메뉴 건너뛰기




Volumn 11, Issue 23, 2011, Pages 2931-2944

Progress of computer-aided drug design (CADD) of proteasome inhibitors

Author keywords

Computer aided drug design; Proteasome inhibitor; Rational drug design

Indexed keywords

APIGENIN; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORONIC ACID DERIVATIVE; BORTEZOMIB; ELLAGIC ACID; GALLIC ACID; GENISTEIN; GREEN TEA EXTRACT; KAEMPFEROL; LUTEOLIN; MYRICETIN; PROTEASOME INHIBITOR; QUERCETIN; RESVERATROL; STATINE 1; STATINE 2; THREONINE PROTEINASE INHIBITOR; TP 101; TP 102; TP 103; TP 104; TP 105; TP 106; TP 107; TP 108; TP 109; TP 110; TP 111; TYROPEPTIN A; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 83455203249     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/156802611798281366     Document Type: Article
Times cited : (5)

References (96)
  • 1
    • 0028307114 scopus 로고
    • Protein structure-based drug design
    • Whittle, P.; Blundell, T. Protein structure-based drug design. Annu. Rev. Bioph. Biom., 1994, 23, 349-375.
    • (1994) Annu. Rev. Bioph. Biom , vol.23 , pp. 349-375
    • Whittle, P.1    Blundell, T.2
  • 2
    • 0042353897 scopus 로고    scopus 로고
    • Molecular recognition and docking algorithms
    • Brooijmans, N.; Kuntz, I. D. Molecular recognition and docking algorithms. Annu. Rev. Bioph. Biom., 2003, 32, 335-373.
    • (2003) Annu. Rev. Bioph. Biom , vol.32 , pp. 335-373
    • Brooijmans, N.1    Kuntz, I.D.2
  • 3
    • 0000238901 scopus 로고
    • QSAR studies on enzyme inhibitors
    • Gupta, S. P. QSAR studies on enzyme inhibitors. Chem. Rev., 1987, 87, 1183-1253.
    • (1987) Chem. Rev , vol.87 , pp. 1183-1253
    • Gupta, S.P.1
  • 4
    • 8544274635 scopus 로고
    • QSAR in design of bioactive compounds
    • Gupta, S. P.; Scient, J. QSAR in design of bioactive compounds. Indus. Res., 1991, 50, 301-310.
    • (1991) Indus. Res , vol.50 , pp. 301-310
    • Gupta, S.P.1    Scient, J.2
  • 5
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • Ciechanover, A.; Orian, A.; Schwartz, A. L. Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays, 2000, 22, 442-451.
    • (2000) Bioessays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 6
    • 0036395180 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis: Its role in human diseases and the design of therapeutic strategies
    • Sakamoto, K. M. Ubiquitin-dependent proteolysis: its role in human diseases and the design of therapeutic strategies. Mol. Genet. Metab., 2002, 77, 44-56.
    • (2002) Mol. Genet. Metab , vol.77 , pp. 44-56
    • Sakamoto, K.M.1
  • 7
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev, A. F.; Goldberg, A. L. Proteasome inhibitors: from research tools to drug candidates. Chem. Biol., 2001, 8, 739-758.
    • (2001) Chem. Biol , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 8
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O.; Tanaka, K.; Goldberg, A. L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem., 1996, 65, 801-847.
    • (1996) Annu. Rev. Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 9
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: Cell biological roles of proteasome activators and inhibitors
    • Rechsteiner, M.; Hill, C. P. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. TRENDS Cell Biol., 2005, 15, 27-33.
    • (2005) TRENDS Cell Biol , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 10
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged protein
    • Goldberg, A. L. Protein degradation and protection against misfolded or damaged proteins. Nature, 2003, 426, 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 11
    • 33646523185 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system: Focus on the heart
    • Zolk, O.; Schenke, C.; Sarikas, A. The ubiquitin-proteasome system: focus on the heart. Cardiovasc. Res., 2006, 70, 410-421.
    • (2006) Cardiovasc. Res , vol.70 , pp. 410-421
    • Zolk, O.1    Schenke, C.2    Sarikas, A.3
  • 13
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet., 1996, 30, 405-439.
    • (1996) Annu. Rev. Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 14
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe, J.; Stock, D.; Jap, B.; Zwickl, P.; Baumeister, W.; Huber, R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science, 1995, 268, 533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 18
    • 0030726159 scopus 로고    scopus 로고
    • Protein translocation channels in the proteasome and other proteases
    • Larsen, C. N.; Finley, D. Protein translocation channels in the proteasome and other proteases. Cell, 1997, 91, 431-434.
