y, Zhang L, Xu Y, Fang H, Xu W (2012b) Design, synthesis and biological evaluation of novel amino acid ureido derivatives as aminopeptidase N/CD13 inhibitors. Bioorg Med Chem 20:3807-3815. doi: 10.1016/j.bmc.2012.04.035
    • (2012) Bioorg Med Chem , vol.20 , pp. 3807-3815
    • Su, L.1    Jia, Y.2    Zhang, L.3    Xu, Y.4    Fang, H.5    Xu, W.6
  • 98
    • 0027479013 scopus 로고
    • Aminopeptidases: Structure and function
    • Taylor A (1993) Aminopeptidases: structure and function. FASEB J 32:290-298
    • (1993) FASEB J , vol.32 , pp. 290-298
    • Taylor, A.1
  • 99
    • 51849151991 scopus 로고    scopus 로고
    • Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: Implications for M1 aminopeptidases and inhibitor design
    • 10.1016/j.chembiol.2008.07.018 18804029
    • Tholander F, Muroya A, Roques B-P, Fournié-Zaluski M-C, Thunnissen MMGM, Haeggström JZ (2008) Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem Biol 15:920-929. doi: 10.1016/j.chembiol.2008.07.018
    • (2008) Chem Biol , vol.15 , pp. 920-929
    • Tholander, F.1    Muroya, A.2    Roques, B.-P.3    Fournié-Zaluski, M.-C.4    Thunnissen, M.5    Haeggström, J.Z.6
  • 100
    • 0035146853 scopus 로고    scopus 로고
    • Crystal structure of human leukotriene A 4 hydrolase, a bifunctional enzyme in inflammation
    • 11175901
    • Thunnissen M, Nordlund P, Haeggström JZ (2001) Crystal structure of human leukotriene A 4 hydrolase, a bifunctional enzyme in inflammation. Nat Struct Biol 8:131-135
    • (2001) Nat Struct Biol , vol.8 , pp. 131-135
    • Thunnissen, M.1    Nordlund, P.2    Haeggström, J.Z.3
  • 102
    • 33746080895 scopus 로고    scopus 로고
    • Clinical significance of aminopeptidase N in non-small cell lung cancer
    • 10.1158/1078-0432.CCR-06-0338 16818694
    • Tokuhara T, Hattori N, Ishida H, Hirai T, Higashiyama M, Kodama K, Miyake M (2006) Clinical significance of aminopeptidase N in non-small cell lung cancer. Clin Cancer Res 12:3971-3978. doi: 10.1158/1078-0432.CCR-06-0338
    • (2006) Clin Cancer Res , vol.12 , pp. 3971-3978
    • Tokuhara, T.1    Hattori, N.2    Ishida, H.3    Hirai, T.4    Higashiyama, M.5    Kodama, K.6    Miyake, M.7
  • 103
    • 40749125369 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase limits MHC class i presentation in dendritic cells but does not affect CD8 T cell responses during viral infections
    • 18209067
    • Towne C, York I, Neijssen J (2008) Puromycin-sensitive aminopeptidase limits MHC class I presentation in dendritic cells but does not affect CD8 T cell responses during viral infections. J Immunol 180:1704-1712
    • (2008) J Immunol , vol.180 , pp. 1704-1712
    • Towne, C.1    York, I.2    Neijssen, J.3
  • 104
    • 41949139764 scopus 로고    scopus 로고
    • Aminopeptidase N (APN)/CD13 inhibitor, Ubenimex, enhances radiation sensitivity in human cervical cancer
    • 10.1186/1471-2407-8-74 2289833 18366676
    • Tsukamoto H, Shibata K, Kajiyama H, Terauchi M, Nawa A, Kikkawa F (2008) Aminopeptidase N (APN)/CD13 inhibitor, Ubenimex, enhances radiation sensitivity in human cervical cancer. BMC Cancer 8:74. doi: 10.1186/1471-2407-8-74
    • (2008) BMC Cancer , vol.8 , pp. 74
    • Tsukamoto, H.1    Shibata, K.2    Kajiyama, H.3    Terauchi, M.4    Nawa, A.5    Kikkawa, F.6
  • 105
    • 0017236348 scopus 로고
    • Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes
    • Umezawa H, Aoyagi T, Suda H (1976) Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes. J Antibiot XXIX:97-99
    • (1976) J Antibiot , vol.29 , pp. 97-99
    • Umezawa, H.1    Aoyagi, T.2    Suda, H.3
  • 107
    • 77958562812 scopus 로고    scopus 로고
    • A phase Ib dose-escalation study to evaluate safety and tolerability of the addition of the aminopeptidase inhibitor tosedostat (CHR-2797) to paclitaxel in patients with advanced solid tumours
    • 10.1038/sj.bjc.6605917 2990605 20877350
    • van Herpen CM, Eskens FA, De Jonge M, Desar I, Hooftman L, Bone EA, Timmer-Bonte JN, Verweij J (2010) A phase Ib dose-escalation study to evaluate safety and tolerability of the addition of the aminopeptidase inhibitor tosedostat (CHR-2797) to paclitaxel in patients with advanced solid tumours. Br J Cancer 103:1362-1368. doi: 10.1038/sj.bjc.6605917
    • (2010) Br J Cancer , vol.103 , pp. 1362-1368
    • Van Herpen, C.M.1    Eskens, F.A.2    De Jonge, M.3    Desar, I.4    Hooftman, L.5    Bone, E.A.6    Timmer-Bonte, J.N.7    Verweij, J.8
  • 108
    • 33846864246 scopus 로고    scopus 로고
    • Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma
    • 10.1152/ajprenal.00148.2006 16985214
    • Varona A, Blanco L, López JI, Gil J, Agirregoitia E, Irazusta J, Larrinaga G (2007) Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma. Am J Physiol Renal Physiol 292:F780-F788. doi: 10.1152/ajprenal.00148.2006
    • (2007) Am J Physiol Renal Physiol , vol.292
    • Varona, A.1    Blanco, L.2    López, J.I.3    Gil, J.4    Agirregoitia, E.5    Irazusta, J.6    Larrinaga, G.7
  • 110
    • 0348019097 scopus 로고    scopus 로고
    • Adipocyte-derived leucine aminopeptidase suppresses angiogenesis in human endometrial carcinoma via renin-angiotensin system
    • 14695154
    • Watanabe Y, Shibata K, Kikkawa F (2003) Adipocyte-derived leucine aminopeptidase suppresses angiogenesis in human endometrial carcinoma via renin-angiotensin system. Clin Cancer Res 9:6497-6503
    • (2003) Clin Cancer Res , vol.9 , pp. 6497-6503
    • Watanabe, Y.1    Shibata, K.2    Kikkawa, F.3
  • 111
    • 79951698213 scopus 로고    scopus 로고
    • Aminopeptidase N (CD13) as a target for cancer chemotherapy
    • 10.1111/j.1349-7006.2010.01826.x 21205077
    • Wickström M, Larsson R, Nygren P, Gullbo J (2011) Aminopeptidase N (CD13) as a target for cancer chemotherapy. Cancer Sci 102:501-508. doi: 10.1111/j.1349-7006.2010.01826.x
    • (2011) Cancer Sci , vol.102 , pp. 501-508
    • Wickström, M.1    Larsson, R.2    Nygren, P.3    Gullbo, J.4
  • 112
    • 36949093286 scopus 로고
    • Aminopeptidase activity in cancer cells
    • 13622768
    • Willighagen R, Planteydt H (1959) Aminopeptidase activity in cancer cells. Nature 183:263-264
    • (1959) Nature , vol.183 , pp. 263-264
    • Willighagen, R.1    Planteydt, H.2
  • 114
    • 0342572532 scopus 로고    scopus 로고
    • Puromycin-sensitive alanyl aminopeptidase from human liver cytosol: Purification and characterization
    • 10978616
    • Yamamoto Y, Li YH, Ushiyama I, Nishimura A, Ohkubo I, Nishi K (2000) Puromycin-sensitive alanyl aminopeptidase from human liver cytosol: purification and characterization. Forensic Sci Int 113:143-146
    • (2000) Forensic Sci Int , vol.113 , pp. 143-146
    • Yamamoto, Y.1    Li, Y.H.2    Ushiyama, I.3    Nishimura, A.4    Ohkubo, I.5    Nishi, K.6
  • 115
    • 1842684993 scopus 로고    scopus 로고
    • Proteasomes get by with lots of help from their friends
    • 15084265
    • Yewdell J, Princiotta M (2004) Proteasomes get by with lots of help from their friends. Immunity 20:362-363
    • (2004) Immunity , vol.20 , pp. 362-363
    • Yewdell, J.1    Princiotta, M.2
  • 116
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • 10.1038/ni860 12436110
    • York IA, Chang S-C, Saric T, Keys JA, Favreau JM, Goldberg AL, Rock KL (2002) The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat Immunol 3:1177-1184. doi: 10.1038/ni860
    • (2002) Nat Immunol , vol.3 , pp. 1177-1184
    • York, I.A.1    Chang, S.-C.2    Saric, T.3    Keys, J.A.4    Favreau, J.M.5    Goldberg, A.L.6    Rock, K.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.