메뉴 건너뛰기




Volumn 7, Issue 5, 2005, Pages 457-468

Rational design of shepherdin, a novel anticancer agent

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; HEAT SHOCK PROTEIN 90; SHEPHERDIN; SURVIVIN; UNCLASSIFIED DRUG;

EID: 21144437911     PISSN: 15356108     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ccr.2005.03.035     Document Type: Article
Times cited : (308)

References (40)
  • 1
    • 0037267333 scopus 로고    scopus 로고
    • Validating survivin as a cancer therapeutic target
    • D.C. Altieri Validating survivin as a cancer therapeutic target Nat. Rev. Cancer 3 2003 46 54
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 46-54
    • Altieri, D.C.1
  • 2
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • A.D. Basso, D.B. Solit, P.N. Munster, and N. Rosen Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2 Oncogene 21 2002 1159 1166
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 3
    • 3242879188 scopus 로고    scopus 로고
    • "The stress of dying": The role of heat shock proteins in the regulation of apoptosis
    • H.M. Beere "The stress of dying": The role of heat shock proteins in the regulation of apoptosis J. Cell Sci. 117 2004 2641 2651
    • (2004) J. Cell Sci. , vol.117 , pp. 2641-2651
    • Beere, H.M.1
  • 4
    • 0029131395 scopus 로고
    • The retro-inverso form of a homeobox-derived short peptide is rapidly internalised by cultured neurones: A new basis for an efficient intracellular delivery system
    • J. Brugidou, C. Legrand, J. Mery, and A. Rabie The retro-inverso form of a homeobox-derived short peptide is rapidly internalised by cultured neurones: A new basis for an efficient intracellular delivery system Biochem. Biophys. Res. Commun. 214 1995 685 693
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 685-693
    • Brugidou, J.1    Legrand, C.2    Mery, J.3    Rabie, A.4
  • 6
    • 9644278114 scopus 로고    scopus 로고
    • Mitochondrial survivin inhibits apoptosis and promotes tumorigenesis
    • T. Dohi, E. Beltrami, N.R. Wall, J. Plescia, and D.C. Altieri Mitochondrial survivin inhibits apoptosis and promotes tumorigenesis J. Clin. Invest. 114 2004 1117 1127
    • (2004) J. Clin. Invest. , vol.114 , pp. 1117-1127
    • Dohi, T.1    Beltrami, E.2    Wall, N.R.3    Plescia, J.4    Altieri, D.C.5
  • 8
    • 0346336791 scopus 로고    scopus 로고
    • Survivin regulates hematopoietic progenitor cell proliferation through p21WAF1/Cip1-dependent and -independent pathways
    • S. Fukuda, C.R. Mantel, and L.M. Pelus Survivin regulates hematopoietic progenitor cell proliferation through p21WAF1/Cip1-dependent and -independent pathways Blood 103 2004 120 127
    • (2004) Blood , vol.103 , pp. 120-127
    • Fukuda, S.1    Mantel, C.R.2    Pelus, L.M.3
  • 10
    • 0342378184 scopus 로고    scopus 로고
    • On the immunogenic properties of retro-inverso peptides. Total retro-inversion of T-cell epitopes causes a loss of binding to MHC II molecules
    • M. Herve, B. Maillere, G. Mourier, C. Texier, S. Leroy, and A. Menez On the immunogenic properties of retro-inverso peptides. Total retro-inversion of T-cell epitopes causes a loss of binding to MHC II molecules Mol. Immunol. 34 1997 157 163
    • (1997) Mol. Immunol. , vol.34 , pp. 157-163
    • Herve, M.1    Maillere, B.2    Mourier, G.3    Texier, C.4    Leroy, S.5    Menez, A.6
  • 12
    • 0344418718 scopus 로고    scopus 로고
    • Effect of D-amino acid substitution on the stability, the secondary structure, and the activity of membrane-active peptide
    • S.Y. Hong, J.E. Oh, and K.H. Lee Effect of D-amino acid substitution on the stability, the secondary structure, and the activity of membrane-active peptide Biochem. Pharmacol. 58 1999 1775 1780
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 1775-1780
    • Hong, S.Y.1    Oh, J.E.2    Lee, K.H.3
  • 13
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • J.S. Isaacs, W. Xu, and L. Neckers Heat shock protein 90 as a molecular target for cancer therapeutics Cancer Cell 3 2003 213 217
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 14
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • R.W. Johnstone, A.A. Ruefli, and S.W. Lowe Apoptosis: A link between cancer genetics and chemotherapy Cell 108 2002 153 164
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 15
    • 0142155259 scopus 로고    scopus 로고
    • Biological applications of protein transduction technology
    • P.S. Kabouridis Biological applications of protein transduction technology Trends Biotechnol. 21 2003 498 503
    • (2003) Trends Biotechnol. , vol.21 , pp. 498-503
    • Kabouridis, P.S.1
  • 16
  • 17
    • 3242893125 scopus 로고    scopus 로고
    • Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin
    • Y.S. Lee, M.G. Marcu, and L. Neckers Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin Chem. Biol. 11 2004 991 998
    • (2004) Chem. Biol. , vol.11 , pp. 991-998
    • Lee, Y.S.1    Marcu, M.G.2    Neckers, L.3
  • 19
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • M.G. Marcu, A. Chadli, I. Bouhouche, M. Catelli, and L.M. Neckers The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone J. Biol. Chem. 275 2000 37181 37186
    • (2000) J. Biol. Chem. , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 20
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions
    • P. Meyer, C. Prodromou, B. Hu, C. Vaughan, S.M. Roe, B. Panaretou, P.W. Piper, and L.H. Pearl Structural and functional analysis of the middle segment of hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions Mol. Cell 11 2003 647 658
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 21
    • 0034674783 scopus 로고    scopus 로고
    • Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket
    • Y. Morishima, P.J. Murphy, D.P. Li, E.R. Sanchez, and W.B. Pratt Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket J. Biol. Chem. 275 2000 18054 18060
    • (2000) J. Biol. Chem. , vol.275 , pp. 18054-18060
    • Morishima, Y.1    Murphy, P.J.2    Li, D.P.3    Sanchez, E.R.4    Pratt, W.B.5
  • 22
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a lamarckian genetic algorithm and empirical binding free energy function
    • G.M. Morris, D.S. Goodsell, R.S. Halliday, R. Huey, W.E. Hart, R.K. Belew, and A.J. Olson Automated docking using a lamarckian genetic algorithm and empirical binding free energy function J Comp Chem 19 1998 1639 1662
    • (1998) J Comp 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
  • 25
    • 0034584880 scopus 로고    scopus 로고
    • STI571: An inhibitor of the BCR-ABL tyrosine kinase for the treatment of chronic myelogenous leukaemia
    • M.E. O'Dwyer, and B.J. Druker STI571: An inhibitor of the BCR-ABL tyrosine kinase for the treatment of chronic myelogenous leukaemia Lancet Oncol. 1 2000 207 211
    • (2000) Lancet Oncol. , vol.1 , pp. 207-211
    • O'Dwyer, M.E.1    Druker, B.J.2
  • 26
    • 3543092021 scopus 로고    scopus 로고
    • Pathways of apoptotic and non-apoptotic death in tumour cells
    • H. Okada, and T.W. Mak Pathways of apoptotic and non-apoptotic death in tumour cells Nat. Rev. Cancer 4 2004 592 603
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 592-603
    • Okada, H.1    Mak, T.W.2
  • 28
    • 0035227317 scopus 로고    scopus 로고
    • A retro-inverso peptide homologous to helix 1 of c-Myc is a potent and specific inhibitor of proliferation in different cellular systems
    • M.P. Pescarolo, L. Bagnasco, D. Malacarne, A. Melchiori, P. Valente, E. Millo, S. Bruno, S. Basso, and S. Parodi A retro-inverso peptide homologous to helix 1 of c-Myc is a potent and specific inhibitor of proliferation in different cellular systems FASEB J. 15 2001 31 33
    • (2001) FASEB J. , vol.15 , pp. 31-33
    • Pescarolo, M.P.1    Bagnasco, L.2    Malacarne, D.3    Melchiori, A.4    Valente, P.5    Millo, E.6    Bruno, S.7    Basso, S.8    Parodi, S.9
  • 31
  • 32
    • 0037386258 scopus 로고    scopus 로고
    • Cytoprotective membrane-permeable peptides designed from the Bax-binding domain of Ku70
    • M. Sawada, P. Hayes, and S. Matsuyama Cytoprotective membrane-permeable peptides designed from the Bax-binding domain of Ku70 Nat. Cell Biol. 5 2003 352 357
    • (2003) Nat. Cell Biol. , vol.5 , pp. 352-357
    • Sawada, M.1    Hayes, P.2    Matsuyama, S.3
  • 34
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • C.E. Stebbins, A.A. Russo, C. Schneider, N. Rosen, F.U. Hartl, and N.P. Pavletich Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent Cell 89 1997 239 250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 35
    • 0347917093 scopus 로고    scopus 로고
    • Cell-cycle targeted therapies
    • C. Swanton Cell-cycle targeted therapies Lancet Oncol. 5 2004 27 36
    • (2004) Lancet Oncol. , vol.5 , pp. 27-36
    • Swanton, C.1
  • 38
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • B. Vogelstein, and K.W. Kinzler Cancer genes and the pathways they control Nat. Med. 10 2004 789 799
    • (2004) Nat. Med. , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 40
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • J.C. Young, I. Moarefi, and F.U. Hartl Hsp90: A specialized but essential protein-folding tool J. Cell Biol. 154 2001 267 273
    • (2001) J. Cell Biol. , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.