    • (1997) Cell , vol.91 , pp. 431-434
    • Larsen, C.N.1    Finley, D.2
  • 19
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W.; Walz, J.; Zühl, F.; Seemüller, E. The proteasome: paradigm of a self-compartmentalizing protease. Cell, 1998, 92, 367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 20
    • 0035290730 scopus 로고    scopus 로고
    • Antigen processing by the proteasome
    • Kloetzel, P. M. Antigen processing by the proteasome. Nat. Rev. Mol. Cell Biol., 2001, 2, 179-187.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 179-187
    • Kloetzel, P.M.1
  • 21
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I- presented peptides
    • Rock, A. L.; Goldberg, K. L. Degradation of cell proteins and the generation of MHC class I- presented peptides. Annu. Rev. Immunol., 1999, 17, 739-779.
    • (1999) Annu. Rev. Immunol , vol.17 , pp. 739-779
    • Rock, A.L.1    Goldberg, K.L.2
  • 22
    • 0028830664 scopus 로고
    • Association of LMP2 and LMP7 genes within the major histocompatibility complex with insulin-dependent diabetes mellitus: Population family studies
    • Deng, G. Y.; Muir, A.; Maclaren, N. K.; She, J. X. Association of LMP2 and LMP7 genes within the major histocompatibility complex with insulin-dependent diabetes mellitus: Population family studies. Am. J. Hum. Genet., 1995, 56, 528-534.
    • (1995) Am. J. Hum. Genet , vol.56 , pp. 528-534
    • Deng, G.Y.1    Muir, A.2    Maclaren, N.K.3    She, J.X.4
  • 26
    • 33144469102 scopus 로고    scopus 로고
    • The proteasome and proteasome inhibitors in cancer therapy
    • Voorhees, P. M.; Orlowski, R. Z. The proteasome and proteasome inhibitors in cancer therapy. Annu. Rev. Pharmacol. Toxicol., 2006, 46, 189-213.
    • (2006) Annu. Rev. Pharmacol. Toxicol , vol.46 , pp. 189-213
    • Voorhees, P.M.1    Orlowski, R.Z.2
  • 27
    • 3242754268 scopus 로고    scopus 로고
    • Genes of the LMP/TAP cluster are associated with the human autoimmune disease vitiligo
    • Casp, C. B.; She, J. X.; McCormack, W. T. Genes of the LMP/TAP cluster are associated with the human autoimmune disease vitiligo. Genes. Immun., 2003, 4, 492-499.
    • (2003) Genes. Immun , vol.4 , pp. 492-499
    • Casp, C.B.1    She, J.X.2    McCormack, W.T.3
  • 28
    • 0037277661 scopus 로고    scopus 로고
    • Proteasome inhibitors as therapeutic agents: Current and future strategies
    • Delcros, J. G.; Baudy Floc'h, M.; Prigent, C.; Arlot-Bonnemains, Y. Proteasome inhibitors as therapeutic agents: current and future strategies. Curr. Med. Chem., 2003, 10, 479-503.
    • (2003) Curr. Med. Chem , vol.10 , pp. 479-503
    • Delcros, J.G.1    Baudy, F.M.2    Prigent, C.3    Arlot-Bonnemains, Y.4
  • 29
    • 27844536479 scopus 로고    scopus 로고
    • Towards immunoproteasomespecific inhibitors: An improved synthesis of dihydroeponemycin
    • Ho, A.; Cyrus, K.; Kim, K. B. Towards immunoproteasomespecific inhibitors: an improved synthesis of dihydroeponemycin. Eur. J. Org. Chem., 2005, 4829-4834.
    • (2005) Eur. J. Org. Chem , pp. 4829-4834
    • Ho, A.1    Cyrus, K.2    Kim, K.B.3
  • 30
    • 66549099025 scopus 로고    scopus 로고
    • Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors
    • Kuhn, D. J.; Hunsucker, S. A.; Chen, Q.; Voorhees, P. M.; Orlowski, M.; Orlowski, R. Z. Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors. Blood, 2009, 113, 4667-4676.
    • (2009) Blood , vol.113 , pp. 4667-4676
    • Kuhn, D.J.1    Hunsucker, S.A.2    Chen, Q.3    Voorhees, P.M.4    Orlowski, M.5    Orlowski, R.Z.6
  • 31
    • 33845872810 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate inhibits induction of immunoproteasome and decreases survival in a rat model of amyotrophic lateral sclerosis
    • Ahtoniemi, T.; Goldsteins, G.; Keksa-Goldsteine, V.; Malm, T.; Kanninen, K.; Salminen, A.; Koistinaho, J. Pyrrolidine dithiocarbamate inhibits induction of immunoproteasome and decreases survival in a rat model of amyotrophic lateral sclerosis. Mol. Pharmacol., 2007, 71, 30-37.
    • (2007) Mol. Pharmacol , vol.71 , pp. 30-37
    • Ahtoniemi, T.1    Goldsteins, G.2    Keksa-Goldsteine, V.3    Malm, T.4    Kanninen, K.5    Salminen, A.6    Koistinaho, J.7
  • 33
    • 32844455767 scopus 로고    scopus 로고
    • Targeting the proteasome as a therapeutic strategy against hematological malignancies
    • Orlowski, R. Z.; Zeger, E. L. Targeting the proteasome as a therapeutic strategy against hematological malignancies. Expert Opin. Invest. Drugs, 2006, 15, 117-130.
    • (2006) Expert Opin. Invest. Drugs , vol.15 , pp. 117-130
    • Orlowski, R.Z.1    Zeger, E.L.2
  • 34
    • 85038456208 scopus 로고    scopus 로고
    • Thomson-pharma Database, Accessed December 2009
    • Thomson-pharma Database. https://www.thomson-pharma.com/ [Accessed December 2009].
  • 35
    • 13844320703 scopus 로고    scopus 로고
    • Proteasome inhibition in multiple myeloma: Therapeutic implication
    • Chauhan, D.; Hideshima, T.; Anderson, K. C. Proteasome inhibition in multiple myeloma: therapeutic implication. Annu. Rev. Pharmacol. Toxicol., 2005, 45, 465-476.
    • (2005) Annu. Rev. Pharmacol. Toxicol , vol.45 , pp. 465-476
    • Chauhan, D.1    Hideshima, T.2    Anderson, K.C.3
  • 37
    • 0035207077 scopus 로고    scopus 로고
    • A population based case-control study of lung cancer and green tea consumption among women living in Shanghai, China
    • Zhong, L.; Goldberg, M. S.; Gao, Y. T.; Hanley, J. A.; Parent, M. E.; Jin, F. A population based case-control study of lung cancer and green tea consumption among women living in Shanghai, China. Epidemiology, 2001, 12, 695-700.
    • (2001) Epidemiology , vol.12 , pp. 695-700
    • Zhong, L.1    Goldberg, M.S.2    Gao, Y.T.3    Hanley, J.A.4    Parent, M.E.5    Jin, F.6
  • 39
    • 0035954244 scopus 로고    scopus 로고
    • Regular consumption of green tea and the risk of breast cancer recurrence: Follow-up study from the Hospital-based Epidemiologic Research Program at Aichi Cancer Center (HERPACC), Japan
    • Inoue, M.; Tajima, K.; Mizutani, M.; Iwata, H.; Iwase, T.; Miura, S.; Hirose, K.; Hamajima, N.; Tominaga, S. Regular consumption of green tea and the risk of breast cancer recurrence: follow-up study from the Hospital-based Epidemiologic Research Program at Aichi Cancer Center (HERPACC), Japan. Cancer Lett., 2001, 167, 175-182.
    • (2001) Cancer Lett , vol.167 , pp. 175-182
    • Inoue, M.1    Tajima, K.2    Mizutani, M.3    Iwata, H.4    Iwase, T.5    Miura, S.6    Hirose, K.7    Hamajima, N.8    Tominaga, S.9
  • 40
    • 0026760907 scopus 로고
    • Effect of (-)-epigallocatechin gallate, the main constituent of green tea, on lung metastasis with mouse B16 melanoma cell lines
    • Taniguchi, S.; Fujiki, H.; Kobayashi, H.; Go, H.; Miyado, K.; Sadano, H.; Shimokawa, R. Effect of (-)-epigallocatechin gallate, the main constituent of green tea, on lung metastasis with mouse B16 melanoma cell lines. Cancer Lett., 1992, 65, 51-54.
    • (1992) Cancer Lett , vol.65 , pp. 51-54
    • Taniguchi, S.1    Fujiki, H.2    Kobayashi, H.3    Go, H.4    Miyado, K.5    Sadano, H.6    Shimokawa, R.7
  • 42
    • 0029124096 scopus 로고
    • Growth inhibition and regression of human prostate and breast tumors in athymic mice by tea epigallocatechin gallate
    • Liao, S.; Umekita, Y.; Guo, J.; Kokontis, J. M.; Hiipakka, R. A. Growth inhibition and regression of human prostate and breast tumors in athymic mice by tea epigallocatechin gallate. Cancer Lett., 1995, 96, 239-243.
    • (1995) Cancer Lett , vol.96 , pp. 239-243
    • Liao, S.1    Umekita, Y.2    Guo, J.3    Kokontis, J.M.4    Hiipakka, R.A.5
  • 43
    • 0033135024 scopus 로고    scopus 로고
    • Prostate cancer chemoprevention by green tea: In vitro and in vivo inhibition of testosterone- mediated induction of ornithine decarboxylase
    • Gupta, S.; Ahmad, N.; Mohan, R. R.; Husain, M. M; Mukhtar, H. Prostate cancer chemoprevention by green tea: in vitro and in vivo inhibition of testosterone- mediated induction of ornithine decarboxylase. Cancer Res., 1999, 59, 2115-2120.
    • (1999) Cancer Res , vol.59 , pp. 2115-2120
    • Gupta, S.1    Ahmad, N.2    Mohan, R.R.3    Husain, M.M.4    Mukhtar, H.5
  • 44
    • 0033065391 scopus 로고    scopus 로고
    • Inhibition of benzo[a]pyrene-induced mutagenesis by (-)-epigallocatechin gallate in the lung of rpsL transgenic mice
    • Muto, S.; Yokoi, T.; Gondo, Y.; Katsuki, M.; Shioyama, Y.; Fujita, K.; Kamataki, T. Inhibition of benzo[a]pyrene-induced mutagenesis by (-)-epigallocatechin gallate in the lung of rpsL transgenic mice. Carcinogenesis, 1999, 20, 421-424.
    • (1999) Carcinogenesis , vol.20 , pp. 421-424
    • Muto, S.1    Yokoi, T.2    Gondo, Y.3    Katsuki, M.4    Shioyama, Y.5    Fujita, K.6    Kamataki, T.7
  • 45
    • 0035918278 scopus 로고    scopus 로고
    • Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo
    • Nam, S.; Smith, D. M.; Dou, Q. P. Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo. J. Biol. Chem. 2001, 276, 13322-13330.
    • (2001) J. Biol. Chem , vol.276 , pp. 13322-13330
    • Nam, S.1    Smith, D.M.2    Dou, Q.P.3
  • 46
    • 0036428820 scopus 로고    scopus 로고
    • Synthetic analogs of green tea polyphenols as proteasome inhibitors
    • Smith, D. M.; Wang, Z.; Kazi, A.; Li, L. H.; Chan, T. H.; Dou, Q. P. Synthetic analogs of green tea polyphenols as proteasome inhibitors. Mol. Med., 2002, 8, 382-392.
    • (2002) Mol. Med , vol.8 , pp. 382-392
    • Smith, D.M.1    Wang, Z.2    Kazi, A.3    Li, L.H.4    Chan, T.H.5    Dou, Q.P.6
  • 49
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem., 1998, 19, 1639-1662.
    • (1998) J. Comput. Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 50
    • 18044383342 scopus 로고    scopus 로고
    • Dietary flavonoids as proteasome inhibitors and apoptosis inducers in human leukemia cells
    • Chen, D.; Daniel, K. G.; Chen, M. S.; Kuhn, D. J.; Landis-Piwowar, K. R.; Dou, Q. P. Dietary flavonoids as proteasome inhibitors and apoptosis inducers in human leukemia cells. Biochem. Pharmacol., 2005, 69, 1421-1432.
    • (2005) Biochem. Pharmacol , vol.69 , pp. 1421-1432
    • Chen, D.1    Daniel, K.G.2    Chen, M.S.3    Kuhn, D.J.4    Landis-Piwowar, K.R.5    Dou, Q.P.6
  • 51
    • 4544254544 scopus 로고    scopus 로고
    • A hydroxyl group of flavonoids affects oral anti-inflammatory activity and inhibition of systemic tumor necrosis factor-alpha production
    • Ueda, H.; Yamazaki, C.; Yamazaki, M. A hydroxyl group of flavonoids affects oral anti-inflammatory activity and inhibition of systemic tumor necrosis factor-alpha production. Biosci. Biotechnol. Biochem., 2004, 1, 119-125.
    • (2004) Biosci. Biotechnol. Biochem , vol.1 , pp. 119-125
    • Ueda, H.1    Yamazaki, C.2    Yamazaki, M.3
  • 52
    • 65249101693 scopus 로고    scopus 로고
    • Homology modeling and docking analysis of the interaction between polyphenols and mammalian 20S proteasomes
    • Mozzicafreddo, M.; Cuccioloni, M.; Cecarini, V.; Eleuteri, A. M.; Angeletti, M. Homology modeling and docking analysis of the interaction between polyphenols and mammalian 20S proteasomes. J. Chem. Inf. Model., 2009, 49, 401-409.
    • (2009) J. Chem. Inf. Model , vol.49 , pp. 401-409
    • Mozzicafreddo, M.1    Cuccioloni, M.2    Cecarini, V.3    Eleuteri, A.M.4    Angeletti, M.5
  • 54
    • 0042622380 scopus 로고    scopus 로고
    • Swiss-Model: An automated protein homology-modeling server
    • Schwede, T.; Kopp, J.; Guex, N.; Peitsch, M. C. Swiss-Model: An automated protein homology-modeling server. Nucleic Acids Res., 2003, 31, 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 57
    • 0343262654 scopus 로고    scopus 로고
    • Crystal structure of epoxomicin: 20S proteasome reveals a molecular basis for selectivity of alpha, beta- epoxyketone proteasome inhibitors
    • Groll, M.; Kim, K. B.; Kairies, N.; Crews, C. Crystal structure of epoxomicin: 20S proteasome reveals a molecular basis for selectivity of alpha, beta- epoxyketone proteasome inhibitors. J. Am. Chem. Soc., 2000, 122, 1237-1238.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 1237-1238
    • Groll, M.1    Kim, K.B.2    Kairies, N.3    Crews, C.4
  • 58
    • 33644845743 scopus 로고    scopus 로고
    • Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome
    • Groll, M.; Berkers, C. R.; Ploegh, H. L.; Ovaa, H. Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome. Structure, 2006, 14, 451-456.
    • (2006) Structure , vol.14 , pp. 451-456
    • Groll, M.1    Berkers, C.R.2    Ploegh, H.L.3    Ovaa, H.4
  • 59
    • 33646137808 scopus 로고    scopus 로고
    • Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding
    • Groll, M.; Huber, R.; Potts, B. C. Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding. J. Am. Chem. Soc., 2006, 128, 5136-5141.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 5136-5141
    • Groll, M.1    Huber, R.2    Potts, B.C.3
  • 60
    • 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, 543-548.
    • (2001) J. Mol. Biol , vol.311 , pp. 543-548
    • Groll, M.1    Koguchi, Y.2    Huber, R.3    Kohno, J.4
  • 61
    • 19444387760 scopus 로고    scopus 로고
    • The 1.9 Å structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions
    • Forster, A.; Masters, E. I.; Whitby, F. G.; Robinson, H.; Hill, C. P. The 1.9 Å structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Mol. Cell, 2005, 18, 589-599.
    • (2005) Mol. Cell , vol.18 , pp. 589-599
    • Forster, A.1    Masters, E.I.2    Whitby, F.G.3    Robinson, H.4    Hill, C.P.5
  • 62
    • 83455193372 scopus 로고    scopus 로고
    • Release, Cambridge, U.K
    • Release 2005, Accelrys Ltd., Cambridge, U.K.
    • (2005) Accelrys Ltd
  • 63
    • 2442680018 scopus 로고    scopus 로고
    • Direct inhibition of the ubiquitin- proteasome pathway by ester bond-containing green tea polyphenols is associated with increased expression of sterol regulatory element-binding protein 2 and LDL receptor
    • Kuhn, D. J.; Burns, A. C.; Kazi, A.; Dou, Q. P. Direct inhibition of the ubiquitin- proteasome pathway by ester bond-containing green tea polyphenols is associated with increased expression of sterol regulatory element-binding protein 2 and LDL receptor. Biochim. Biophys. Acta, 2004, 1682, 1-10.
    • (2004) Biochim. Biophys. Acta , vol.1682 , pp. 1-10
    • Kuhn, D.J.1    Burns, A.C.2    Kazi, A.3    Dou, Q.P.4
  • 64
    • 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.; Kinoshita, N.; Homma, Y.; Hamada, M.; Iinuma, H.; Takeuchi, T. 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, 997-1003.
    • (2001) J. Antibiot , vol.54 , pp. 997-1003
    • Momose, I.1    Sekizawa, R.2    Hashizume, H.3    Kinoshita, N.4    Homma, Y.5    Hamada, M.6    Iinuma, H.7    Takeuchi, T.8
  • 65
    • 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.; Ikeda, D.; Naganawa, H.; Iinuma, H.; Takeuchi, T. Tyropeptins A and B, new proteasome inhibitors produced by Kitasatospora sp. MK993-dF2. II. Structure determination and synthesis. J. Antibiot., 2001, 54, 1004-1012.
    • (2001) J. Antibiot , vol.54 , pp. 1004-1012
    • Momose, I.1    Sekizawa, R.2    Hirosawa, S.3    Ikeda, D.4    Naganawa, H.5    Iinuma, H.6    Takeuchi, T.7
  • 67
    • 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.; Iinuma, H.; Ikeda, D. Structure-based design of derivatives of tyropeptin A as the potent and selective inhibitors of mammalian 20S proteasome. Bioorg. Med. Chem. Lett., 2005, 15, 1867-1871.
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 1867-1871
    • Momose, I.1    Umezawa, Y.2    Hirosawa, S.3    Iinuma, H.4    Ikeda, D.5
  • 70
    • 0032054015 scopus 로고    scopus 로고
    • CH/l{cyrillic} interactions as demonstrated in the crystal structure of guanine-nucleotide binding proteins, Src homology-2 domains and human growth hormone in complex with their specific ligands
    • Umezawa, Y.; Nishio, M. CH/l{cyrillic} interactions as demonstrated in the crystal structure of guanine-nucleotide binding proteins, Src homology-2 domains and human growth hormone in complex with their specific ligands. Bioorg. Med. Chem., 1998, 6, 493-504.
    • (1998) Bioorg. Med. Chem , vol.6 , pp. 493-504
    • Umezawa, Y.1    Nishio, M.2
  • 71
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky, A.; Michaud, C.; Powers, J. C.; Orlowski, M. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry, 1992, 31, 9421-9428.
    • (1992) Biochemistry , vol.31 , pp. 9421-9428
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 72
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class 1 molecules
    • Rock, K. L.; Gramm, C.; Rothstein, L.; Clark, K.; Stein, R.; Dick, L.; Hwang, D.; Goldberg, A. L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class 1 molecules. Cell, 1994, 78, 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 73
    • 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.; Ito, H.; Kawashima, S. Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-Leucine and tri-Leucine. J. Biochem., 1996, 119, 572-576.
    • (1996) J. Biochem , vol.119 , pp. 572-576
    • Tsubuki, S.1    Saito, Y.2    Tomioka, M.3    Ito, H.4    Kawashima, S.5
  • 74
    • 0027980321 scopus 로고
    • The ubiquitin- proteosome pathway is required for processing the NFkB1 precursor protein and the activation of NF-kB
    • Palombella, V. J.; Rando, O. J.; Goldberg, A. L.; Maniatis, T. The ubiquitin- proteosome pathway is required for processing the NFkB1 precursor protein and the activation of NF-kB. Cell, 1994, 78, 773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 75
    • 70350350874 scopus 로고    scopus 로고
    • Covalent complexes of proteasome model with peptide aldehyde inhibitors MG132 and MG101: Docking and molecular dynamics study
    • Zhang, S. W.; Shi, Y. W.; Jin, H. W.; Liu, Z. M.; Zhang, L. R.; Zhang, L. H. Covalent complexes of proteasome model with peptide aldehyde inhibitors MG132 and MG101: docking and molecular dynamics study. J. Mol. Model., 2009, 15, 1481-1490.
    • (2009) J. Mol. Model , vol.15 , pp. 1481-1490
    • Zhang, S.W.1    Shi, Y.W.2    Jin, H.W.3    Liu, Z.M.4    Zhang, L.R.5    Zhang, L.H.6
  • 76
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones, G.; Willett, P.; Glen, R. C.; Leach, A. R.; Taylor, R. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol., 1997, 267, 727-748.
    • (1997) J. Mol. Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 77
    • 83455185511 scopus 로고    scopus 로고
    • The Cambridge Crystallographic Data Centre GOLD 4.0, 609 CCDC, Cambridge, UK
    • The Cambridge Crystallographic Data Centre GOLD 4.0, 609 CCDC, Cambridge, UK. 2008.
    • (2008)
  • 78
    • 31044446240 scopus 로고    scopus 로고
    • 3D-QSAR studies on tripeptide aldehyde inhibitors of proteasome using CoMFA and CoMSIA methods. Bioorg. Med
    • Zhu, Y. Q.; Pei, J. F.; Liu, Z. M.; Lai, L. H.; Cui, J. R.; Li, R. T. 3D-QSAR studies on tripeptide aldehyde inhibitors of proteasome using CoMFA and CoMSIA methods. Bioorg. Med. Chem., 2006, 14, 1483-1496.
    • (2006) Chem , vol.14 , pp. 1483-1496
    • Zhu, Y.Q.1    Pei, J.F.2    Liu, Z.M.3    Lai, L.H.4    Cui, J.R.5    Li, R.T.6
  • 80
    • 33646753668 scopus 로고    scopus 로고
    • Optimization of subsite binding to the β5 subunit of the human 20S proteasome using vinyl sulfones and 2-keto-1,3,4-oxadiazoles: Syntheses and cellular properties of potent, selective proteasome inhibitors
    • Rydzewski, R. M.; Burrill, L.; Mendonca, R.; Palmer, J. T.; Rice, M.; Tahilramani, R.; Bass, K. E.; Leung, L.; Gjerstad, E.; Janc, J. W.; Pan, L. Optimization of subsite binding to the β5 subunit of the human 20S proteasome using vinyl sulfones and 2-keto-1,3,4-oxadiazoles: syntheses and cellular properties of potent, selective proteasome inhibitors. J. Med. Chem., 2006, 49, 2953-2968.
    • (2006) J. Med. Chem , vol.49 , pp. 2953-2968
    • Rydzewski, R.M.1    Burrill, L.2    Mendonca, R.3    Palmer, J.T.4    Rice, M.5    Tahilramani, R.6    Bass, K.E.7    Leung, L.8    Gjerstad, E.9    Janc, J.W.10    Pan, L.11
  • 81
    • 33846568091 scopus 로고    scopus 로고
    • Design and synthesis of a novel class of furanbased molecules as potential 20S proteasome inhibitors
    • Fu, Y. Q.; Xu, B.; Zou, X. M.; Ma, C.; Yang, X. M.; Mou, K.; Fu, G.; Lü, Y.; Xu, P. Design and synthesis of a novel class of furanbased molecules as potential 20S proteasome inhibitors. Bioorg. Med. Chem. Lett., 2007, 17, 1102-1106.
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , pp. 1102-1106
    • Fu, Y.Q.1    Xu, B.2    Zou, X.M.3    Ma, C.4    Yang, X.M.5    Mou, K.6    Fu, G.7    Lü, Y.8    Xu, P.9
  • 82
    • 40749103758 scopus 로고    scopus 로고
    • Novel CADD-based peptidyl vinyl ester derivatives as potential proteasome inhibitors
    • Mou, K.; Xu, B.; Ma, C.; Yang, X. M.; Zou, X. M.; Lü, Y.; Xu, P. Novel CADD-based peptidyl vinyl ester derivatives as potential proteasome inhibitors. Bioorg. Med. Chem. Lett., 2008, 18, 2198-2202.
    • (2008) Bioorg. Med. Chem. Lett , vol.18 , pp. 2198-2202
    • Mou, K.1    Xu, B.2    Ma, C.3    Yang, X.M.4    Zou, X.M.5    Lü, Y.6    Xu, P.7
  • 83
    • 0035927192 scopus 로고    scopus 로고
    • Modeling of the binding mode of a non-covalent inhibitor of the 20S proteasome. Application to structure-based analogue design
    • Furet, P.; Imbach, P.; Fürst, P.; Lang, M.; Noorani, M.; Zimmermann, J.; García-Echeverría, C. Modeling of the binding mode of a non-covalent inhibitor of the 20S proteasome. Application to structure-based analogue design. Bioorg. Med. Chem. Lett., 2001, 11, 1321-1324.
    • (2001) Bioorg. Med. Chem. Lett , vol.11 , pp. 1321-1324
    • Furet, P.1    Imbach, P.2    Fürst, P.3    Lang, M.4    Noorani, M.5    Zimmermann, J.6    García-Echeverría, C.7
  • 84
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph., 1990, 8, 52-56.
    • (1990) J. Mol. Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 86
    • 0030771347 scopus 로고    scopus 로고
    • QSAR and 3D QSAR in drug design Part 1: Methodology. Drug Discov
    • Kubinyi, H. QSAR and 3D QSAR in drug design Part 1: methodology. Drug Discov. Today, 1997, 2, 457-467.
    • (1997) Today , vol.2 , pp. 457-467
    • Kubinyi, H.1
  • 87
    • 85038459721 scopus 로고    scopus 로고
    • Tripos Inc., St. Louis, USA, version 7.3
    • Tripos Inc., St. Louis, USA, version 7.3.
  • 88
    • 69949163678 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of tripeptide boronic acid proteasome inhibitors
    • Zhu, Y. Q.; Yao, S. Y; Xu, B.; Ge, Z. M.; Cui, J. R.; Chen, T. M.; Li, R. T. Design, synthesis and biological evaluation of tripeptide boronic acid proteasome inhibitors. Bioorg. Med. Chem., 2009, 17, 6851-6861.
    • (2009) Bioorg. Med. Chem , vol.17 , pp. 6851-6861
    • Zhu, Y.Q.1    Yao, S.Y.2    Xu, B.3    Ge, Z.M.4    Cui, J.R.5    Chen, T.M.6    Li, R.T.7
  • 90
    • 61449124148 scopus 로고    scopus 로고
    • 3DQSAR studies of boron-containing dipeptides as proteasome inhibitors with CoMFA and CoMSIA methods
    • Zhu, Y. Q.; Lei, M.; Lu, A. J.; Zhao, X.; Yin, X. J.; Gao, Q. Z. 3DQSAR studies of boron-containing dipeptides as proteasome inhibitors with CoMFA and CoMSIA methods. Eur. J. Med. Chem., 2009, 44, 1486-1499.
    • (2009) Eur. J. Med. Chem , vol.44 , pp. 1486-1499
    • Zhu, Y.Q.1    Lei, M.2    Lu, A.J.3    Zhao, X.4    Yin, X.J.5    Gao, Q.Z.6
  • 91
    • 0042389512 scopus 로고    scopus 로고
    • A new strategy for molecular modeling and receptor-based design of carborane containing compounds
    • Johnsamuel, J.; Byun, Y.; Jones, T. P.; Endo, Y.; Tjarks, W. A new strategy for molecular modeling and receptor-based design of carborane containing compounds. J. Organomet. Chem., 2003, 680, 223-231.
    • (2003) J. Organomet. Chem , vol.680 , pp. 223-231
    • Johnsamuel, J.1    Byun, Y.2    Jones, T.P.3    Endo, Y.4    Tjarks, W.5
  • 92
    • 0042833010 scopus 로고    scopus 로고
    • A convenient method for the computer-aided molecular design of carborane containing compounds
    • Johnsamuel, J.; Byun, Y.; Jones, T. P.; Endo, Y.; Tjarks, W. A convenient method for the computer-aided molecular design of carborane containing compounds. Bioorg. Med. Chem. Lett., 2003, 13, 3213-3216.
    • (2003) Bioorg. Med. Chem. Lett , vol.13 , pp. 3213-3216
    • Johnsamuel, J.1    Byun, Y.2    Jones, T.P.3    Endo, Y.4    Tjarks, W.5
  • 93
    • 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 α-amino acid boronates
    • Zhu, Y. Q.; Zhao, X.; Zhu, X. R; Wu, G.; Li, Y. J.; Ma, Y. H.; Yuan, Y. X.; Yang, J.; Hu, Y.; Ai, L.; Gao, Q. Z. Design, synthesis, biological evaluation, and structure-activity relationship (SAR) discussion of dipeptidyl boronate proteasome inhibitors, part I: comprehensive understanding of the SAR of α-amino acid boronates. J. Med. Chem., 2009, 52, 4192-4199.
    • (2009) J. Med. Chem , vol.52 , pp. 4192-4199
    • Zhu, Y.Q.1    Zhao, X.2    Zhu, X.R.3    Wu, G.4    Li, Y.J.5    Ma, Y.H.6    Yuan, Y.X.7    Yang, J.8    Hu, Y.9    Ai, L.10    Gao, Q.Z.11
  • 94
    • 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. L.; Zhu, Y. Q. Pharmacophore modeling, docking studies and synthesis of novel dipeptide proteasome inhibitors containing boron atoms. J. Chem. Inf. Mol., 2009, 49, 2092-2100.
    • (2009) J. Chem. Inf. Mol , vol.49 , pp. 2092-2100
    • Lei, M.1    Zhao, X.2    Wang, Z.L.3    Zhu, Y.Q.4
  • 95
    • 85038456245 scopus 로고    scopus 로고
    • Catalyst, 4.11; Accelrys Inc.: San Diego, CA, USA
    • Catalyst, 4.11; Accelrys Inc.: San Diego, CA, USA.
  • 96
    • 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, 687-717.
    • (2007) Chem. Rev , vol.107 , pp. 687-717
    • Borissenko, L.1    Groll, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.