메뉴 건너뛰기




Volumn 23, Issue 12, 2012, Pages 1617-1626

Sulforaphane inhibits pancreatic cancer through disrupting Hsp90-p50Cdc37 complex and direct interactions with amino acids residues of Hsp90

Author keywords

Hsp90; NMR; P50Cdc37; Pancreatic cancer; Sulforaphane

Indexed keywords

CELL CYCLE PROTEIN 37; HEAT SHOCK PROTEIN 90; SULFORAPHANE;

EID: 84869090566     PISSN: 09552863     EISSN: 18734847     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2011.11.004     Document Type: Article
Times cited : (53)

References (49)
  • 1
    • 51349088974 scopus 로고    scopus 로고
    • Multi-targeted prevention of cancer by sulforaphane
    • Clarke J.D., Dashwood R.H., Ho E. Multi-targeted prevention of cancer by sulforaphane. Cancer Lett 2008, 269:291-304.
    • (2008) Cancer Lett , vol.269 , pp. 291-304
    • Clarke, J.D.1    Dashwood, R.H.2    Ho, E.3
  • 2
    • 24944480252 scopus 로고    scopus 로고
    • Phenethyl isothiocyanate and sulforaphane and their N-acetylcysteine conjugates inhibit malignant progression of lung adenomas induced by tobacco carcinogens in A/J mice
    • Conaway C.C., Wang C.X., Pittman B., et al. Phenethyl isothiocyanate and sulforaphane and their N-acetylcysteine conjugates inhibit malignant progression of lung adenomas induced by tobacco carcinogens in A/J mice. