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Volumn 10, Issue 6, 2010, Pages 540-549

Specificity in the interaction of natural products with their target proteins- A biochemical and structural insight

Author keywords

Cancer; Mechanism; Molecular target; Natural products; Specificity; Structure

Indexed keywords

APOGOSSYPOL; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; EPIDITHIODIKETOPIPERAZINE; FLAVOPIRIDOL; FUMAGILLIN; GOSSYPOL DERIVATIVE; IMATINIB; NATURAL PRODUCT; PLADIENOLIDE; PROTEASOME INHIBITOR; PROTEIN MDM2; PROTEIN P53; RESVERATROL; SALINOSPORAMIDE A; UNCLASSIFIED DRUG;

EID: 77953709832     PISSN: 13895575     EISSN: None     Source Type: Journal    
DOI: 10.2174/138955710791384090     Document Type: Article
Times cited : (10)

References (90)
  • 1
    • 34247109045 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the last 25 years
    • Newman, D. J.; Cragg, G. M. Natural products as sources of new drugs over the last 25 years. J. Nat. Prod., 2007, 70, 461-77.
    • (2007) J. Nat. Prod. , vol.70 , pp. 461-477
    • Newman, D.J.1    Cragg, G.M.2
  • 2
    • 0030221053 scopus 로고    scopus 로고
    • Understanding and controlling the cell cycle with natural products
    • Hung, D. T.; Jamison, T. F.; Schreiber, S. L. Understanding and controlling the cell cycle with natural products. Chem. Biol., 1996, 3, 623-39.
    • (1996) Chem. Biol. , vol.3 , pp. 623-639
    • Hung, D.T.1    Jamison, T.F.2    Schreiber, S.L.3
  • 3
    • 43749106622 scopus 로고    scopus 로고
    • Polymeric black tea polyphenols inhibit mouse skin chemical carcinogenesis by decreasing cell proliferation
    • Patel, R.; Krishnan, R.; Ramchandani, A.; Maru, G. Polymeric black tea polyphenols inhibit mouse skin chemical carcinogenesis by decreasing cell proliferation. Cell Prolif., 2008, 41, 532-53.
    • (2008) Cell Prolif , vol.41 , pp. 532-553
    • Patel, R.1    Krishnan, R.2    Ramchandani, A.3    Maru, G.4
  • 4
    • 65649137735 scopus 로고    scopus 로고
    • Chemoprotective mechanism of the natural compounds, epigallocatechin-3-O-gallate, quercetin and curcumin against cancer and cardiovascular diseases
    • Jagtap, S.; Meganathan, K.; Wagh, V.; Winkler, J.; Hescheler, J.; Sachinidis, A. Chemoprotective mechanism of the natural compounds, epigallocatechin-3-O-gallate, quercetin and curcumin against cancer and cardiovascular diseases. Curr. Med. Chem., 2009, 16, 1451-62.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 1451-1462
    • Jagtap, S.1    Meganathan, K.2    Wagh, V.3    Winkler, J.4    Hescheler, J.5    Sachinidis, A.6
  • 5
    • 55349122598 scopus 로고    scopus 로고
    • Triphala inhibits both in vitro and in vivo xenograft growth of pancreatic tumor cells by inducing apoptosis
    • Shi, Y.; Sahu, R. P.; Srivastava, S. K. Triphala inhibits both in vitro and in vivo xenograft growth of pancreatic tumor cells by inducing apoptosis. BMC Cancer, 2008, 8, 294.
    • (2008) BMC Cancer , vol.8 , pp. 294
    • Shi, Y.1    Sahu, R.P.2    Srivastava, S.K.3
  • 6
    • 77149179813 scopus 로고    scopus 로고
    • Curcumin as an anticancer agent: Review of the gap between basic and clinical applications
    • Bar-Sela, G.; Epelbaum, R.; Schaffer, M. Curcumin as an anticancer agent: review of the gap between basic and clinical applications. Curr. Med. Chem., 2010, 17(3), 190-197.
    • (2010) Curr. Med. Chem. , vol.17 , Issue.3 , pp. 190-197
    • Bar-Sela, G.1    Epelbaum, R.2    Schaffer, M.3
  • 7
    • 73349094986 scopus 로고    scopus 로고
    • Curcumin and cancer cells: How many ways can curry kill tumor cells selectively?
    • Ravindran, J.; Prasad, S.; Aggarwal, B. B. Curcumin and cancer cells: how many ways can curry kill tumor cells selectively? AAPS. J., 2009, 11, 495-510.
    • (2009) AAPS. J. , vol.11 , pp. 495-510
    • Ravindran, J.1    Prasad, S.2    Aggarwal, B.B.3
  • 9
    • 0033865492 scopus 로고    scopus 로고
    • Molecular mechanisms of anticancer activity of natural dietetic products
    • Colic, M.; Pavelic, K. Molecular mechanisms of anticancer activity of natural dietetic products. J. Mol. Med., 2000, 78, 333-336.
    • (2000) J. Mol. Med. , vol.78 , pp. 333-336
    • Colic, M.1    Pavelic, K.2
  • 10
    • 70350225860 scopus 로고    scopus 로고
    • Harnessing the fruits of nature for the development of multi-targeted cancer therapeutics
    • Sarkar, F. H.; Li, Y. Harnessing the fruits of nature for the development of multi-targeted cancer therapeutics. Cancer Treat. Rev., 2009, 35, 597-607.
    • (2009) Cancer Treat. Rev. , vol.35 , pp. 597-607
    • Sarkar, F.H.1    Li, Y.2
  • 12
    • 64949178567 scopus 로고    scopus 로고
    • Cytotoxicity and cellular uptake of doxorubicin and its formamidine derivatives in HL60 sensitive and HL60/MX2 resistant cells
    • Kik, K.; Wasowska-Lukawska, M.; Oszczapowicz, I.; Szmigiero, L. Cytotoxicity and cellular uptake of doxorubicin and its formamidine derivatives in HL60 sensitive and HL60/MX2 resistant cells. Anticancer Res., 2009, 29, 1429-1433.
    • (2009) Anticancer Res , vol.29 , pp. 1429-1433
    • Kik, K.1    Wasowska-Lukawska, M.2    Oszczapowicz, I.3    Szmigiero, L.4
  • 13
    • 35748968504 scopus 로고    scopus 로고
    • DNA topoisomerase II structures and anthracycline activity: Insights into ternary complex formation
    • Dal Ben, D.; Palumbo, M.; Zagotto, G.; Capranico, G.; Moro, S. DNA topoisomerase II structures and anthracycline activity: insights into ternary complex formation. Curr. Pharm. Des., 2007, 13, 2766-2780.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 2766-2780
    • dal Ben, D.1    Palumbo, M.2    Zagotto, G.3    Capranico, G.4    Moro, S.5
  • 14
    • 4344623889 scopus 로고    scopus 로고
    • Imatinib as a paradigm of targeted therapies
    • Druker, B. J. Imatinib as a paradigm of targeted therapies. Adv. Cancer Res., 2004, 91, 1-30.
    • (2004) Adv. Cancer Res. , vol.91 , pp. 1-30
    • Druker, B.J.1
  • 15
    • 70350490045 scopus 로고    scopus 로고
    • Gefitinib: A review of its use in the treatment of locally advanced/metastatic non-small cell lung cancer
    • Sanford, M.; Scott, L. J. Gefitinib: a review of its use in the treatment of locally advanced/metastatic non-small cell lung cancer. Drugs, 2009, 69, 2303-2328.
    • (2009) Drugs , vol.69 , pp. 2303-2328
    • Sanford, M.1    Scott, L.J.2
  • 16
    • 65349097586 scopus 로고    scopus 로고
    • Tubulin-interactive natural products as anticancer agents (1)
    • Kingston, D. G. Tubulin-interactive natural products as anticancer agents (1). J. Nat. Prod., 2009, 72, 507-515.
    • (2009) J. Nat. Prod. , vol.72 , pp. 507-515
    • Kingston, D.G.1
  • 17
    • 39149137869 scopus 로고    scopus 로고
    • Plant-derived compounds in clinical trials
    • Saklani, A.; Kutty, S. K. Plant-derived compounds in clinical trials. Drug Discov. Today, 2008, 13, 161-171.
    • (2008) Drug Discov. Today. , vol.13 , pp. 161-171
    • Saklani, A.1    Kutty, S.K.2
  • 18
    • 33746622984 scopus 로고    scopus 로고
    • Strategies for optimizing combinations of molecularly targeted anticancer agents
    • Dancey, J. E.; Chen, H. X. Strategies for optimizing combinations of molecularly targeted anticancer agents. Nat. Rev. Drug Discov., 2006, 5, 649-659.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 649-659
    • Dancey, J.E.1    Chen, H.X.2
  • 19
    • 42449147919 scopus 로고    scopus 로고
    • Bcl-2 antagonist apogossypol (NSC736630) displays single-agent activity in Bcl-2-transgenic mice and has superior efficacy with less toxicity compared with gossypol (NSC19048)
    • Kitada, S.; Kress, C. L.; Krajewska, M.; Jia, L.; Pellecchia, M.; Reed, J. C. Bcl-2 antagonist apogossypol (NSC736630) displays single-agent activity in Bcl-2-transgenic mice and has superior efficacy with less toxicity compared with gossypol (NSC19048). Blood, 2008, 111, 3211-3219.
    • (2008) Blood , vol.111 , pp. 3211-3219
    • Kitada, S.1    Kress, C.L.2    Krajewska, M.3    Jia, L.4    Pellecchia, M.5    Reed, J.C.6
  • 20
    • 33745305095 scopus 로고    scopus 로고
    • Antiangiogenic drugs: From bench to clinical trials
    • Quesada, A. R.; Munoz-Chapuli, R.; Medina, M. A. Antiangiogenic drugs: from bench to clinical trials. Med. Res. Rev., 2006, 26, 483-530.
    • (2006) Med. Res. Rev. , vol.26 , pp. 483-530
    • Quesada, A.R.1    Munoz-Chapuli, R.2    Medina, M.A.3
  • 21
    • 35048895357 scopus 로고    scopus 로고
    • Targeting protein-protein interactions: Lessons from p53/MDM2
    • Murray, J. K.; Gellman, S. H. Targeting protein-protein interactions: lessons from p53/MDM2. Biopolymers, 2007, 88, 657-686.
    • (2007) Biopolymers , vol.88 , pp. 657-686
    • Murray, J.K.1    Gellman, S.H.2
  • 22
    • 2642551603 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor Velcade (Bortezomib)
    • Adams, J.; Kauffman, M. Development of the proteasome inhibitor Velcade (Bortezomib). Cancer Invest., 2004, 22, 304-311.
    • (2004) Cancer Invest , vol.22 , pp. 304-311
    • Adams, J.1    Kauffman, M.2
  • 23
    • 77249121048 scopus 로고    scopus 로고
    • Geldanamycin and its anticancer activities
    • Fukuyo, Y.; Hunt, C. R.; Horikoshi, N. Geldanamycin and its anticancer activities. Cancer Lett., 2010, 290, 24-35.
    • (2010) Cancer Lett , vol.290 , pp. 24-35
    • Fukuyo, Y.1    Hunt, C.R.2    Horikoshi, N.3
  • 24
    • 63149118507 scopus 로고    scopus 로고
    • Ready for a comeback of natural products in oncology
    • Bailly, C. Ready for a comeback of natural products in oncology. Biochem. Pharmacol., 2009, 77, 1447-1457.
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 1447-1457
    • Bailly, C.1
  • 25
    • 34748826129 scopus 로고    scopus 로고
    • HSP90 antagonist, geldanamycin, inhibits proliferation, induces apoptosis and blocks migration of rhabdomyosarcoma cells in vitro and seeding into bone marrow in vivo
    • Lesko, E.; Gozdzik, J.; Kijowski, J.; Jenner, B.; Wiecha, O.; Majka, M. HSP90 antagonist, geldanamycin, inhibits proliferation, induces apoptosis and blocks migration of rhabdomyosarcoma cells in vitro and seeding into bone marrow in vivo. Anticancer Drugs, 2007, 18, 1173-1181.
    • (2007) Anticancer Drugs , vol.18 , pp. 1173-1181
    • Lesko, E.1    Gozdzik, J.2    Kijowski, J.3    Jenner, B.4    Wiecha, O.5    Majka, M.6
  • 26
    • 43749123904 scopus 로고    scopus 로고
    • Hsp90-inhibitor geldanamycin abrogates G2 arrest in p53-negative leukemia cell lines through the depletion of Chk1
    • Sugimoto, K.; Sasaki, M.; Isobe, Y.; Tsutsui, M.; Suto, H.; Ando, J.; Tamayose, K.; Ando, M.; Oshimi, K. Hsp90-inhibitor geldanamycin abrogates G2 arrest in p53-negative leukemia cell lines through the depletion of Chk1. Oncogene, 2008, 27, 3091-3101.
    • (2008) Oncogene , vol.27 , pp. 3091-3101
    • Sugimoto, K.1    Sasaki, M.2    Isobe, Y.3    Tsutsui, M.4    Suto, H.5    Ando, J.6    Tamayose, K.7    Ando, M.8    Oshimi, K.9
  • 28
    • 15944387964 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib sensitizes cells to killing by death receptor ligand TRAIL via BH3-only proteins Bik and Bim
    • Nikrad, M.; Johnson, T.; Puthalalath, H.; Coultas, L.; Adams, J.; Kraft, A. S. The proteasome inhibitor bortezomib sensitizes cells to killing by death receptor ligand TRAIL via BH3-only proteins Bik and Bim. Mol. Cancer Ther., 2005, 4, 443-449.
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 443-449
    • Nikrad, M.1    Johnson, T.2    Puthalalath, H.3    Coultas, L.4    Adams, J.5    Kraft, A.S.6
  • 30
    • 33847066706 scopus 로고    scopus 로고
    • Functions of the proteasome: From protein degradation and immune surveillance to cancer therapy
    • Goldberg, A. L. Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem. Soc. Trans., 2007, 35, 12-17.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 12-17
    • Goldberg, A.L.1
  • 31
    • 33947596504 scopus 로고    scopus 로고
    • Why is cancer drug discovery so difficult?
    • Kamb, A.; Wee, S.; Lengauer, C. Why is cancer drug discovery so difficult? Nat. Rev. Drug Discov., 2007, 6, 115-120.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 115-120
    • Kamb, A.1    Wee, S.2    Lengauer, C.3
  • 32
    • 65549152514 scopus 로고    scopus 로고
    • Equally potent inhibition of c-Src and Abl by compounds that recognize inactive kinase conformations
    • Seeliger, M. A.; Ranjitkar, P.; Kasap, C.; Shan, Y.; Shaw, D. E.; Shah, N. P.; Kuriyan, J.; Maly, D. J. Equally potent inhibition of c-Src and Abl by compounds that recognize inactive kinase conformations. Cancer Res., 2009, 69, 2384-2392.
    • (2009) Cancer Res , vol.69 , pp. 2384-2392
    • Seeliger, M.A.1    Ranjitkar, P.2    Kasap, C.3    Shan, Y.4    Shaw, D.E.5    Shah, N.P.6    Kuriyan, J.7    Maly, D.J.8
  • 33
    • 33847659183 scopus 로고    scopus 로고
    • C-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty
    • Seeliger, M. A.; Nagar, B.; Frank, F.; Cao, X.; Henderson, M. N.; Kuriyan, J. c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty. Structure, 2007, 15, 299-311.
    • (2007) Structure , vol.15 , pp. 299-311
    • Seeliger, M.A.1    Nagar, B.2    Frank, F.3    Cao, X.4    Henderson, M.N.5    Kuriyan, J.6
  • 35
    • 62449337409 scopus 로고    scopus 로고
    • The structure of the leukemia drug imatinib bound to human quinine reductase 2 (NQO2)
    • Winger, J. A.; Hantschel, O.; Superti-Furga, G.; Kuriyan, J. The structure of the leukemia drug imatinib bound to human quinine reductase 2 (NQO2). BMC Struct. Biol., 2009, 9, 7.
    • (2009) BMC Struct. Biol. , vol.9 , pp. 7
    • Winger, J.A.1    Hantschel, O.2    Superti-Furga, G.3    Kuriyan, J.4
  • 36
    • 28344433705 scopus 로고    scopus 로고
    • NRH:Quinine reductase 2: An enzyme of surprises and mysteries
    • Vella, F.; Ferry, G.; Delagrange, P.; Boutin, J. A. NRH:quinine reductase 2: an enzyme of surprises and mysteries. Biochem. Pharmacol., 2005, 71, 1-12.
    • (2005) Biochem. Pharmacol. , vol.71 , pp. 1-12
    • Vella, F.1    Ferry, G.2    Delagrange, P.3    Boutin, J.A.4
  • 37
    • 4444267291 scopus 로고    scopus 로고
    • Crystal structure of quinone reductase 2 in complex with resveratrol
    • Buryanovskyy, L.; Fu, Y.; Boyd, M.; Ma, Y.; Hsieh, T. C.; Wu, J. M.; Zhang, Z. Crystal structure of quinone reductase 2 in complex with resveratrol. Biochemistry, 2004, 43, 11417-11426.
    • (2004) Biochemistry , vol.43 , pp. 11417-11426
    • Buryanovskyy, L.1    Fu, Y.2    Boyd, M.3    Ma, Y.4    Hsieh, T.C.5    Wu, J.M.6    Zhang, Z.7
  • 38
    • 0032536187 scopus 로고    scopus 로고
    • Resveratrol, a remarkable inhibitor of ribonucleotide reductase
    • Fontecave, M.; Lepoivre, M.; Elleingand, E.; Gerez, C.; Guittet, O. Resveratrol, a remarkable inhibitor of ribonucleotide reductase. FEBS Lett., 1998, 421, 277-279.
    • (1998) FEBS Lett , vol.421 , pp. 277-279
    • Fontecave, M.1    Lepoivre, M.2    Elleingand, E.3    Gerez, C.4    Guittet, O.5
  • 39
    • 4544327822 scopus 로고    scopus 로고
    • Identification and purification of resveratrol targeting proteins using immobilized resveratrol affinity chromatography
    • Wang, Z.; Hsieh, T. C.; Zhang, Z.; Ma, Y.; Wu, J. M. Identification and purification of resveratrol targeting proteins using immobilized resveratrol affinity chromatography. Biochem. Biophys. Res. Commun., 2004, 323, 743-749.
