메뉴 건너뛰기




Volumn 8, Issue 5, 2013, Pages 537-568

Recent advances in proteasome inhibitor discovery

Author keywords

Cancer; Drug discovery; Inhibition; Modeling; Proteolysis; Rational design; Screening

Indexed keywords

2 3 [N (2 AMINO 6 BENZYLOXYCARBONYLAMINOHEXANOYL)HYDRAZINO] 4,4,4 TRIFLUORO BUTYRYLAMINO 3 PHENYLPROPIONIC ACID METHYL ESTER; 2 3 [N (6 AMINO 2 TERT BUTOXY CARBONYLAMINOHEXANOYL)HYDRAZINO] 4,4,4 TRIFLUOROBUTARYLAMINO 3 PHENYLPROPIONIC ACID METHYL ESTER CITRIC ACID SALT; 2 [3 (N 6 AMINO 2 (2 (3 PHENOXYPHENYL)ACETYLAMINO)HEXANOYLHYD)HYDRAZINO] 4,4,4 TRIFLUORO BUTYRYLAMINO 3 PHENYL PROPIONIC ACID METHYL ESTER TRIFLUORO ACETIC ACID SALT; 3 METHOXY 2 [3 METHOXY 2 [(2 METHYL 1,3 THIAZOL 5 YL)FORMAMIDO]PROPANAMIDO] N [1 [2 METHLYOXIRAN 2 YL] 1 OXO 3 PHENYLPROPAN 2 YL]PROPANAMIDE; 4 SALICYLIDENE 1,7 BIS(4 HYDROXY, 3 METHOXYPHENYL) 1,6 HEPTADIENE 3,5 DIONE; 5,6,3,4 TETRAHYDROXY 7 METHOXYFLAVONE; ALDEHYDE DERIVATIVE; ALLYL 1 [1 (1 (ETHYLSULFONYL) 5 METHYLHEX 1 EN 3 YLAMINO) 4 METHYL 1 OXOPENTAN 2 YL] 2 OXO 1,2 DIHYDROPYRIDIN 3 YLCARBAMATE; ALLYL 1 [1 (1 (ETHYLSULFONYL) 5 METHYLHEX 1 EN 3YLAMINO) 1 OXO 3 PHENYLPROPAN 2 YL] 2 OXO 1,2 DIHYDROPYRIDIN 3 YLCARBAMATE; BENZYL 1 [1 (1 (ETHYLSULFONYL) 5 METHYLHEX 1 EN 3 YLAMINO) 1 OXO 3 PHENYLPROPAN 2 YL] 2 OXO 1,2 DIHYDROPYRIDIN 3 YLCARBAMATE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CARFILZOMIB; FLAVONOID; GENISTEIN; GLIDOBACTIN A; GLIDOBACTIN DERIVATIVE; HYDROXYFLAVANONE; ISOLIQUIRITIGENIN; METAL COMPLEX; N [3 (1H TETRAZOL 5 YLTHIO) 4 HYDROXYNAPHTHALEN 1 YL] 4 (TRIFLUOROMETHYL)BIPHENYL 4 SULFONAMIDE; N1 [(DIETHYLAMINO)ETHYL] N4 [4METHYL 1 OXO 1 (1 OXO 3 PHENYLPROPAN 2 YLAMINO)PENTAN 2 YL]TEREPHTHALAMIDE; N1 [2 (DIPROPYLAMINO)ETHYL] N4 [4 METHYL 1 (4 METHYL 1 (4 METHYL 1 OXOPENTAN 2 YLAMINO) 1 OXOPENTAN 2 YL AMINO) 1 OXOPENTAN 2 YL] TEREPHTHALAMIDE,HYDROCHLORIDE SALT; NCI109268; PHENYLALANINE DERIVATIVE; PROTEASOME INHIBITOR; SYRINGOLIN A; TERREIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VINYL DERIVATIVE;

EID: 84876753857     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1517/17460441.2013.780020     Document Type: Review
Times cited : (14)

References (195)
  • 1
    • 0029353809 scopus 로고
    • The proteasome: A protein-degrading organelle?
    • Rubin DM, Finley D. The proteasome: a protein-degrading organelle? Curr Biol 1995;5:854-4
    • (1995) Curr Biol , vol.5 , pp. 854-854
    • Rubin, D.M.1    Finley, D.2
  • 2
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm review of a self-compartmentalizing protease
    • Baumeister W, Walz J, Proteolysis C. The proteasome: paradigm review of a self-compartmentalizing protease. Cell 1998;92:367-80
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Proteolysis, C.3
  • 3
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • Ciechanover A, Orian A, Schwartz AL. Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays 2000;22(5):442-51
    • (2000) Bioessays , vol.22 , Issue.5 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 4
  • 5
    • 0036713383 scopus 로고    scopus 로고
    • Proteasome subunit Rpn1 binds ubiquitin-like protein domains
    • Elsasser S, Gali RR, Schwickart M, et al. Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat Cell Biol 2002;4(9):725-30
    • (2002) Nat Cell Biol , vol.4 , Issue.9 , pp. 725-730
    • Elsasser, S.1    Gali, R.R.2    Schwickart, M.3
  • 6
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart CM, Cohen RE. Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 2004;5(3):177-87
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.3 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 7
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 A resolution
    • Groll M, Ditzel L, Lowe J, et al. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature (London) 1997;386(6624):463-71
    • (1997) Nature (London) , vol.386 , Issue.6624 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3
  • 8
    • 33947659939 scopus 로고    scopus 로고
    • 20S proteasome and its inhibitors: Crystallographic knowledge for drug development
    • Borissenko L, Groll M. 20S proteasome and its inhibitors: crystallographic knowledge for drug development. Chem Rev 2007;107(3):687-717
    • (2007) Chem Rev , vol.107 , Issue.3 , pp. 687-717
    • Borissenko, L.1    Groll, M.2
  • 9
    • 78649350792 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and assays to determine responses to inhibitors
    • Tsvetkov L, Nanjundan M, Domino M, Daniel KG. The ubiquitin-proteasome system and assays to determine responses to inhibitors. Expert Opin Drug Discov 2010;5(12):1221-36
    • (2010) Expert Opin Drug Discov , vol.5 , Issue.12 , pp. 1221-1236
    • Tsvetkov, L.1    Nanjundan, M.2    Domino, M.3    Daniel, K.G.4
  • 10
    • 84856373151 scopus 로고    scopus 로고
    • Proteasome Inhibitors: An expanding army attacking a unique target
    • Kisselev AF, van der Linden WA, Overkleeft HS. Proteasome inhibitors: an expanding army attacking a unique target. Chem Biol 2012;19(1):99-115
    • (2012) Chem Biol , vol.19 , Issue.1 , pp. 99-115
    • Kisselev, A.F.1    Van Der Linden, W.A.2    Overkleeft, H.S.3
  • 11
    • 1042278905 scopus 로고    scopus 로고
    • Proteasome and peptidase function in MHC-class-Imediated antigen presentation
    • Kloetzel PM, Ossendorp F. Proteasome and peptidase function in MHC-class-Imediated antigen presentation. Curr Opin Immunol 2004;16(1):76-81
    • (2004) Curr Opin Immunol , vol.16 , Issue.1 , pp. 76-81
    • Kloetzel, P.M.1    Ossendorp, F.2
  • 12
    • 44749085669 scopus 로고    scopus 로고
    • Thymoproteasome: Probable role in generating positively selecting peptides
    • Murata S, Takahama Y, Tanaka K. Thymoproteasome: probable role in generating positively selecting peptides. Curr Opin Immunol 2008;20(2):192-6
    • (2008) Curr Opin Immunol , vol.20 , Issue.2 , pp. 192-196
    • Murata, S.1    Takahama, Y.2    Tanaka, K.3
  • 13
  • 14
    • 0033920566 scopus 로고    scopus 로고
    • An W, Hwang S, Trepel J, et al.
    • An W, Hwang S, Trepel J, et al. Protease inhibitor-induced apoptosis: accumulation of wt p53, p21WAF1/ CIP1, and induction of apoptosis are independent markers of proteasome inhibition. Leukemia 2000;14(7):1276
    • (2000) Leukemia , vol.14 , Issue.7 , pp. 1276
  • 15
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: A novel target for cancer chemotherapy
    • Almond J, Cohen G, et al. The proteasome: a novel target for cancer chemotherapy. Leukemia 2002;16(4):433
    • (2002) Leukemia , vol.16 , Issue.4 , pp. 433
    • Almond, J.1    Cohen, G.2
  • 16
    • 58149159907 scopus 로고    scopus 로고
    • Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: Therapeutic approaches
    • Paul S. Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: therapeutic approaches. Bioessays 2008;30(11-12):1172-84
    • (2008) Bioessays , vol.30 , Issue.11-12 , pp. 1172-1184
    • Paul, S.1
  • 17
    • 77649162855 scopus 로고    scopus 로고
    • Sent to destroy the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease
    • Willis MS, Townley-Tilson WHD, Kang EY, et al. Sent to destroy the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease. Circ Res 2010;106(3):463-78
    • (2010) Circ Res , vol.106 , Issue.3 , pp. 463-478
    • Willis, M.S.1    Whd, T.2    Kang, E.Y.3
  • 18
    • 72949089694 scopus 로고    scopus 로고
    • Proteasome Inhibition during Myocardial Infarction
    • Yu X, Kem DC. Proteasome inhibition during myocardial infarction. Cardiovasc Res 2010;85(2):312-20
    • (2010) Cardiovasc Res , vol.85 , Issue.2 , pp. 312-320
    • Yu, X.1    Kem, D.C.2
  • 19
    • 78650840827 scopus 로고    scopus 로고
    • The role of proteasome inhibition with bortezomib in the treatment of antibody-mediated rejection after kidney-only or kidney-combined organ transplantation
    • Flechner SM, Fatica R, Askar M, et al. The role of proteasome inhibition with bortezomib in the treatment of antibody-mediated rejection after kidney-only or kidney-combined organ transplantation. Transplantation 2010;90(12):1486
    • (2010) Transplantation , vol.90 , Issue.12 , pp. 1486
    • Flechner, S.M.1    Fatica, R.2    Askar, M.3
  • 20
    • 0028038601 scopus 로고
    • Peptidomimeticstailored enzyme inhibitors
    • Gante J. Peptidomimeticstailored enzyme inhibitors. Angew Chem Int Ed Engl 1994;33(17):1699-720
    • (1994) Angew Chem Int Ed Engl , vol.33 , Issue.17 , pp. 1699-1720
    • Gante, J.1
  • 21
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev AF, Goldberg AL. Proteasome inhibitors: from research tools to drug candidates. Chem Biol 2001;8(8):739-58
    • (2001) Chem Biol , vol.8 , Issue.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 24
    • 84860436602 scopus 로고    scopus 로고
    • Advances in the understanding of mechanisms and therapeutic use of bortezomib
    • Mujtaba T, Dou Q. Advances in the understanding of mechanisms and therapeutic use of bortezomib. Discov Med 2011;12(67):471-80
    • (2011) Discov Med , vol.12 , Issue.67 , pp. 471-480
    • Mujtaba, T.1    Dou, Q.2
  • 25
    • 0037376230 scopus 로고    scopus 로고
    • Potential for proteasome inhibition in the treatment of cancer
    • Adams J, et al. Potential for proteasome inhibition in the treatment of cancer. Drug Discov Today 2003;8(7):307
    • (2003) Drug Discov Today , vol.8 , Issue.7 , pp. 307
    • Adams, J.1
  • 26
    • 67650754085 scopus 로고    scopus 로고
    • Design, synthesis, biological evaluation, and structure-activity relationship (SAR) discussion of dipeptidyl boronate proteasome inhibitors, part I: Comprehensive understanding of the SAR of a-amino acid boronates
    • Zhu Y, Zhao X, Zhu X, et al. Design, synthesis, biological evaluation, and structure-activity relationship (SAR) discussion of dipeptidyl boronate proteasome inhibitors, part I: comprehensive understanding of the SAR of a-amino acid boronates. J Med Chem 2009;52(14):4192-9
    • (2009) J Med Chem , vol.52 , Issue.14 , pp. 4192-4199
    • Zhu, Y.1    Zhao, X.2    Zhu, X.3
  • 27
    • 84876757363 scopus 로고    scopus 로고
    • Food US, Administration D
    • Food US, Administration D. Approved Drugs - Carfilzomib. 2012. Available from: http://www.fda. gov/Drugs/InformationOnDrugs/ ApprovedDrugs/ucm312945.htm
    • (2012) Approved Drugs - Carfilzomib
  • 28
    • 84873893188 scopus 로고    scopus 로고
    • Carfilzomib: A novel treatment in relapsed and refractory multiple myeloma
    • Fostier K, De Becker A, Schots R. Carfilzomib: a novel treatment in relapsed and refractory multiple myeloma. Onco Targets Ther 2012;5:237
    • (2012) Onco Targets Ther , vol.5 , pp. 237
    • Fostier, K.1    De Becker, A.2    Schots, R.3
  • 29
    • 53049083867 scopus 로고    scopus 로고
    • Mechanisms of proteasome inhibitor action and resistance in cancer
    • McConkey DJ, Zhu K. Mechanisms of proteasome inhibitor action and resistance in cancer. Drug Resist Updat 2008;11(4):164-79
    • (2008) Drug Resist Updat , vol.11 , Issue.4 , pp. 164-179
    • McConkey, D.J.1    Zhu, K.2
  • 31
    • 11144323163 scopus 로고    scopus 로고
    • Virtual screening of chemical libraries
    • Shoichet BK. Virtual screening of chemical libraries. Nature;2004;432(7019):862-5
    • (2004) Nature , vol.432 , Issue.7019 , pp. 862-865
    • Shoichet, B.K.1
  • 32
    • 8844263008 scopus 로고    scopus 로고
    • Docking and scoring in virtual screening for drug discovery: Methods and applications
    • Kitchen DB, Decornez H, Furr JR, Bajorath J. Docking and scoring in virtual screening for drug discovery: methods and applications. Nat Rev Drug Discov 2004;3(11):935-49
    • (2004) Nat Rev Drug Discov , vol.3 , Issue.11 , pp. 935-949
    • Kitchen, D.B.1    Decornez, H.2    Furr, J.R.3    Bajorath, J.4
  • 33
    • 34247487568 scopus 로고    scopus 로고
    • NCI/NIH DTP
    • NCI/NIH DTP. DTP - Diversity Set Information. Available from: http://dtp. nci.nih.gov/branches/dscb/diversity.html
    • DTP - Diversity Set Information
  • 34
    • 1542270307 scopus 로고    scopus 로고
    • Organic copper complexes as a new class of proteasome inhibitors and apoptosis inducers in human cancer cells
    • Daniel KG, Gupta P, Harbach RH, et al. Organic copper complexes as a new class of proteasome inhibitors and apoptosis inducers in human cancer cells. Biochem Pharmacol 2004;67(6):1139-51
    • (2004) Biochem Pharmacol , vol.67 , Issue.6 , pp. 1139-1151
    • Daniel, K.G.1    Gupta, P.2    Harbach, R.H.3
  • 35
    • 77949538037 scopus 로고    scopus 로고
    • Discovery of novel proteasome inhibitors using a high-content cell-based screening system
    • Lavelin I, Beer A, Kam Z, et al. Discovery of novel proteasome inhibitors using a high-content cell-based screening system. PLoS One 2009;4(12):e8503
    • (2009) PLoS One , vol.4 , Issue.12
    • Lavelin, I.1    Beer, A.2    Kam, Z.3
  • 36
    • 77955420821 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of naphthoquinone analogs as a novel class of proteasome inhibitors
    • Lawrence HR, Kazi A, Luo Y, et al. Synthesis and biological evaluation of naphthoquinone analogs as a novel class of proteasome inhibitors. Bioorg Med Chem 2010;18(15):5576-92
    • (2010) Bioorg Med Chem , vol.18 , Issue.15 , pp. 5576-5592
    • Lawrence, H.R.1    Kazi, A.2    Luo, Y.3
  • 37
    • 84858010952 scopus 로고    scopus 로고
    • Discovery and synthesis of hydronaphthoquinones as novel proteasome inhibitors
    • Ge Y, Kazi A, Marsilio F, et al. Discovery and synthesis of hydronaphthoquinones as novel proteasome inhibitors. J Med Chem 2012;55(5):1978-98
    • (2012) J Med Chem , vol.55 , Issue.5 , pp. 1978-1998
    • Ge, Y.1    Kazi, A.2    Marsilio, F.3
  • 38
    • 84862815656 scopus 로고    scopus 로고
    • Design and synthesis of naphthoquinone derivatives as antiproliferative agents and 20S proteasome inhibitors
    • Xu K, Xiao Z, Tang YB, et al. Design and synthesis of naphthoquinone derivatives as antiproliferative agents and 20S proteasome inhibitors. Bioorg Med Chem Lett 2012;22(8):2772-4
    • (2012) Bioorg Med Chem Lett , vol.22 , Issue.8 , pp. 2772-2774
    • Xu, K.1    Xiao, Z.2    Tang, Y.B.3
  • 39
    • 77951769949 scopus 로고    scopus 로고
    • Studies on terrein as a new class of proteasome inhibitors
    • Demasi M, Felicio A, Pacheco A, et al. Studies on terrein as a new class of proteasome inhibitors. J Braz Chem Soc 2010;21(2):299-305
    • (2010) J Braz Chem Soc , vol.21 , Issue.2 , pp. 299-305
    • Demasi, M.1    Felicio, A.2    Pacheco, A.3
  • 40
    • 77956687927 scopus 로고    scopus 로고
    • Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S beta5-subunit
    • Blackburn C, Gigstad KM, Hales P, et al. Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S beta5-subunit. Biochem J 2010;430(Pt 3):461
    • (2010) Biochem J , vol.430 , Issue.PART 3 , pp. 461
    • Blackburn, C.1    Gigstad, K.M.2    Hales, P.3
  • 41
    • 33846886919 scopus 로고    scopus 로고
    • High-throughput bioluminescence screening of ubiquitin-proteasome pathway inhibitors from chemical and natural sources
    • Ausseil F, Samson A, Aussagues Y, et al. High-throughput bioluminescence screening of ubiquitin-proteasome pathway inhibitors from chemical and natural sources. J Biomol Screen 2007;12(1):106-16
    • (2007) J Biomol Screen , vol.12 , Issue.1 , pp. 106-116
    • Ausseil, F.1    Samson, A.2    Aussagues, Y.3
  • 42
    • 84856411945 scopus 로고    scopus 로고
    • Proteasome Inhibitors from Neoboutonia melleri
    • Long C, Beck J, Cantagrel F, et al. Proteasome Inhibitors from Neoboutonia melleri. J Nat Prod 2011;75(1):34-47
    • (2011) J Nat Prod , vol.75 , Issue.1 , pp. 34-47
    • Long, C.1    Beck, J.2    Cantagrel, F.3
  • 43
    • 74849107544 scopus 로고    scopus 로고
    • Novel organic proteasome inhibitors identified by virtual and in vitro screening
    • Basse N, Montes M, Marechal X, et al. Novel organic proteasome inhibitors identified by virtual and in vitro screening. J Med Chem 2009;53(1):509-13
    • (2009) J Med Chem , vol.53 , Issue.1 , pp. 509-513
    • Basse, N.1    Montes, M.2    Marechal, X.3
  • 44
    • 84855288982 scopus 로고    scopus 로고
    • Hydroxyureas as noncovalent proteasome inhibitors
    • Gallastegui N, Beck P, Arciniega M, et al. Hydroxyureas as noncovalent proteasome inhibitors. Angew Chem Int Ed 2012;51(1):247-9
    • (2012) Angew Chem Int Ed , vol.51 , Issue.1 , pp. 247-249
    • Gallastegui, N.1    Beck, P.2    Arciniega, M.3
  • 45
    • 69949163678 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of tripeptide boronic acid proteasome inhibitors
    • Zhu Y, Yao S, Xu B, et al. Design, synthesis and biological evaluation of tripeptide boronic acid proteasome inhibitors. Bioorg Med Chem 2009;17(19):6851-61
    • (2009) Bioorg Med Chem , vol.17 , Issue.19 , pp. 6851-6861
    • Zhu, Y.1    Yao, S.2    Xu, B.3
  • 46
    • 77949367260 scopus 로고    scopus 로고
    • Synthesis, in vitro and in vivo biological evaluation, docking studies, and structure-activity relationship (SAR) discussion of dipeptidyl boronic acid proteasome inhibitors composed of beta-amino acids
    • Zhu Y, Zhu X, Wu G, et al. Synthesis, in vitro and in vivo biological evaluation, docking studies, and structure-activity relationship (SAR) discussion of dipeptidyl boronic acid proteasome inhibitors composed of beta-amino acids. J Med Chem 2010;53(5):1990-9
    • (2010) J Med Chem , vol.53 , Issue.5 , pp. 1990-1999
    • Zhu, Y.1    Zhu, X.2    Wu, G.3
  • 47
    • 78650317245 scopus 로고    scopus 로고
    • Synthesis, in vitro and in vivo biological evaluation, and comprehensive understanding of structure-activity relationships of dipeptidyl boronic acid proteasome inhibitors constructed from beta-amino acids
    • Zhu Y, Wu G, Zhu X, et al. Synthesis, in vitro and in vivo biological evaluation, and comprehensive understanding of structure-activity relationships of dipeptidyl boronic acid proteasome inhibitors constructed from beta-amino acids. J Med Chem 2010;53:8619-26
    • (2010) J Med Chem , vol.53 , pp. 8619-8626
    • Zhu, Y.1    Wu, G.2    Zhu, X.3
  • 48
    • 0035702794 scopus 로고    scopus 로고
    • Tyropeptins A and B, new proteasome inhibitors produced by Kitasatospora sp. MK993-dF2. I. Taxonomy, isolation, physico-chemical properties and biological activities
    • Momose I, Sekizawa R, Hashizume H, et al. Tyropeptins A and B, new proteasome inhibitors produced by Kitasatospora sp. MK993-dF2. I. Taxonomy, isolation, physico-chemical properties and biological activities. J Antibiot 2001;54(12):997-1003
    • (2001) J Antibiot , vol.54 , Issue.12 , pp. 997-1003
    • Momose, I.1    Sekizawa, R.2    Hashizume, H.3
  • 49
    • 0035702629 scopus 로고    scopus 로고
    • Tyropeptins A and B, new proteasome inhibitors produced by Kitasatospora sp. MK993-dF2. II. Structure determination and synthesis
    • Momose I, Sekizawa R, Hirosawa S, et al. Tyropeptins A and B, new proteasome inhibitors produced by Kitasatospora sp. MK993-dF2. II. Structure determination and synthesis. J Antibiot 2001;54(12):1004-12
    • (2001) J Antibiot , vol.54 , Issue.12 , pp. 1004-1012
    • Momose, I.1    Sekizawa, R.2    Hirosawa, S.3
  • 50
    • 63149175963 scopus 로고    scopus 로고
    • Synthesis of boronic acid derivatives of tyropeptin: Proteasome inhibitors
    • Watanabe T, Momose I, Abe M, et al. Synthesis of boronic acid derivatives of tyropeptin: proteasome inhibitors. Bioorg Med Chem Lett 2009;19(8):2343-5
    • (2009) Bioorg Med Chem Lett , vol.19 , Issue.8 , pp. 2343-2345
    • Watanabe, T.1    Momose, I.2    Abe, M.3
  • 51
    • 77957557116 scopus 로고    scopus 로고
    • Structure-activity relationship of boronic acid derivatives of tyropeptin: Proteasome inhibitors
    • Watanabe T, Abe H, Momose I, et al. Structure-activity relationship of boronic acid derivatives of tyropeptin: Proteasome inhibitors. Bioorg Med Chem Lett 2010;20(19):5839-42
    • (2010) Bioorg Med Chem Lett , vol.20 , Issue.19 , pp. 5839-5842
    • Watanabe, T.1    Abe, H.2    Momose, I.3
  • 52
    • 84887212220 scopus 로고    scopus 로고
    • Belactosin A, a novel antitumor antibiotic acting on cyclin/CDK mediated cell cycle regulation, produced by Streptomyces sp
    • Asai A, Hasegawa A, Ochiai K, et al. Belactosin A, a novel antitumor antibiotic acting on cyclin/CDK mediated cell cycle regulation, produced by Streptomyces sp. ChemInform 2000;31:24
    • (2000) ChemInform , vol.31 , pp. 24
    • Asai, A.1    Hasegawa, A.2    Ochiai, K.3
  • 53
    • 1642276251 scopus 로고    scopus 로고
    • A new structural class of proteasome inhibitors identified by microbial screening using yeast-based assay
    • Asai A, Tsujita T, Sharma SV, et al. A new structural class of proteasome inhibitors identified by microbial screening using yeast-based assay. Biochem Pharmacol 2004;67(2):227-34
    • (2004) Biochem Pharmacol , vol.67 , Issue.2 , pp. 227-234
    • Asai, A.1    Tsujita, T.2    Sharma, S.V.3
  • 54
    • 65749085916 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of boron peptide analogues of Belactosin C as proteasome inhibitors
    • Nakamura H, Watanabe M, Ban HS, et al. Synthesis and biological evaluation of boron peptide analogues of Belactosin C as proteasome inhibitors. Bioorg Med Chem Lett 2009;19(12):3220-4
    • (2009) Bioorg Med Chem Lett , vol.19 , Issue.12 , pp. 3220-3224
    • Nakamura, H.1    Watanabe, M.2    Ban, H.S.3
  • 55
    • 70349918652 scopus 로고    scopus 로고
    • Pharmacophore modeling, docking studies, and synthesis of novel dipeptide proteasome inhibitors containing boron atoms
    • Lei M, Zhao X, Wang Z, Zhu Y. Pharmacophore modeling, docking studies, and synthesis of novel dipeptide proteasome inhibitors containing boron atoms. J Chem Inf Model 2009;49(9):2092-100
    • (2009) J Chem Inf Model , vol.49 , Issue.9 , pp. 2092-2100
    • Lei, M.1    Zhao, X.2    Wang, Z.3    Zhu, Y.4
  • 57
    • 39749143840 scopus 로고    scopus 로고
    • Discovery of a potent, selective, and orally active proteasome inhibitor for the treatment of cancer
    • Dorsey BD, Iqbal M, Chatterjee S, et al. Discovery of a potent, selective, and orally active proteasome inhibitor for the treatment of cancer. J Med Chem 2008;51(4):1068-72
    • (2008) J Med Chem , vol.51 , Issue.4 , pp. 1068-1072
    • Dorsey, B.D.1    Iqbal, M.2    Chatterjee, S.3
  • 58
    • 33746356860 scopus 로고    scopus 로고
    • Recent advances (1995-2005) in fluorinated pharmaceuticals based on natural products
    • Bégué JP, Bonnet-Delpon D. Recent advances (1995-2005) in fluorinated pharmaceuticals based on natural products. J fluorine Chem 2006;127(8):992-1012
    • (2006) J Fluorine Chem , vol.127 , Issue.8 , pp. 992-1012
    • Bégué, J.P.1    Bonnet-Delpon, D.2
  • 59
    • 84887211925 scopus 로고    scopus 로고
    • The many roles for fluorine in medicinal chemistry
    • Hagmann WK. The many roles for fluorine in medicinal chemistry. ChemInform 2008;39:45
    • (2008) ChemInform , vol.39 , pp. 45
    • Hagmann, W.K.1
  • 60
    • 33645454126 scopus 로고    scopus 로고
    • Fluorine in medicinal chemistry: A review of anti-cancer agents
    • Isanbor C, OHagan D. Fluorine in medicinal chemistry: a review of anti-cancer agents. J Fluorine Chem 2006;127(3):303-19
    • (2006) J Fluorine Chem , vol.127 , Issue.3 , pp. 303-319
    • Isanbor, C.1    Ohagan, D.2
  • 62
    • 67650032601 scopus 로고    scopus 로고
    • New difluoro Knoevenagel condensates of curcumin, their Schiff bases and copper complexes as proteasome inhibitors and apoptosis inducers in cancer cells
    • Padhye S, Yang H, Jamadar A, et al. New difluoro Knoevenagel condensates of curcumin, their Schiff bases and copper complexes as proteasome inhibitors and apoptosis inducers in cancer cells. Pharm Res 2009;26(8):1874-80
    • (2009) Pharm Res , vol.26 , Issue.8 , pp. 1874-1880
    • Padhye, S.1    Yang, H.2    Jamadar, A.3
  • 63
    • 33746614663 scopus 로고    scopus 로고
    • Selective fluorination in drug design and development: An overview of biochemical rationales
    • Kirk KL. Selective fluorination in drug design and development: an overview of biochemical rationales. Curr Top Med Chem 2006;6(14):1447-56
    • (2006) Curr Top Med Chem , vol.6 , Issue.14 , pp. 1447-1456
    • Kirk, K.L.1
  • 64
    • 4444355871 scopus 로고    scopus 로고
    • Fluorine in medicinal chemistry
    • Bohm HJ, Banner D, Bendels S, et al. Fluorine in medicinal chemistry. ChemBioChem 2004;5(5):637-43
    • (2004) ChemBioChem , vol.5 , Issue.5 , pp. 637-643
    • Bohm, H.J.1    Banner, D.2    Bendels, S.3
  • 65
    • 57849087338 scopus 로고    scopus 로고
    • Novel fluorinated pseudopeptides as proteasome inhibitors
    • Formicola L, Maréchal X, Basse N, et al. Novel fluorinated pseudopeptides as proteasome inhibitors. Bioorg Med Chem Lett 2009;19(1):83-6
    • (2009) Bioorg Med Chem Lett , vol.19 , Issue.1 , pp. 83-86
    • Formicola, L.1    Maréchal, X.2    Basse, N.3
  • 66
    • 23844508811 scopus 로고    scopus 로고
    • A labdane diterpene glucoside from the rhizomes of curcuma mangga
    • Abas F, Lajis NH, Shaari K, et al. A labdane diterpene glucoside from the rhizomes of curcuma mangga. J Nat Prod 2005;68(7):1090-3
    • (2005) J Nat Prod , vol.68 , Issue.7 , pp. 1090-1093
    • Abas, F.1    Lajis, N.H.2    Shaari, K.3
  • 67
    • 34248205135 scopus 로고    scopus 로고
    • Polymeric nanoparticle-encapsulated curcumin (nanocurcumin): A novel strategy for human cancer therapy
    • Bisht S, Feldmann G, Soni S, et al. Polymeric nanoparticle-encapsulated curcumin (nanocurcumin): a novel strategy for human cancer therapy. J Nanobiotechnology 2007;5(3):1-18
    • (2007) J Nanobiotechnology , vol.5 , Issue.3 , pp. 1-18
    • Bisht, S.1    Feldmann, G.2    Soni, S.3
  • 68
    • 2542450825 scopus 로고    scopus 로고
    • Role of curcumin, a naturally occurring phenolic compound of turmeric in accelerating the repair of excision wound, in mice whole-body exposed to various doses of g-radiation
    • Jagetia GC, Rajanikant G. Role of curcumin, a naturally occurring phenolic compound of turmeric in accelerating the repair of excision wound, in mice whole-body exposed to various doses of g-radiation. J Surg Res 2004;120(1):127-38
    • (2004) J Surg Res , vol.120 , Issue.1 , pp. 127-138
    • Jagetia, G.C.1    Rajanikant, G.2
  • 69
    • 54749132655 scopus 로고    scopus 로고
    • Curcumin inhibits the proteasome activity in human colon cancer cells in vitro and in vivo
    • Milacic V, Banerjee S, Landis-Piwowar KR, et al. Curcumin inhibits the proteasome activity in human colon cancer cells in vitro and in vivo. Cancer Res 2008;68(18):7283-92
    • (2008) Cancer Res , vol.68 , Issue.18 , pp. 7283-7292
    • Milacic, V.1    Banerjee, S.2    Landis-Piwowar, K.R.3
  • 70
    • 77949343548 scopus 로고    scopus 로고
    • Incorporation of fluorinated phenylalanine generates highly specific inhibitor of proteasomes chymotrypsin-like sites
    • Geurink PP, Liu N, Spaans MP, et al. Incorporation of fluorinated phenylalanine generates highly specific inhibitor of proteasomes chymotrypsin-like sites. J Med Chem 2010;53(5):2319-23
    • (2010) J Med Chem , vol.53 , Issue.5 , pp. 2319-2323
    • Geurink, P.P.1    Liu, N.2    Spaans, M.P.3
  • 71
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution
    • Lowe J, Stock D, Jap B, et al. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science (New York, NY). 1995;268(5210):533
    • (1995) Science (New York, NY) , vol.268 , Issue.5210 , pp. 533
    • Lowe, J.1    Stock, D.2    Jap, B.3
  • 72
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky A, Michaud C, Powers JC, Orlowski M. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 1992;31(39):9421-8
    • (1992) Biochemistry , vol.31 , Issue.39 , pp. 9421-9428
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 73
    • 15044349908 scopus 로고    scopus 로고
    • Structure-based design of derivatives of tyropeptin A as the potent and selective inhibitors of mammalian 20S proteasome
    • Momose I, Umezawa Y, Hirosawa S, et al. Structure-based design of derivatives of tyropeptin A as the potent and selective inhibitors of mammalian 20S proteasome. Bioorg Med Chem Lett 2005;15(7):1867-71
    • (2005) Bioorg Med Chem Lett , vol.15 , Issue.7 , pp. 1867-1871
    • Momose, I.1    Umezawa, Y.2    Hirosawa, S.3
  • 74
    • 0033117370 scopus 로고    scopus 로고
    • Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes
    • Loidl G, Groll M, Musiol HJ, et al. Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes. Chem Biol 1999;6(4):197-204
    • (1999) Chem Biol , vol.6 , Issue.4 , pp. 197-204
    • Loidl, G.1    Groll, M.2    Musiol, H.J.3
  • 75
    • 79955464405 scopus 로고    scopus 로고
    • MG132 treatment attenuates cardiac remodeling and dysfunction following aortic banding in rats via the NF-kB TGFb1 pathway
    • Ma Y, Chen B, Liu D, et al. MG132 treatment attenuates cardiac remodeling and dysfunction following aortic banding in rats via the NF-kB/ TGFb1 pathway. Biochem Pharmacol 2011;81(10):1228-36
    • (2011) Biochem Pharmacol , vol.81 , Issue.10 , pp. 1228-1236
    • Ma, Y.1    Chen, B.2    Liu, D.3
  • 76
    • 0033765620 scopus 로고    scopus 로고
    • A survey of calpain inhibitors
    • Donkor I. A survey of calpain inhibitors. Curr Med Chem 2000;7(12):1171-88
    • (2000) Curr Med Chem , vol.7 , Issue.12 , pp. 1171-1188
    • Donkor, I.1
  • 77
    • 0029877917 scopus 로고    scopus 로고
    • Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine
    • Tsubuki S, Saito Y, Tomioka M, et al. Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine. J Biochem 1996;119(3):572-6
    • (1996) J Biochem , vol.119 , Issue.3 , pp. 572-576
    • Tsubuki, S.1    Saito, Y.2    Tomioka, M.3
  • 78
    • 0027416049 scopus 로고
    • In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal
    • Sherwood SW, Kung AL, Roitelman J, et al. In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal. Proc Natl Acad Sci 1993;90(8):3353-7
    • (1993) Proc Natl Acad Sci , vol.90 , Issue.8 , pp. 3353-3357
    • Sherwood, S.W.1    Kung, A.L.2    Roitelman, J.3
  • 79
    • 33646407310 scopus 로고    scopus 로고
    • MG132 induced apoptosis is associated with p53-independent induction of pro-apoptotic Noxa and transcriptional activity of beta-catenin
    • Jullig M, Zhang W, Ferreira A, Stott N. MG132 induced apoptosis is associated with p53-independent induction of pro-apoptotic Noxa and transcriptional activity of beta-catenin. Apoptosis 2006;11(4):627-41
    • (2006) Apoptosis , vol.11 , Issue.4 , pp. 627-641
    • Jullig, M.1    Zhang, W.2    Ferreira, A.3    Stott, N.4
  • 80
    • 68249153842 scopus 로고    scopus 로고
    • The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH
    • Han YH, Moon HJ, You BR, Park WH. The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH. Oncol Rep 2009;22(1):215-21
    • (2009) Oncol Rep , vol.22 , Issue.1 , pp. 215-221
    • Han, Y.H.1    Moon, H.J.2    You, B.R.3    Park, W.H.4
  • 81
    • 80053248961 scopus 로고    scopus 로고
    • Synthesis and sar study of novel peptide aldehydes as inhibitors of 20S Proteasome
    • Ma Y, Xu B, Fang Y, et al. Synthesis and SAR study of novel peptide aldehydes as inhibitors of 20S proteasome. Molecules 2011;16(9):7551-64
    • (2011) Molecules , vol.16 , Issue.9 , pp. 7551-7564
    • Ma, Y.1    Xu, B.2    Fang, Y.3
  • 82
    • 79959757218 scopus 로고    scopus 로고
    • Development of novel peptidomimetics containing a vinyl sulfone moiety as proteasome inhibitors
    • Ettari R, Bonaccorso C, Micale N, et al. Development of novel peptidomimetics containing a vinyl sulfone moiety as proteasome inhibitors. ChemMedChem 2011;6(7):1228-37
    • (2011) ChemMedChem , vol.6 , Issue.7 , pp. 1228-1237
    • Ettari, R.1    Bonaccorso, C.2    Micale, N.3
  • 83
    • 80054890742 scopus 로고    scopus 로고
    • New aldehyde and vinylsulfone proteasome inhibitors for targeted melanoma therapy
    • Vivier M, Rapp M, Galmier MJ, et al. New aldehyde and vinylsulfone proteasome inhibitors for targeted melanoma therapy. Eur J Med Chem 2011;46(11):5705-10
    • (2011) Eur J Med Chem , vol.46 , Issue.11 , pp. 5705-5710
    • Vivier, M.1    Rapp, M.2    Galmier, M.J.3
  • 84
    • 78650051900 scopus 로고    scopus 로고
    • Nature of pharmacophore influences active site specificity of proteasome inhibitors
    • Screen M, Britton M, Downey SL, et al. Nature of pharmacophore influences active site specificity of proteasome inhibitors. J Biol Chem 2010;285(51):40125-34
    • (2010) J Biol Chem , vol.285 , Issue.51 , pp. 40125-40134
    • Screen, M.1    Britton, M.2    Downey, S.L.3
  • 86
    • 69249206535 scopus 로고    scopus 로고
    • Capillary electrophoresis for screening of 20S proteasome inhibitors
    • Chen W, Mou K, Xu B, et al. Capillary electrophoresis for screening of 20S proteasome inhibitors. Anal Biochem 2009;394(1):62-7
    • (2009) Anal Biochem , vol.394 , Issue.1 , pp. 62-67
    • Chen, W.1    Mou, K.2    Xu, B.3
  • 87
    • 33645471039 scopus 로고    scopus 로고
    • Peptide and peptide-like modulators of 20S proteasome enzymatic activity in cancer cells
    • García-Echeverría C. Peptide and peptide-like modulators of 20S proteasome enzymatic activity in cancer cells. Int J Pept Res Ther 2006;12(1):49-64
    • (2006) Int J Pept Res Ther , vol.12 , Issue.1 , pp. 49-64
    • García-Echeverría, C.1
  • 88
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers JC, Asgian JL, Ekici OD, et al. Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem Rev 2002;102(12):4639-750
    • (2002) Chem Rev , vol.102 , Issue.12 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3
  • 89
    • 78650465724 scopus 로고    scopus 로고
    • Synthesis and proteasome inhibition of N-allyl vinyl ester-based peptides
    • Baldisserotto A, Franceschini C, Scalambra F, et al. Synthesis and proteasome inhibition of N-allyl vinyl ester-based peptides. J Pept Sci 2010;16(11):659-63
    • (2010) J Pept Sci , vol.16 , Issue.11 , pp. 659-663
    • Baldisserotto, A.1    Franceschini, C.2    Scalambra, F.3
  • 90
    • 34447116376 scopus 로고    scopus 로고
    • Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome
    • Demo SD, Kirk CJ, Aujay MA, et al. Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome. Cancer Res 2007;67(13):6383-91
    • (2007) Cancer Res , vol.67 , Issue.13 , pp. 6383-6391
    • Demo, S.D.1    Kirk, C.J.2    Ma, A.3
  • 91
    • 50249092779 scopus 로고    scopus 로고
    • Development of proteasome inhibitors in oncology and autoimmune diseases
    • Bennett M, Kirk C, et al. Development of proteasome inhibitors in oncology and autoimmune diseases. Curr Opin Drug Discov Dev 2008;11(5):616
    • (2008) Curr Opin Drug Discov Dev , vol.11 , Issue.5 , pp. 616
    • Bennett, M.1    Kirk, C.2
  • 92
    • 36148944490 scopus 로고    scopus 로고
    • Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma
    • Kuhn DJ, Chen Q, Voorhees PM, et al. Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma. Blood 2007;110(9):3281-90
    • (2007) Blood , vol.110 , Issue.9 , pp. 3281-3290
    • Kuhn, D.J.1    Chen, Q.2    Voorhees, P.M.3
  • 93
    • 35748970136 scopus 로고    scopus 로고
    • Multicenter phase i studies to evaluate the safety, tolerability, and clinical response to intensive dosing with the proteasome inhibitor PR-171 in patients with relapsed or refractory hematological malignancies
    • 688A
    • Oconnor O, Orlowski R, Alsina M, et al. Multicenter phase I studies to evaluate the safety, tolerability, and clinical response to intensive dosing with the proteasome inhibitor PR-171 in patients with relapsed or refractory hematological malignancies. Blood 2006;108(11):687A-8A
    • (2006) Blood , vol.108 , Issue.11
    • Oconnor, O.1    Orlowski, R.2    Alsina, M.3
  • 94
    • 33847410207 scopus 로고    scopus 로고
    • The proteasome inhibitors bortezomib and PR-171 have antiproliferative and proapoptotic effects on primary human acute myeloid leukaemia cells
    • Stapnes C, Døskeland AP, Hatfield K, et al. The proteasome inhibitors bortezomib and PR-171 have antiproliferative and proapoptotic effects on primary human acute myeloid leukaemia cells. Br J Haematol 2007;136(6):814-28
    • (2007) Br J Haematol , vol.136 , Issue.6 , pp. 814-828
    • Stapnes, C.1    Døskeland, A.P.2    Hatfield, K.3
  • 95
    • 50249138003 scopus 로고    scopus 로고
    • Safety and antitumor efficacy of the proteasome inhibitor carfilzomib (PR- 171) dosed for five consecutive days in hematologic malignancies: Phase 1 results
    • Orlowski R, Stewart K, Vallone M, et al. Safety and antitumor efficacy of the proteasome inhibitor carfilzomib (PR- 171) dosed for five consecutive days in hematologic malignancies: phase 1 results. BLOOD-New York 2007;110(11):409
    • (2007) BLOOD-New York , vol.110 , Issue.11 , pp. 409
    • Orlowski, R.1    Stewart, K.2    Vallone, M.3
  • 96
    • 50249150555 scopus 로고    scopus 로고
    • Phase 1 single agent antitumor activity of twice weekly consecutive day dosing of the proteasome inhibitor carfilzomib (PR-171) in hematologic malignancies
    • Alsina M, Trudel S, Vallone M, et al. Phase 1 single agent antitumor activity of twice weekly consecutive day dosing of the proteasome inhibitor carfilzomib (PR-171) in hematologic malignancies. Blood (New York) 2007;110(11):411
    • (2007) Blood (New York) , vol.110 , Issue.11 , pp. 411
    • Alsina, M.1    Trudel, S.2    Vallone, M.3
  • 97
    • 65649139708 scopus 로고    scopus 로고
    • Design and synthesis of an orally bioavailable and selective peptide epoxyketone proteasome inhibitor (PR- 047)
    • Zhou HJ, Aujay MA, Bennett MK, et al. Design and synthesis of an orally bioavailable and selective peptide epoxyketone proteasome inhibitor (PR- 047). J Med Chem 2009;52(9):3028-38
    • (2009) J Med Chem , vol.52 , Issue.9 , pp. 3028-3038
    • Zhou, H.J.1    Ma, A.2    Bennett, M.K.3
  • 98
    • 23944491179 scopus 로고    scopus 로고
    • Pseudomonas syringae genes induced during colonization of leaf surfaces
    • Marco ML, Legac J, Lindow SE. Pseudomonas syringae genes induced during colonization of leaf surfaces. Environ Microbiol 2005;7(9):1379-91
    • (2005) Environ Microbiol , vol.7 , Issue.9 , pp. 1379-1391
    • Marco, M.L.1    Legac, J.2    Lindow, S.E.3
  • 99
    • 0023798582 scopus 로고
    • Glidobactins A, B and C, new antitumor antibiotics. I. Production, isolation, chemical properties and biological activity
    • Oka M, Nishiyama Y, Ohta S, et al. Glidobactins A, B and C, new antitumor antibiotics. I. Production, isolation, chemical properties and biological activity. J Antibiot (Tokyo) 1988;41(10):1331
    • (1988) J Antibiot (Tokyo) , vol.41 , Issue.10 , pp. 1331
    • Oka, M.1    Nishiyama, Y.2    Ohta, S.3
  • 100
    • 66149090781 scopus 로고    scopus 로고
    • Synthetic and structural studies on syringolin A and B reveal critical determinants of selectivity and potency of proteasome inhibition
    • Clerc J, Groll M, Illich DJ, et al. Synthetic and structural studies on syringolin A and B reveal critical determinants of selectivity and potency of proteasome inhibition. Proc Nat Acad Sci 2009;106(16):6507-12
    • (2009) Proc Nat Acad Sci , vol.106 , Issue.16 , pp. 6507-6512
    • Clerc, J.1    Groll, M.2    Illich, D.J.3
  • 101
    • 77954756715 scopus 로고    scopus 로고
    • Convergent synthesis and biological evaluation of syringolin A and derivatives as eukaryotic 20S proteasome inhibitors
    • Clerc J, Schellenberg B, Groll M, et al. Convergent synthesis and biological evaluation of syringolin A and derivatives as eukaryotic 20S proteasome inhibitors. Eur J Org Chem 2010;2010(21):3991-4003
    • (2010) Eur J Org Chem , vol.2010 , Issue.21 , pp. 3991-4003
    • Clerc, J.1    Schellenberg, B.2    Groll, M.3
  • 102
    • 84867496886 scopus 로고    scopus 로고
    • Activity Enhancement of Synthetic Syrbactin Proteasome Inhibitor Hybrid and Biological Evaluation in Tumor Cells
    • Archer CR, Groll M, Stein ML, et al. Activity enhancement of synthetic syrbactin proteasome inhibitor hybrid and biological evaluation in tumor cells. Biochemistry 2012;51(34):6880-8
    • (2012) Biochemistry , vol.51 , Issue.34 , pp. 6880-6888
    • Archer, C.R.1    Groll, M.2    Stein, M.L.3
  • 103
    • 82955223252 scopus 로고    scopus 로고
    • Discovery of a potent and highly b1 specific proteasome inhibitor from a focused library of urea-containing peptide vinyl sulfones and peptide epoxyketones
    • van der Linden WA, Willems LI, Shabaneh TB, et al. Discovery of a potent and highly b1 specific proteasome inhibitor from a focused library of urea-containing peptide vinyl sulfones and peptide epoxyketones. Org Biomol Chem 2012;10(1):181-94
    • (2012) Org Biomol Chem , vol.10 , Issue.1 , pp. 181-194
    • Van Der Linden, W.A.1    Willems, L.I.2    Shabaneh, T.B.3
  • 104
    • 33751040506 scopus 로고    scopus 로고
    • Syringolin A, a new plant elicitor from the phytopathogenic bacterium Pseudomonas syringae pv. syringae, inhibits the proliferation of neuroblastoma and ovarian cancer cells and induces apoptosis
    • Coleman C, Rocetes J, Park D, et al. Syringolin A, a new plant elicitor from the phytopathogenic bacterium Pseudomonas syringae pv. syringae, inhibits the proliferation of neuroblastoma and ovarian cancer cells and induces apoptosis. Cell Prolif 2006;39(6):599-609
    • (2006) Cell Prolif , vol.39 , Issue.6 , pp. 599-609
    • Coleman, C.1    Rocetes, J.2    Park, D.3
  • 105
    • 42049085712 scopus 로고    scopus 로고
    • A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism
    • Groll M, Schellenberg B, Bachmann AS, et al. A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism. Nature 2008;452(7188):755-8
    • (2008) Nature , vol.452 , Issue.7188 , pp. 755-758
    • Groll, M.1    Schellenberg, B.2    Bachmann, A.S.3
  • 106
    • 78649885502 scopus 로고    scopus 로고
    • The natural product hybrid of syringolin a and glidobactin a synergizes proteasome inhibition potency with subsite selectivity
    • Clerc J, Li N, Krahn D, et al. The natural product hybrid of Syringolin A and Glidobactin A synergizes proteasome inhibition potency with subsite selectivity. Chem Commun 2011;47(1):385-7
    • (2011) Chem Commun , vol.47 , Issue.1 , pp. 385-387
    • Clerc, J.1    Li, N.2    Krahn, D.3
  • 107
    • 54849417391 scopus 로고    scopus 로고
    • Natural polyphenols as proteasome modulators and their role as anti-cancer compounds
    • Bonfili L, Cecarini V, Amici M, et al. Natural polyphenols as proteasome modulators and their role as anti-cancer compounds. FEBS J 2008;275(22):5512-26
    • (2008) FEBS J , vol.275 , Issue.22 , pp. 5512-5526
    • Bonfili, L.1    Cecarini, V.2    Amici, M.3
  • 108
    • 34249780515 scopus 로고    scopus 로고
    • Structure-proteasome-inhibitory activity relationships of dietary flavonoids in human cancer cells
    • Chen D, Chen MS, Cui QC, et al. Structure-proteasome-inhibitory activity relationships of dietary flavonoids in human cancer cells. Front Biosci 2007;12:1935-45
    • (2007) Front Biosci , vol.12 , pp. 1935-1945
    • Chen, D.1    Chen, M.S.2    Cui, Q.C.3
  • 109
    • 18044383342 scopus 로고    scopus 로고
    • Dietary flavonoids as proteasome inhibitors and apoptosis inducers in human leukemia cells
    • Chen D, Daniel KG, Chen MS, et al. Dietary flavonoids as proteasome inhibitors and apoptosis inducers in human leukemia cells. Biochem Pharmacol 2005;69(10):1421-32
    • (2005) Biochem Pharmacol , vol.69 , Issue.10 , pp. 1421-1432
    • Chen, D.1    Daniel, K.G.2    Chen, M.S.3
  • 110
    • 70350332192 scopus 로고    scopus 로고
    • Inhibitory effect of flavonoids on 26S proteasome activity
    • Chang TL. Inhibitory effect of flavonoids on 26S proteasome activity. J Agric Food Chem 2009;57(20):9706-15
    • (2009) J Agric Food Chem , vol.57 , Issue.20 , pp. 9706-9715
    • Chang, T.L.1
  • 111
    • 79952175319 scopus 로고    scopus 로고
    • 20S proteasome inhibitory activity of flavonoids isolated from spatholobus suberectus
    • Shim SH. 20S proteasome inhibitory activity of flavonoids isolated from Spatholobus suberectus. Phytother Res 2011;25(4):615-18
    • (2011) Phytother Res , vol.25 , Issue.4 , pp. 615-618
    • Shim, S.H.1
  • 112
    • 33744924884 scopus 로고    scopus 로고
    • Microarray-assisted pathway analysis identifies mitogen-activated protein kinase signaling as a mediator of resistance to the green tea polyphenol epigallocatechin 3-gallate in her-2/neu-overexpressing breast cancer cells
    • Guo S, Lu J, Subramanian A, Sonenshein GE. Microarray-assisted pathway analysis identifies mitogen-activated protein kinase signaling as a mediator of resistance to the green tea polyphenol epigallocatechin 3-gallate in her-2/neu-overexpressing breast cancer cells. Cancer Res 2006;66(10):5322-9
    • (2006) Cancer Res , vol.66 , Issue.10 , pp. 5322-5329
    • Guo, S.1    Lu, J.2    Subramanian, A.3    Sonenshein, G.E.4
  • 113
    • 33745627071 scopus 로고    scopus 로고
    • Green tea, black tea and breast cancer risk: A meta-analysis of epidemiological studies
    • Sun CL, Yuan JM, Koh WP, Mimi CY. Green tea, black tea and breast cancer risk: a meta-analysis of epidemiological studies. Carcinogenesis 2006;27(7):1310-15
    • (2006) Carcinogenesis , vol.27 , Issue.7 , pp. 1310-1315
    • Sun, C.L.1    Yuan, J.M.2    Koh, W.P.3    Mimi, C.Y.4
  • 114
    • 0035731418 scopus 로고    scopus 로고
    • Green tea and its catechins inhibit breast cancer xenografts
    • Sartippour MR, Heber D, Ma J, et al. Green tea and its catechins inhibit breast cancer xenografts. Nutr Cancer 2001;40(2):149-56
    • (2001) Nutr Cancer , vol.40 , Issue.2 , pp. 149-156
    • Sartippour, M.R.1    Heber, D.2    Ma, J.3
  • 115
    • 0031878494 scopus 로고    scopus 로고
    • Inhibition of spontaneous formation of lung tumors and rhabdomyosarcomas in A/J mice by black and green tea
    • Landau JM, Wang ZY, Yang GY, et al. Inhibition of spontaneous formation of lung tumors and rhabdomyosarcomas in A/J mice by black and green tea. Carcinogenesis 1998;19(3):501-7
    • (1998) Carcinogenesis , vol.19 , Issue.3 , pp. 501-507
    • Landau, J.M.1    Wang, Z.Y.2    Yang, G.Y.3
  • 116
    • 21144458334 scopus 로고    scopus 로고
    • Synergistic effect of green tea catechins on cell growth and apoptosis induction in gastric carcinoma cells
    • Horie N, Hirabayashi N, Takahashi Y, et al. Synergistic effect of green tea catechins on cell growth and apoptosis induction in gastric carcinoma cells. Biol Pharm Bull 2005;28(4):574-9
    • (2005) Biol Pharm Bull , vol.28 , Issue.4 , pp. 574-579
    • Horie, N.1    Hirabayashi, N.2    Takahashi, Y.3
  • 117
    • 31544473720 scopus 로고    scopus 로고
    • Chemoprevention of human prostate cancer by oral administration of green tea catechins in volunteers with high-grade prostate intraepithelial neoplasia: A preliminary report from a one-year proof-of-principle study
    • Bettuzzi S, Brausi M, Rizzi F, et al. Chemoprevention of human prostate cancer by oral administration of green tea catechins in volunteers with high-grade prostate intraepithelial neoplasia: a preliminary report from a one-year proof-of-principle study. Cancer Res 2006;66(2):1234-40
    • (2006) Cancer Res , vol.66 , Issue.2 , pp. 1234-1240
    • Bettuzzi, S.1    Brausi, M.2    Rizzi, F.3
  • 118
    • 0042738859 scopus 로고    scopus 로고
    • Inhibition of bladder tumor growth by the green tea derivative epigallocatechin-3-gallate
    • Kemberling J, Hampton JA, Keck RW, et al. Inhibition of bladder tumor growth by the green tea derivative epigallocatechin-3-gallate. J Urol 2003;170(3):773-6
    • (2003) J Urol , vol.170 , Issue.3 , pp. 773-776
    • Kemberling, J.1    Hampton, J.A.2    Keck, R.W.3
  • 119
    • 0347417005 scopus 로고    scopus 로고
    • Docking studies and model development of tea polyphenol proteasome inhibitors: Applications to rational drug design
    • Smith DM, Daniel KG, Wang Z, et al. Docking studies and model development of tea polyphenol proteasome inhibitors: applications to rational drug design. Proteins 2003;54(1):58-70
    • (2003) Proteins , vol.54 , Issue.1 , pp. 58-70
    • Smith, D.M.1    Daniel, K.G.2    Wang, Z.3
  • 120
    • 0035918278 scopus 로고    scopus 로고
    • Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo
    • Nam S, Smith DM, Dou QP. Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo. J Biol Chem 2001;276(16):13322-30
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 13322-13330
    • Nam, S.1    Smith, D.M.2    Dou, Q.P.3
  • 121
    • 0033072318 scopus 로고    scopus 로고
    • Methylation of tea catechins by rat liver homogenates
    • Okushio K, Suzuki M, Matsumoto N, et al. Methylation of tea catechins by rat liver homogenates. Biosci Biotechnol Biochem 1999;63(2):430-2
    • (1999) Biosci Biotechnol Biochem , vol.63 , Issue.2 , pp. 430-432
    • Okushio, K.1    Suzuki, M.2    Matsumoto, N.3
  • 122
    • 0037403751 scopus 로고    scopus 로고
    • Enzymology of methylation of tea catechins and inhibition of catechol-O-methyltransferase by (-)-epigallocatechin gallate
    • Lu H, Meng X, Yang CS. Enzymology of methylation of tea catechins and inhibition of catechol-O-methyltransferase by (-)-epigallocatechin gallate. Drug Metab Dispos 2003;31(5):572-9
    • (2003) Drug Metab Dispos , vol.31 , Issue.5 , pp. 572-579
    • Lu, H.1    Meng, X.2    Yang, C.S.3
  • 123
    • 75449099982 scopus 로고    scopus 로고
    • Proteasome inhibition in human breast cancer cells with high catechol-omethyltransferase activity by green tea polyphenol EGCG Analogs
    • Huo C, Yang H, Cui QC, et al. Proteasome inhibition in human breast cancer cells with high catechol-Omethyltransferase activity by green tea polyphenol EGCG analogs. Bioorg Med Chem 2010;18(3):1252-8
    • (2010) Bioorg Med Chem , vol.18 , Issue.3 , pp. 1252-1258
    • Huo, C.1    Yang, H.2    Cui, Q.C.3
  • 124
    • 33847656177 scopus 로고    scopus 로고
    • Methylation of green tea polyphenols affects their binding to and inhibitory poses of the proteasome beta5 subunit
    • Daniel KG, Landis-Piwowar KR, Chen D, et al. Methylation of green tea polyphenols affects their binding to and inhibitory poses of the proteasome beta5 subunit. Int J Mol Med 2006;18(4):625
    • (2006) Int J Mol Med , vol.18 , Issue.4 , pp. 625
    • Daniel, K.G.1    Landis-Piwowar, K.R.2    Chen, D.3
  • 125
    • 77955722773 scopus 로고    scopus 로고
    • Computational modeling of the potential interactions of the proteasome b5 subunit and catechol-Omethyltransferase- resistant EGCG analogs
    • Kanwar J, Mohammad I, Yang H, et al. Computational modeling of the potential interactions of the proteasome b5 subunit and catechol- Omethyltransferase- resistant EGCG analogs. Int J Mol Med 2010;26(2):209
    • (2010) Int J Mol Med , vol.26 , Issue.2 , pp. 209
    • Kanwar, J.1    Mohammad, I.2    Yang, H.3
  • 126
    • 79953888335 scopus 로고    scopus 로고
    • Identification of an EGCG oxidation derivative with proteasome modulatory activity
    • Bonfili L, Cuccioloni M, Mozzicafreddo M, et al. Identification of an EGCG oxidation derivative with proteasome modulatory activity. Biochimie 2011;93(5):931-40
    • (2011) Biochimie , vol.93 , Issue.5 , pp. 931-940
    • Bonfili, L.1    Cuccioloni, M.2    Mozzicafreddo, M.3
  • 127
    • 0037455147 scopus 로고    scopus 로고
    • Salinosporamide A: A highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora
    • Feling RH, Buchanan GO, Mincer TJ, et al. Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora. Angew Chem Int Ed 2003;42(3):355-7
    • (2003) Angew Chem Int Ed , vol.42 , Issue.3 , pp. 355-357
    • Feling, R.H.1    Buchanan, G.O.2    Mincer, T.J.3
  • 128
    • 62149103377 scopus 로고    scopus 로고
    • Discovery and development of the anticancer agent salinosporamide A (NPI-0052)
    • Fenical W, Jensen PR, Palladino MA, et al. Discovery and development of the anticancer agent salinosporamide A (NPI-0052). Bioorg Med Chem 2009;17(6):2175-80
    • (2009) Bioorg Med Chem , vol.17 , Issue.6 , pp. 2175-2180
    • Fenical, W.1    Jensen, P.R.2    Ma, P.3
  • 129
    • 77952564354 scopus 로고    scopus 로고
    • From natural product to clinical trials: NPI-0052 (salinosporamide A), a marine actinomycete-derived anticancer agent
    • Buss AD, Butler MS, editors 1st edition. Royal Publishing, Cambridge, UK
    • Lam KS, Lloyd GK, Neuteboom STC, et al. From natural product to clinical trials: NPI-0052 (salinosporamide A), a marine actinomycete-derived anticancer agent. In: Buss AD, Butler MS, editors, Natural products chemistry for drug discovery. 1st edition. Royal Publishing, Cambridge, UK; 2009
    • (2009) Natural Products Chemistry for Drug Discovery
    • Lam, K.S.1    Lloyd, G.K.2    Stc, N.3
  • 130
    • 78650864040 scopus 로고    scopus 로고
    • Bioinspired total Synthesis and human proteasome inhibitory activity of (-)-salinosporamide A,(-)- homosalinosporamide A, and derivatives obtained via organonucleophile promoted bis-cyclizations
    • Nguyen H, Ma G, Gladysheva T, et al. Bioinspired total Synthesis and human proteasome inhibitory activity of (-)-salinosporamide A,(-)- homosalinosporamide A, and derivatives obtained via organonucleophile promoted bis-cyclizations. J Org Chem 2011;76(1):2
    • (2011) J Org Chem , vol.76 , Issue.1 , pp. 2
    • Nguyen, H.1    Ma, G.2    Gladysheva, T.3
  • 131
    • 79953692091 scopus 로고    scopus 로고
    • Mining the cinnabaramide biosynthetic pathway to generate novel proteasome inhibitors
    • Rachid S, Huo L, Herrmann J, et al. Mining the cinnabaramide biosynthetic pathway to generate novel proteasome inhibitors. Chembiochem 2011;12(6):922-31
    • (2011) Chembiochem , vol.12 , Issue.6 , pp. 922-931
    • Rachid, S.1    Huo, L.2    Herrmann, J.3
  • 132
    • 77957991639 scopus 로고    scopus 로고
    • Design Synthesis, and biological evaluation of dibromotyrosine analogues inspired by marine natural products as inhibitors of human prostate cancer proliferation, invasion, and migration
    • Sallam AA, Ramasahayam S, Meyer SA, Sayed KAE. Design, synthesis, and biological evaluation of dibromotyrosine analogues inspired by marine natural products as inhibitors of human prostate cancer proliferation, invasion, and migration. Bioorg Med Chem 2010;18(21):7446-57
    • (2010) Bioorg Med Chem , vol.18 , Issue.21 , pp. 7446-7457
    • Sallam, A.A.1    Ramasahayam, S.2    Meyer, S.A.3    Sayed, K.A.E.4
  • 133
    • 60049083840 scopus 로고    scopus 로고
    • Discovery, design, and synthesis of anti-metastatic lead phenylmethylene hydantoins inspired by marine natural products
    • Mudit M, Khanfar M, Muralidharan A, et al. Discovery, design, and synthesis of anti-metastatic lead phenylmethylene hydantoins inspired by marine natural products. Bioorg Med Chem 2009;17(4):1731-8
    • (2009) Bioorg Med Chem , vol.17 , Issue.4 , pp. 1731-1738
    • Mudit, M.1    Khanfar, M.2    Muralidharan, A.3
  • 134
    • 84887212172 scopus 로고    scopus 로고
    • TMC-95A, B, C, and D, novel proteasome inhibitors produced by apiospora montagnei sacc. TC 1093. Taxonomy, production, isolation, and biological activities
    • Koguchi Y, Kohno J, Nishio M, et al. TMC-95A, B, C, and D, novel proteasome inhibitors produced by apiospora montagnei sacc. TC 1093. Taxonomy, production, isolation, and biological activities. Chem Inform 2000;31(26):no-o
    • (2000) Chem Inform , vol.31
    • Koguchi, Y.1    Kohno, J.2    Nishio, M.3
  • 135
    • 0035902778 scopus 로고    scopus 로고
    • Crystal structure of the 20 S proteasome: TMC-95A complex: A non-covalent proteasome inhibitor
    • Groll M, Koguchi Y, Huber R, Kohno J. Crystal structure of the 20 S proteasome: TMC-95A complex: a non-covalent proteasome inhibitor. J Mol Biol 2001;311(3):543-8
    • (2001) J Mol Biol , vol.311 , Issue.3 , pp. 543-548
    • Groll, M.1    Koguchi, Y.2    Huber, R.3    Kohno, J.4
  • 136
    • 0036462506 scopus 로고    scopus 로고
    • The total synthesis of proteasome inhibitors TMC-95A and TMC-95B: Discovery of a new method to generate cis-propenyl amides
    • Lin S, Danishefsky SJ. The total synthesis of proteasome inhibitors TMC-95A and TMC-95B: discovery of a new method to generate cis-propenyl amides. Angew Chem Int Ed 2002;41(3):512-15
    • (2002) Angew Chem Int Ed , vol.41 , Issue.3 , pp. 512-515
    • Lin, S.1    Danishefsky, S.J.2
  • 138
    • 4344584933 scopus 로고    scopus 로고
    • A concise, total synthesis of the TMC-95A/B proteasome inhibitors
    • Albrecht BK, Williams RM. A concise, total synthesis of the TMC-95A/B proteasome inhibitors. Proc Nat Acad Sci USA 2004;101(33):11949-54
    • (2004) Proc Nat Acad Sci USA , vol.101 , Issue.33 , pp. 11949-11954
    • Albrecht, B.K.1    Williams, R.M.2
  • 139
    • 0036494798 scopus 로고    scopus 로고
    • The core structure of TMC-95A Is a promising lead for reversible proteasome inhibition
    • Kaiser M, Groll M, Renner C, et al. The core structure of TMC-95A Is a promising lead for reversible proteasome inhibition. Angew Chem Int Ed 2002;41(5):780-3
    • (2002) Angew Chem Int Ed , vol.41 , Issue.5 , pp. 780-783
    • Kaiser, M.1    Groll, M.2    Renner, C.3
  • 140
    • 0035906945 scopus 로고    scopus 로고
    • Synthesis of the functionalized macrocyclic core of proteasome inhibitors TMC-95A and B
    • Lin S, Danishefsky SJ. Synthesis of the functionalized macrocyclic core of proteasome inhibitors TMC-95A and B. Angew Chemie Int Ed 2001;40(10):1967-70
    • (2001) Angew Chemie Int Ed , vol.40 , Issue.10 , pp. 1967-1970
    • Lin, S.1    Danishefsky, S.J.2
  • 141
    • 0344235341 scopus 로고    scopus 로고
    • Synthesis of macrocyclic peptide analogues of proteasome inhibitor TMC-95A
    • Berthelot A, Piguel S, Le Dour G, Vidal J. Synthesis of macrocyclic peptide analogues of proteasome inhibitor TMC-95A. J Org Chem 2003;68(25):9835-8
    • (2003) J Org Chem , vol.68 , Issue.25 , pp. 9835-9838
    • Berthelot, A.1    Piguel, S.2    Le Dour, G.3    Vidal, J.4
  • 142
    • 77957656769 scopus 로고    scopus 로고
    • 20S Proteasome Inhibition: Designing Noncovalent Linear Peptide Mimics of the Natural Product TMC-95A
    • Groll M, Gallastegui N, Maréchal X, et al. 20S proteasome inhibition: designing noncovalent linear peptide mimics of the natural product TMC-95A. Chem Med Chem 2010;5(10):1701-5
    • (2010) Chem Med Chem , vol.5 , Issue.10 , pp. 1701-1705
    • Groll, M.1    Gallastegui, N.2    Maréchal, X.3
  • 143
    • 34250806632 scopus 로고    scopus 로고
    • Linear TMC-95-based proteasome inhibitors
    • Basse N, Piguel S, Papapostolou D, et al. Linear TMC-95-based proteasome inhibitors. J Med Chem 2007;50(12):2842-50
    • (2007) J Med Chem , vol.50 , Issue.12 , pp. 2842-2850
    • Basse, N.1    Piguel, S.2    Papapostolou, D.3
  • 144
    • 84860350522 scopus 로고    scopus 로고
    • Noncovalent inhibition of 20S proteasome by pegylated dimerized inhibitors
    • Maréchal X, Pujol A, Richy N, et al. Noncovalent inhibition of 20S proteasome by pegylated dimerized inhibitors. Eur J Med Chem 2012;52:322-7
    • (2012) Eur J Med Chem , vol.52 , pp. 322-327
    • Maréchal, X.1    Pujol, A.2    Richy, N.3
  • 145
    • 33751275548 scopus 로고    scopus 로고
    • A novel anticancer gold (III) dithiocarbamate compound inhibits the activity of a purified 20S proteasome and 26S protea some in human breast cancer cell cultures and xenografts
    • Milacic V, Chen D, Ronconi L, et al. A novel anticancer gold (III) dithiocarbamate compound inhibits the activity of a purified 20S proteasome and 26S protea some in human breast cancer cell cultures and xenografts. Cancer Res 2006;66(21):10478-86
    • (2006) Cancer Res , vol.66 , Issue.21 , pp. 10478-10486
    • Milacic, V.1    Chen, D.2    Ronconi, L.3
  • 146
    • 64449085700 scopus 로고    scopus 로고
    • The tumor proteasome as a novel target for gold (III) complexes: Implications for breast cancer therapy
    • Milacic V, Dou QP. The tumor proteasome as a novel target for gold (III) complexes: implications for breast cancer therapy. Coord Chem Rev 2009;253(11):1649-60
    • (2009) Coord Chem Rev , vol.253 , Issue.11 , pp. 1649-1660
    • Milacic, V.1    Dou, Q.P.2
  • 147
    • 54549114503 scopus 로고    scopus 로고
    • Ni (II), Cu (II), and Zn (II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells
    • Cvek B, Milacic V, Taraba J, Dou QP. Ni (II), Cu (II), and Zn (II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells. J Med Chem 2008;51(20):6256-8
    • (2008) J Med Chem , vol.51 , Issue.20 , pp. 6256-6258
    • Cvek, B.1    Milacic, V.2    Taraba, J.3    Dou, Q.P.4
  • 148
    • 67649969204 scopus 로고    scopus 로고
    • Comparative activities of nickel (II) and zinc (II) complexes of asymmetric [NN O] ligands as 26S proteasome inhibitors
    • Frezza M, Hindo SS, Tomco D, et al. Comparative activities of nickel (II) and zinc (II) complexes of asymmetric [NN O] ligands as 26S proteasome inhibitors. Inorg Chem 2009;48(13):5928-37
    • (2009) Inorg Chem , vol.48 , Issue.13 , pp. 5928-5937
    • Frezza, M.1    Hindo, S.S.2    Tomco, D.3
  • 149
    • 84901648175 scopus 로고    scopus 로고
    • Clioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells
    • R908
    • Daniel KG, Chen D, Orlu S, et al. Clioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells. Breast Cancer Res 2005;7(6):R897-908
    • (2005) Breast Cancer Res , vol.7 , Issue.6
    • Daniel, K.G.1    Chen, D.2    Orlu, S.3
  • 150
    • 73949101373 scopus 로고    scopus 로고
    • Novel 8-hydroxylquinoline analogs induce copper-dependent proteasome inhibition and cell death in human breast cancer cells
    • Milacic V, Jiao P, Zhang B, et al. Novel 8-hydroxylquinoline analogs induce copper-dependent proteasome inhibition and cell death in human breast cancer cells. Int J Oncol 2009;35(6):1481-91
    • (2009) Int J Oncol , vol.35 , Issue.6 , pp. 1481-1491
    • Milacic, V.1    Jiao, P.2    Zhang, B.3
  • 151
    • 70349911835 scopus 로고    scopus 로고
    • Metals in anticancer therapy: Copper (II) complexes as inhibitors of the 20S proteasome
    • Hindo SS, Frezza M, Tomco D, et al. Metals in anticancer therapy: copper (II) complexes as inhibitors of the 20S proteasome. Eur J Med Chem 2009;44(11):4353-61
    • (2009) Eur J Med Chem , vol.44 , Issue.11 , pp. 4353-4361
    • Hindo, S.S.1    Frezza, M.2    Tomco, D.3
  • 152
    • 84868486281 scopus 로고    scopus 로고
    • Cellular and computational studies of proteasome inhibition and apoptosis induction in human cancer cells by amino acid schiff base-copper complexes
    • Zuo J, Bi C, Fan Y, et al. Cellular and computational studies of proteasome inhibition and apoptosis induction in human cancer cells by amino acid schiff base-copper complexes. J Inorg Biochem 2013;118:83-93
    • (2013) J Inorg Biochem , vol.118 , pp. 83-93
    • Zuo, J.1    Bi, C.2    Fan, Y.3
  • 153
    • 34548050479 scopus 로고    scopus 로고
    • A gold (I) phosphine complex selectively induces apoptosis in breast cancer cells: Implications for anticancer therapeutics targeted to mitochondria
    • Rackham O, Nichols SJ, Leedman PJ, et al. A gold (I) phosphine complex selectively induces apoptosis in breast cancer cells: implications for anticancer therapeutics targeted to mitochondria. Biochem Pharmacol 2007;74(7):992-1002
    • (2007) Biochem Pharmacol , vol.74 , Issue.7 , pp. 992-1002
    • Rackham, O.1    Nichols, S.J.2    Leedman, P.J.3
  • 154
    • 0037036523 scopus 로고    scopus 로고
    • Concentrations of Fe,Cu and Zn in breast tissue: A synchrotron XRF study
    • Geraki K, Farquharson M, Bradley D. Concentrations of Fe, Cu and Zn in breast tissue: a synchrotron XRF study. Phys Med Biol 2002;47(13):2327
    • (2002) Phys Med Biol , vol.47 , Issue.13 , pp. 2327
    • Geraki, K.1    Farquharson, M.2    Bradley, D.3
  • 155
    • 0037222751 scopus 로고    scopus 로고
    • Copper and ceruloplasmin status in serum of prostate and colon cancer patients
    • Nayak SB, Bhat VR, Upadhyay D, Udupa SL. Copper and ceruloplasmin status in serum of prostate and colon cancer patients. Indian J Physiol Pharmacol 2003;47(1):108-10
    • (2003) Indian J Physiol Pharmacol , vol.47 , Issue.1 , pp. 108-110
    • Nayak, S.B.1    Bhat, V.R.2    Upadhyay, D.3    Udupa, S.L.4
  • 156
    • 0024356579 scopus 로고
    • Serum and tissue trace metal levels in lung cancer
    • Diez M, Arroyo M, Cerdan F, et al. Serum and tissue trace metal levels in lung cancer. Oncology 1989;46(4):230-4
    • (1989) Oncology , vol.46 , Issue.4 , pp. 230-234
    • Diez, M.1    Arroyo, M.2    Cerdan, F.3
  • 157
    • 0027448830 scopus 로고
    • Quantitative analysis of copper, zinc and copper/zinc ratio in selected human brain tumors
    • Yoshida D, Ikeda Y, Nakazawa S. Quantitative analysis of copper, zinc and copper/zinc ratio in selected human brain tumors. J Neurooncol 1993;16(2):109-15
    • (1993) J Neurooncol , vol.16 , Issue.2 , pp. 109-115
    • Yoshida, D.1    Ikeda, Y.2    Nakazawa, S.3
  • 158
    • 77951688202 scopus 로고    scopus 로고
    • Antiplasmodial thiostrepton derivatives: Proteasome inhibitors with a dual mode of action
    • Schoof S, Pradel G, Aminake MN, et al. Antiplasmodial thiostrepton derivatives: proteasome inhibitors with a dual mode of action. Angew Chem Int Ed 2010;49(19):3317-21
    • (2010) Angew Chem Int Ed , vol.49 , Issue.19 , pp. 3317-3321
    • Schoof, S.1    Pradel, G.2    Aminake, M.N.3
  • 159
    • 0029928912 scopus 로고    scopus 로고
    • Betulinic acid and dihydrobetulinic acid derivatives as potent anti-HIV agents
    • Kashiwada Y, Hashimoto F, Cosentino LM, et al. Betulinic acid and dihydrobetulinic acid derivatives as potent anti-HIV agents. J Med Chem 1996;39(5):1016
    • (1996) J Med Chem , vol.39 , Issue.5 , pp. 1016
    • Kashiwada, Y.1    Hashimoto, F.2    Cosentino, L.M.3
  • 160
    • 84865763587 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome pathway by methyl N-(6-Phenylsulfanyl-1Hbenzimidazol- 2-yl) carbamate leads to a potent cytotoxic effect in tumor cells A novel antiproliferative agent with a potential therapeutic implication
    • Dogra N, Mukhopadhyay T. Impairment of the ubiquitin-proteasome pathway by methyl N-(6-Phenylsulfanyl-1Hbenzimidazol- 2-yl) carbamate leads to a potent cytotoxic effect in tumor cells A novel antiproliferative agent with a potential therapeutic implication. J Biol Chem 2012;287(36):30625-40
    • (2012) J Biol Chem , vol.287 , Issue.36 , pp. 30625-30640
    • Dogra, N.1    Mukhopadhyay, T.2
  • 161
    • 84863490720 scopus 로고    scopus 로고
    • Cationic porphyrins are reversible proteasome inhibitors
    • Santoro AM, Lo Giudice MC, Durso A, et al. Cationic porphyrins are reversible proteasome inhibitors. J Am Chem Soc 2012;134(25):10451-7
    • (2012) J Am Chem Soc , vol.134 , Issue.25 , pp. 10451-10457
    • Santoro, A.M.1    Lo Giudice, M.C.2    Durso, A.3
  • 162
    • 36749000794 scopus 로고    scopus 로고
    • Malaria chemotherapeutics part I: History of antimalarial drug development, currently used therapeutics, and drugs in clinical development
    • Schlitzer M. Malaria chemotherapeutics part I: history of antimalarial drug development, currently used therapeutics, and drugs in clinical development. Chem Med Chem 2007;2(7):944-86
    • (2007) Chem Med Chem , vol.2 , Issue.7 , pp. 944-986
    • Schlitzer, M.1
  • 163
    • 0019554974 scopus 로고
    • Clinical evaluation of Panolog Cream used to treat canine and feline dermatoses
    • Nesbitt G, Fox P. Clinical evaluation of Panolog Cream used to treat canine and feline dermatoses. Vet Med Small Anim Clin 1981;76(4):535
    • (1981) Vet Med Small Anim Clin , vol.76 , Issue.4 , pp. 535
    • Nesbitt, G.1    Fox, P.2
  • 164
    • 0031030313 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum protein synthesis
    • McConkey GA, Rogers MJ, McCutchan TF. Inhibition of Plasmodium falciparum protein synthesis. J Biol Chem 1997;272(4):2046-9
    • (1997) J Biol Chem , vol.272 , Issue.4 , pp. 2046-2049
    • McConkey, G.A.1    Rogers, M.J.2    McCutchan, T.F.3
  • 165
    • 0039730001 scopus 로고    scopus 로고
    • How an inhibitor of the HIV-I protease modulates proteasome activity
    • Schmidtke G, Holzhutter HG, Bogyo M, et al. How an inhibitor of the HIV-I protease modulates proteasome activity. J Biol Chem 1999;274(50):35734-40
    • (1999) J Biol Chem , vol.274 , Issue.50 , pp. 35734-35740
    • Schmidtke, G.1    Holzhutter, H.G.2    Bogyo, M.3
  • 166
    • 0035087062 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus activity of YK-FH312 (a betulinic acid derivative), a novel compound blocking viral maturation
    • Kanamoto T, Kashiwada Y, Kanbara K, et al. Anti-human immunodeficiency virus activity of YK-FH312 (a betulinic acid derivative), a novel compound blocking viral maturation. Antimicrob Agents Chemother 2001;45(4):1225-30
    • (2001) Antimicrob Agents Chemother , vol.45 , Issue.4 , pp. 1225-1230
    • Kanamoto, T.1    Kashiwada, Y.2    Kanbara, K.3
  • 167
    • 80052566948 scopus 로고    scopus 로고
    • New betulinic acid derivatives as potent proteasome inhibitors
    • Qian K, Kim SY, Hung HY, et al. New betulinic acid derivatives as potent proteasome inhibitors. Bioorg Med Chem Lett 2011;21(19):5944-7
    • (2011) Bioorg Med Chem Lett , vol.21 , Issue.19 , pp. 5944-5947
    • Qian, K.1    Kim, S.Y.2    Hung, H.Y.3
  • 168
    • 0033710443 scopus 로고    scopus 로고
    • Echinococcosis: An emerging or re-emerging zoonosis?
    • Eckert J, Conraths F, Tackmann K, et al. Echinococcosis: an emerging or re-emerging zoonosis? Int J Parasitol 2000;30(12):1283-94
    • (2000) Int J Parasitol , vol.30 , Issue.12 , pp. 1283-1294
    • Eckert, J.1    Conraths, F.2    Tackmann, K.3
  • 169
    • 0028049132 scopus 로고
    • Effect of chemotherapy on the larval mass and the long-term course of alveolar echinococcosis
    • Ammann RW, Ilitsch N, Marincek B, Freiburghaus AU. Effect of chemotherapy on the larval mass and the long-term course of alveolar echinococcosis. Hepatology 1994;19(3):735-42
    • (1994) Hepatology , vol.19 , Issue.3 , pp. 735-742
    • Ammann, R.W.1    Ilitsch, N.2    Marincek, B.3    Freiburghaus, A.U.4
  • 170
    • 0020261057 scopus 로고
    • Treatment of human echinococcosis with mebendazole. Preliminary observations in 28 patients
    • Muller E, Akovbiantz A, Ammann R, et al. Treatment of human echinococcosis with mebendazole. Preliminary observations in 28 patients. Hepatogastroenterology 1982;29(6):236
    • (1982) Hepatogastroenterology , vol.29 , Issue.6 , pp. 236
    • Muller, E.1    Akovbiantz, A.2    Ammann, R.3
  • 173
    • 11144224746 scopus 로고    scopus 로고
    • Disulfiram facilitates intracellular Cu uptake and induces apoptosis in human melanoma cells
    • Cen D, Brayton D, Shahandeh B, et al. Disulfiram facilitates intracellular Cu uptake and induces apoptosis in human melanoma cells. J Med Chem 2004;47(27):6914-20
    • (2004) J Med Chem , vol.47 , Issue.27 , pp. 6914-6920
    • Cen, D.1    Brayton, D.2    Shahandeh, B.3
  • 174
    • 33751285781 scopus 로고    scopus 로고
    • Disulfiram, a clinically used anti-alcoholism drug and copper-binding agent, induces apoptotic cell death in breast cancer cultures and xenografts via inhibition of the proteasome activity
    • Chen D, Cui QC, Yang H, Dou QP. Disulfiram, a clinically used anti-alcoholism drug and copper-binding agent, induces apoptotic cell death in breast cancer cultures and xenografts via inhibition of the proteasome activity. Cancer Res 2006;66(21):10425-33
    • (2006) Cancer Res , vol.66 , Issue.21 , pp. 10425-10433
    • Chen, D.1    Cui, Q.C.2    Yang, H.3    Dou, Q.P.4
  • 175
    • 84865563465 scopus 로고    scopus 로고
    • Disulfiram, an old drug with new potential therapeutic uses for human hematological malignancies
    • Conticello C, Martinetti D, Adamo L, et al. Disulfiram, an old drug with new potential therapeutic uses for human hematological malignancies. Int J Cancer 2012;31(9):2197-203
    • (2012) Int J Cancer , vol.31 , Issue.9 , pp. 2197-2203
    • Conticello, C.1    Martinetti, D.2    Adamo, L.3
  • 176
    • 84869141941 scopus 로고    scopus 로고
    • Drug repurposing: Far beyond new targets for old drugs
    • Oprea T, Mestres J. Drug repurposing: far beyond new targets for old drugs. AAPS J 2012;14:1-5
    • (2012) AAPS J , Issue.14 , pp. 1-5
    • Oprea, T.1    Mestres, J.2
  • 177
    • 45849099115 scopus 로고    scopus 로고
    • Argyrin A reveals a critical role for the tumor suppressor protein p27(kip1) in mediating antitumor activities in response to proteasome inhibition
    • Nickeleit I, Zender S, Sasse F, et al. Argyrin A reveals a critical role for the tumor suppressor protein p27(kip1) in mediating antitumor activities in response to proteasome inhibition. Cancer Cell 2008;14(1):23-35
    • (2008) Cancer Cell , vol.14 , Issue.1 , pp. 23-35
    • Nickeleit, I.1    Zender, S.2    Sasse, F.3
  • 178
    • 77953086957 scopus 로고    scopus 로고
    • Synthesis and biological ucharacterization of argyrin
    • Bulow L, Nickeleit I, Girbig AK, et al. Synthesis and biological ucharacterization of argyrin F. ChemMedChem 2010;5(6):832-6
    • (2010) F. ChemMedChem , vol.5 , Issue.6 , pp. 832-836
    • Bulow, L.1    Nickeleit, I.2    Girbig, A.K.3
  • 179
    • 79953014673 scopus 로고    scopus 로고
    • Elucidation of the structure and intermolecular interactions of a reversible cyclic-peptide inhibitor of the proteasome by NMR spectroscopy and molecular modeling
    • Stauch B, Simon B, Basile T, et al. Elucidation of the structure and intermolecular interactions of a reversible cyclic-peptide inhibitor of the proteasome by NMR spectroscopy and molecular modeling. Angew Chem 2010;122(23):4026-30
    • (2010) Angew Chem , vol.122 , Issue.23 , pp. 4026-4030
    • Stauch, B.1    Simon, B.2    Basile, T.3
  • 180
    • 77956300868 scopus 로고    scopus 로고
    • A, b-unsaturated N-acylpyrrole peptidyl derivatives: New proteasome inhibitors
    • Baldisserotto A, Ferretti V, Destro F, et al. a, b-unsaturated N-acylpyrrole peptidyl derivatives: new proteasome inhibitors. J Med Chem 2010;53(17):6511-15
    • (2010) J Med Chem , vol.53 , Issue.17 , pp. 6511-6515
    • Baldisserotto, A.1    Ferretti, V.2    Destro, F.3
  • 181
    • 44749093175 scopus 로고    scopus 로고
    • Curcumin: From ancient medicine to current clinical trials
    • Hatcher H, Planalp R, Cho J, et al. Curcumin: from ancient medicine to current clinical trials. Cell Mol Life Sci 2008;65(11):1631-52
    • (2008) Cell Mol Life Sci , vol.65 , Issue.11 , pp. 1631-1652
    • Hatcher, H.1    Planalp, R.2    Cho, J.3
  • 182
    • 84934444192 scopus 로고    scopus 로고
    • Curcumin: The Indian solid gold. The molecular targets and therapeutic uses of curcumin in health and disease
    • Aggarwal BB, Sundaram C, Malani N, Ichikawa H. Curcumin: the Indian solid gold. The molecular targets and therapeutic uses of curcumin in health and disease. Adv Exp Med Biol 2007;595:1-75
    • (2007) Adv Exp Med Biol , vol.595 , pp. 1-75
    • Aggarwal, B.B.1    Sundaram, C.2    Malani, N.3    Ichikawa, H.4
  • 183
    • 33847610748 scopus 로고    scopus 로고
    • The proteasome as a potential target for novel anticancer drugs and chemosensitizers
    • Landis-Piwowar KR, Milacic V, Chen D, et al. The proteasome as a potential target for novel anticancer drugs and chemosensitizers. Drug Resist Updat 2006;9(6):263-73
    • (2006) Drug Resist Updat , vol.9 , Issue.6 , pp. 263-273
    • Landis-Piwowar, K.R.1    Milacic, V.2    Chen, D.3
  • 184
    • 77957882350 scopus 로고    scopus 로고
    • Evaluation of curcumin acetates and amino acid conjugates as proteasome inhibitors
    • Wan SB, Yang H, Zhou Z, et al. Evaluation of curcumin acetates and amino acid conjugates as proteasome inhibitors. Int J Mol Med 2010;26(4):447
    • (2010) Int J Mol Med , vol.26 , Issue.4 , pp. 447
    • Wan, S.B.1    Yang, H.2    Zhou, Z.3
  • 185
    • 78650188894 scopus 로고    scopus 로고
    • Scytonemides A and B, cyclic peptides with 20S proteasome inhibitory
    • Krunic A, Vallat A, Mo S, et al. Scytonemides A and B, cyclic peptides with 20S proteasome inhibitory activity from the cultured cyanobacterium Scytonema hofmanii. J Nat Prod 2010;73(11):1927
    • (2010) J Nat Prod , vol.73 , Issue.11 , pp. 1927
    • Krunic, A.1    Vallat, A.2    Mo, S.3
  • 186
    • 47349101944 scopus 로고    scopus 로고
    • Synthesis and proteasome inhibition of glycyrrhetinic acid derivatives
    • Huang L, Yu D, Ho P, et al. Synthesis and proteasome inhibition of glycyrrhetinic acid derivatives. Bioorg Med Chem Lett 2008;16(14):6696-701
    • (2008) Bioorg Med Chem Lett , vol.16 , Issue.14 , pp. 6696-6701
    • Huang, L.1    Yu, D.2    Ho, P.3
  • 187
    • 34948849213 scopus 로고    scopus 로고
    • Activation and inhibition of the proteasome by betulinic acid and its derivatives
    • Huang L, Ho P, Chen CH. Activation and inhibition of the proteasome by betulinic acid and its derivatives. FEBS Lett 2007;581(25):4955-9
    • (2007) FEBS Lett , vol.581 , Issue.25 , pp. 4955-4959
    • Huang, L.1    Ho, P.2    Chen, C.H.3
  • 188
    • 79952485141 scopus 로고    scopus 로고
    • Synthesis and proteasome inhibition of lithocholic acid derivatives
    • Dang Z, Lin A, Ho P, et al. Synthesis and proteasome inhibition of lithocholic acid derivatives. Bioorg Med Chem Lett 2011;21(7):1926-1928
    • (2011) Bioorg Med Chem Lett , vol.21 , Issue.7 , pp. 1926-1928
    • Dang, Z.1    Lin, A.2    Ho, P.3
  • 189
    • 84861539859 scopus 로고    scopus 로고
    • Palauamine and related oroidin alkaloids dibromophakellin and dibromophakellstatin inhibit the human 20s proteasome
    • Lansdell TA, Hewlett NM, Skoumbourdis AP, et al. Palauamine and related oroidin alkaloids dibromophakellin and dibromophakellstatin inhibit the human 20s proteasome. J Nat Prod 2012;75(5):980-5
    • (2012) J Nat Prod , vol.75 , Issue.5 , pp. 980-985
    • Lansdell, T.A.1    Hewlett, N.M.2    Skoumbourdis, A.P.3
  • 190
    • 84860458560 scopus 로고    scopus 로고
    • Serendipity in discovery of proteasome inhibitors
    • Dunn D, Iqbal M, Husten J, et al. Serendipity in discovery of proteasome inhibitors. Bioorg Med Chem Lett 2012;22:3503-5
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 3503-3505
    • Dunn, D.1    Iqbal, M.2    Husten, J.3
  • 191
    • 0032940438 scopus 로고    scopus 로고
    • Effects of petrosaspongiolide M, a novel phospholipase A2 inhibitor, on acute and chronic inflammation
    • Garcia-Pastor P, Randazzo A, Gomez-Paloma L, et al. Effects of petrosaspongiolide M, a novel phospholipase A2 inhibitor, on acute and chronic inflammation. J Pharmacol Exp Ther 1999;289(1):166-72
    • (1999) J Pharmacol Exp Ther , vol.289 , Issue.1 , pp. 166-172
    • Garcia-Pastor, P.1    Randazzo, A.2    Gomez-Paloma, L.3
  • 192
    • 77952968118 scopus 로고    scopus 로고
    • Chemical proteomics discloses petrosapongiolide M an antiinflammatory marine sesterterpene as a proteasome inhibitor
    • Margarucci L, Monti MC, Tosco A, et al. Chemical proteomics discloses petrosapongiolide M, an antiinflammatory marine sesterterpene, as a proteasome inhibitor. Angew Chem Int Ed 2010;49(23):3960-3
    • (2010) Angew Chem Int Ed , vol.49 , Issue.23 , pp. 3960-3963
    • Margarucci, L.1    Monti, M.C.2    Tosco, A.3
  • 193
    • 84860253988 scopus 로고    scopus 로고
    • Modulation of proteasome machinery by natural and synthetic analogues of the marine bioactive compound petrosaspongiolide
    • Margarucci L, Tosco A, De Simone R, et al. Modulation of proteasome machinery by natural and synthetic analogues of the marine bioactive compound petrosaspongiolide m. ChemBioChem 2012;13(7):982-6
    • (2012) M. ChemBioChem , vol.13 , Issue.7 , pp. 982-986
    • Margarucci, L.1    Tosco, A.2    De Simone, R.3
  • 194
    • 27644518292 scopus 로고    scopus 로고
    • Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates
    • Kisselev AF, Goldberg AL. Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates. Methods Enzymol 2005;398:364-78
    • (2005) Methods Enzymol , vol.398 , pp. 364-378
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 195
    • 0036896223 scopus 로고    scopus 로고
    • Antitumor effect of the human immunodeficiency virus protease inhibitor ritonavir induction of tumor-cell apoptosis associated with perturbation of proteasomal proteolysis
    • Gaedicke S, Firat-Geier E, Constantiniu O, et al. Antitumor effect of the human immunodeficiency virus protease inhibitor ritonavir induction of tumor-cell apoptosis associated with perturbation of proteasomal proteolysis. Cancer Res 2002;62(23):6901-8
    • (2002) Cancer Res , vol.62 , Issue.23 , pp. 6901-6908
    • Gaedicke, S.1    Firat-Geier, E.2    Constantiniu, O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.