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 743-749
    • Wang, Z.1    Hsieh, T.C.2    Zhang, Z.3    Ma, Y.4    Wu, J.M.5
  • 40
    • 0034777238 scopus 로고    scopus 로고
    • Effect of estradiol, diethylstilbestrol, and resveratrol on F0F1-ATPase activity from mitochondrial preparations of rat heart, liver, and brain
    • Kipp, J. L.; Ramirez, V. D. Effect of estradiol, diethylstilbestrol, and resveratrol on F0F1-ATPase activity from mitochondrial preparations of rat heart, liver, and brain. Endocrine, 2001, 15, 165-175.
    • (2001) Endocrine , vol.15 , pp. 165-175
    • Kipp, J.L.1    Ramirez, V.D.2
  • 41
    • 0037378391 scopus 로고    scopus 로고
    • Resveratrol-induced G2 arrest through the inhibition of CDK7 and p34CDC2 kinases in colon carcinoma HT29 cells
    • Liang, Y. C.; Tsai, S. H.; Chen, L.; Lin-Shiau, S. Y.; Lin, J. K. Resveratrol-induced G2 arrest through the inhibition of CDK7 and p34CDC2 kinases in colon carcinoma HT29 cells. Biochem. Pharmacol., 2003, 65, 1053-1060.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 1053-1060
    • Liang, Y.C.1    Tsai, S.H.2    Chen, L.3    Lin-Shiau, S.Y.4    Lin, J.K.5
  • 42
    • 33745823841 scopus 로고    scopus 로고
    • Ribonucleotide reductase inhibitors and future drug design
    • Shao, J.; Zhou, B.; Chu, B.; Yen, Y. Ribonucleotide reductase inhibitors and future drug design. Curr. Cancer Drug Targets, 2006, 6, 409-4031.
    • (2006) Curr. Cancer Drug Targets , vol.6 , pp. 409-4031
    • Shao, J.1    Zhou, B.2    Chu, B.3    Yen, Y.4
  • 43
    • 19044394312 scopus 로고    scopus 로고
    • Overview of ribonucleotide reductase inhibitors: An appealing target in anti-tumour therapy
    • Cerqueira, N. M.; Pereira, S.; Fernandes, P. A.; Ramos, M. J. Overview of ribonucleotide reductase inhibitors: an appealing target in anti-tumour therapy. Curr. Med. Chem., 2005, 12, 1283-1294.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1283-1294
    • Cerqueira, N.M.1    Pereira, S.2    Fernandes, P.A.3    Ramos, M.J.4
  • 45
    • 0034886973 scopus 로고    scopus 로고
    • Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases
    • Larsson, K. M.; Andersson, J.; Sjoberg, B. M.; Nordlund, P.; Logan, D. T. Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases. Structure, 2001, 9, 739-750.
    • (2001) Structure , vol.9 , pp. 739-750
    • Larsson, K.M.1    Andersson, J.2    Sjoberg, B.M.3    Nordlund, P.4    Logan, D.T.5
  • 46
    • 7544227865 scopus 로고    scopus 로고
    • Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase
    • Larsson, K. M.; Jordan, A.; Eliasson, R.; Reichard, P.; Logan, D. T.; Nordlund, P. Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase. Nat. Struct. Mol. Biol., 2004, 11, 1142-1149.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1142-1149
    • Larsson, K.M.1    Jordan, A.2    Eliasson, R.3    Reichard, P.4    Logan, D.T.5    Nordlund, P.6
  • 47
    • 0029705324 scopus 로고    scopus 로고
    • Automated docking of flexible ligands: Applications of AutoDock
    • Goodsell, D. S.; Morris, G. M.; Olson, A. J. Automated docking of flexible ligands: applications of AutoDock. J. Mol. Recognit., 1996, 9, 1-5.
    • (1996) J. Mol. Recognit. , vol.9 , pp. 1-5
    • Goodsell, D.S.1    Morris, G.M.2    Olson, A.J.3
  • 48
    • 33645802169 scopus 로고    scopus 로고
    • Cyclin-dependent kinase pathways as targets for cancer treatment
    • Shapiro, G. I. Cyclin-dependent kinase pathways as targets for cancer treatment. J. Clin. Oncol., 2006, 24, 1770-1783.
    • (2006) J. Clin. Oncol. , vol.24 , pp. 1770-1783
    • Shapiro, G.I.1
  • 54
    • 2342427030 scopus 로고    scopus 로고
    • Inhibition of anti-apoptotic Bcl-2 family proteins by natural polyphenols: New avenues for cancer chemoprevention and chemotherapy
    • Pellecchia, M.; Reed, J. C. Inhibition of anti-apoptotic Bcl-2 family proteins by natural polyphenols: new avenues for cancer chemoprevention and chemotherapy. Curr. Pharm. Des., 2004, 10, 1387-1398.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1387-1398
    • Pellecchia, M.1    Reed, J.C.2
  • 55
    • 0031815389 scopus 로고    scopus 로고
    • Inhibition of growth and induction of apoptosis in human cancer cell lines by tea polyphenols
    • Yang, G. Y.; Liao, J.; Kim, K.; Yurkow, E. J.; Yang, C. S. Inhibition of growth and induction of apoptosis in human cancer cell lines by tea polyphenols. Carcinogenesis, 1998, 19, 611-616.
    • (1998) Carcinogenesis , vol.19 , pp. 611-616
    • Yang, G.Y.1    Liao, J.2    Kim, K.3    Yurkow, E.J.4    Yang, C.S.5
  • 56
    • 0347626109 scopus 로고    scopus 로고
    • Cancer prevention by tea polyphenols is linked to their direct inhibition of antiapoptotic Bcl-2-family proteins
    • Leone, M.; Zhai, D.; Sareth, S.; Kitada, S.; Reed, J. C.; Pellecchia, M. Cancer prevention by tea polyphenols is linked to their direct inhibition of antiapoptotic Bcl-2-family proteins. Cancer Res., 2003, 63, 8118-8121.
    • (2003) Cancer Res , vol.63 , pp. 8118-8121
    • Leone, M.1    Zhai, D.2    Sareth, S.3    Kitada, S.4    Reed, J.C.5    Pellecchia, M.6
  • 57
    • 34047217206 scopus 로고    scopus 로고
    • Randomized phase III trial of fludarabine plus cyclophosphamide with or without oblimersen sodium (Bcl-2 antisense) in patients with relapsed or refractory chronic lymphocytic leukemia
    • O'Brien, S.; Moore, J. O.; Boyd, T. E.; Larratt, L. M.; Skotnicki, A.; Koziner, B.; Chanan-Khan, A. A.; Seymour, J. F.; Bociek, R. G.; Pavletic, S.; Rai, K. R. Randomized phase III trial of fludarabine plus cyclophosphamide with or without oblimersen sodium (Bcl-2 antisense) in patients with relapsed or refractory chronic lymphocytic leukemia. J. Clin. Oncol. 2007, 25, 1114-1120.
    • (2007) J. Clin. Oncol. , vol.25 , pp. 1114-1120
    • O'Brien, S.1    Moore, J.O.2    Boyd, T.E.3    Larratt, L.M.4    Skotnicki, A.5    Koziner, B.6    Chanan-Khan, A.A.7    Seymour, J.F.8    Bociek, R.G.9    Pavletic, S.10    Rai, K.R.11
  • 59
    • 77950224306 scopus 로고    scopus 로고
    • Preclinical Studies of Apogossypolone, a Novel Pan Inhibitor of Bcl-2 and Mcl-1, Synergistically Potentiates Cytotoxic Effect of Gemcitabine in Pancreatic Cancer Cells
    • Banerjee, S.; Choi, M.; Aboukameel, A.; Wang, Z.; Mohammad, M.; Chen, J.; Yang, D.; Sarkar, F. H.; Mohammad, R. M. Preclinical Studies of Apogossypolone, a Novel Pan Inhibitor of Bcl-2 and Mcl-1, Synergistically Potentiates Cytotoxic Effect of Gemcitabine in Pancreatic Cancer Cells. Pancreas., 2010, 39, 323-331.
    • (2010) Pancreas , vol.39 , pp. 323-331
    • Banerjee, S.1    Choi, M.2    Aboukameel, A.3    Wang, Z.4    Mohammad, M.5    Chen, J.6    Yang, D.7    Sarkar, F.H.8    Mohammad, R.M.9
  • 61
    • 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
  • 62
    • 67650249228 scopus 로고    scopus 로고
    • Molecular basis for cancer chemoprevention by green tea polyphenol EGCG
    • Tachibana, H. Molecular basis for cancer chemoprevention by green tea polyphenol EGCG. Forum Nutr., 2009, 61, 156-169.
    • (2009) Forum Nutr , vol.61 , pp. 156-169
    • Tachibana, H.1
  • 63
    • 70350271965 scopus 로고    scopus 로고
    • Epidithiodiketopiperazines block the interaction between hypoxia-inducible factor-1alpha (HIF-1alpha) and p300 by a zinc ejection mechanism
    • Cook, K. M.; Hilton, S. T.; Mecinovic, J.; Motherwell, W. B.; Figg, W. D.; Schofield, C. J. Epidithiodiketopiperazines block the interaction between hypoxia-inducible factor-1alpha (HIF-1alpha) and p300 by a zinc ejection mechanism. J. Biol. Chem., 2009, 284, 26831-26838.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26831-26838
    • Cook, K.M.1    Hilton, S.T.2    Mecinovic, J.3    Motherwell, W.B.4    Figg, W.D.5    Schofield, C.J.6
  • 64
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart, C. M. Back to the future with ubiquitin. Cell, 2004, 116, 181-190.
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 65
    • 37249026703 scopus 로고    scopus 로고
    • Intracellular protein degradation from a vague idea through the lysosome and the ubiquitin-proteasome system and on to human diseases and drug targeting: Nobel Lecture, December 8, 2004
    • Ciechanover, A. Intracellular protein degradation from a vague idea through the lysosome and the ubiquitin-proteasome system and on to human diseases and drug targeting: Nobel Lecture, December 8, 2004. Ann. N. Y. Acad. Sci., 2007, 1116, 1-28.
    • (2007) Ann. N. Y. Acad. Sci. , vol.1116 , pp. 1-28
    • Ciechanover, A.1
  • 66
    • 10944267182 scopus 로고    scopus 로고
    • Ubiquitin: A Nobel protein
    • Wilkinson, K. D. Ubiquitin: a Nobel protein. Cell, 2004, 119, 741-745.
    • (2004) Cell , vol.119 , pp. 741-745
    • Wilkinson, K.D.1
  • 67
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H.; Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev., 2002, 82, 373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 68
    • 33745674468 scopus 로고    scopus 로고
    • Drug discovery in the ubiquitin-proteasome system
    • Nalepa, G.; Rolfe, M.; Harper, J. W. Drug discovery in the ubiquitin-proteasome system. Nat. Rev. Drug Discov. 2006, 5, 596-613.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 596-613
    • Nalepa, G.1    Rolfe, M.2    Harper, J.W.3
  • 71
    • 33745597909 scopus 로고    scopus 로고
    • Predicting protein interaction sites: Binding hot-spots in protein-protein and protein-ligand interfaces
    • Burgoyne, N. J.; Jackson, R. M. Predicting protein interaction sites: binding hot-spots in protein-protein and protein-ligand interfaces. Bioinformatics, 2006, 22, 1335-1342.
    • (2006) Bioinformatics , vol.22 , pp. 1335-1342
    • Burgoyne, N.J.1    Jackson, R.M.2
  • 72
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • Fuertes, G.; Martin De Llano, J. J.; Villarroya, A.; Rivett, A. J.; Knecht, E. Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem. J., 2003, 375, 75-86.
    • (2003) Biochem. J. , vol.375 , pp. 75-86
    • Fuertes, G.1    de Martin, L.J.J.2    Villarroya, A.3    Rivett, A.J.4    Knecht, E.5
  • 74
    • 0036015847 scopus 로고    scopus 로고
    • Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome
    • Groll, M.; Nazif, T.; Huber, R.; Bogyo, M. Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome. Chem. Biol., 2002, 9, 655-662.
    • (2002) Chem. Biol. , vol.9 , pp. 655-662
    • Groll, M.1    Nazif, T.2    Huber, R.3    Bogyo, M.4
  • 75
    • 71749110782 scopus 로고    scopus 로고
    • The 26 S proteasome: From basic mechanisms to drug targeting
    • Navon, A.; Ciechanover, A. The 26 S proteasome: from basic mechanisms to drug targeting. J. Biol. Chem., 2009, 284, 33713-33718.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33713-33718
    • Navon, A.1    Ciechanover, A.2
  • 76
    • 38949125853 scopus 로고    scopus 로고
    • Combination of proteasome inhibitors bortezomib and NPI-0052 trigger in vivo synergistic cytotoxicity in multiple myeloma
    • Chauhan, D.; Singh, A.; Brahmandam, M.; Podar, K.; Hideshima, T.; Richardson, P.; Munshi, N.; Palladino, M. A.; Anderson, K. C. Combination of proteasome inhibitors bortezomib and NPI-0052 trigger in vivo synergistic cytotoxicity in multiple myeloma. Blood, 2008, 111, 1654-1664.
    • (2008) Blood , vol.111 , pp. 1654-1664
    • Chauhan, D.1    Singh, A.2    Brahmandam, M.3    Podar, K.4    Hideshima, T.5    Richardson, P.6    Munshi, N.7    Palladino, M.A.8    Anderson, K.C.9
  • 77
    • 33646841837 scopus 로고    scopus 로고
    • Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate
    • Kisselev, A. F.; Callard, A.; Goldberg, A. L. Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate. J. Biol. Chem., 2006, 281, 8582-8590.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8582-8590
    • Kisselev, A.F.1    Callard, A.2    Goldberg, A.L.3
  • 78
    • 70349290496 scopus 로고    scopus 로고
    • Roles of P67/MetAP2 as a tumor suppressor
    • Datta, B. Roles of P67/MetAP2 as a tumor suppressor. Biochim. Biophys. Acta. 2009, 1796, 281-2892.
    • (2009) Biochim. Biophys. Acta. , vol.1796 , pp. 281-2892
    • Datta, B.1
  • 79
    • 13044300888 scopus 로고    scopus 로고
    • Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2
    • Griffith, E. C.; Su, Z.; Niwayama, S.; Ramsay, C. A.; Chang, Y. H.; Liu, J. O. Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2. Proc. Natl. Acad. Sci. USA, 1998, 95, 15183-15188.
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 15183-15188
    • Griffith, E.C.1    Su, Z.2    Niwayama, S.3    Ramsay, C.A.4    Chang, Y.H.5    Liu, J.O.6
  • 80
    • 1542274566 scopus 로고    scopus 로고
    • A single amino acid residue defines the difference in ovalicin sensitivity between type I and II methionine aminopeptidases
    • Brdlik, C. M.; Crews, C. M. A single amino acid residue defines the difference in ovalicin sensitivity between type I and II methionine aminopeptidases. J. Biol. Chem., 2004, 279, 9475-9480.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9475-9480
    • Brdlik, C.M.1    Crews, C.M.2
  • 81
    • 0038344159 scopus 로고    scopus 로고
    • Reactivity of functional groups on the protein surface: Development of epoxide probes for protein labeling
    • Chen, G.; Heim, A.; Riether, D.; Yee, D.; Milgrom, Y.; Gawinowicz, M. A.; Sames, D. Reactivity of functional groups on the protein surface: development of epoxide probes for protein labeling. J. Am. Chem. Soc., 2003, 125, 8130-8133.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8130-8133
    • Chen, G.1    Heim, A.2    Riether, D.3    Yee, D.4    Milgrom, Y.5    Gawinowicz, M.A.6    Sames, D.7
  • 82
    • 1842865013 scopus 로고    scopus 로고
    • Pladienolides, new substances from culture of Streptomyces platensis Mer-11107. III. In vitro and in vivo antitumor activities
    • Mizui, Y.; Sakai, T.; Iwata, M.; Uenaka, T.; Okamoto, K.; Shimizu, H.; Yamori, T.; Yoshimatsu, K.; Asada, M. Pladienolides, new substances from culture of Streptomyces platensis Mer-11107. III. In vitro and in vivo antitumor activities. J Antibiot. (Tokyo), 2004, 57, 188-196.
    • (2004) J Antibiot. (Tokyo) , vol.57 , pp. 188-196
    • Mizui, Y.1    Sakai, T.2    Iwata, M.3    Uenaka, T.4    Okamoto, K.5    Shimizu, H.6    Yamori, T.7    Yoshimatsu, K.8    Asada, M.9
  • 84
    • 73849090207 scopus 로고    scopus 로고
    • Identification and characterization of molecular targets of natural products by mass spectrometry
    • Cheng, K. W.; Wong, C. C.; Wang, M.; He, Q. Y.; Chen, F. Identification and characterization of molecular targets of natural products by mass spectrometry. Mass Spectrom. Rev., 29, 126-155.
    • Mass Spectrom. Rev. , vol.29 , pp. 126-155
    • Cheng, K.W.1    Wong, C.C.2    Wang, M.3    He, Q.Y.4    Chen, F.5
  • 86
    • 0041973445 scopus 로고    scopus 로고
    • Can an in silico drug-target search method be used to probe potential mechanisms of medicinal plant ingredients?
    • Chen, X.; Ung, C. Y.; Chen, Y. Can an in silico drug-target search method be used to probe potential mechanisms of medicinal plant ingredients? Nat. Prod. Rep., 2003, 20, 432-444.
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 432-444
    • Chen, X.1    Ung, C.Y.2    Chen, Y.3
  • 87
  • 90
    • 22244488279 scopus 로고    scopus 로고
    • Methionine aminopeptidases type I and type II are essential to control cell proliferation
    • Bernier, S. G.; Taghizadeh, N.; Thompson, C. D.; Westlin, W. F.; Hannig, G. Methionine aminopeptidases type I and type II are essential to control cell proliferation. J Cell Biochem., 2005, 95, 1191-1203.
    • (2005) J Cell Biochem , vol.95 , pp. 1191-1203
    • Bernier, S.G.1    Taghizadeh, N.2    Thompson, C.D.3    Westlin, W.F.4    Hannig, G.5


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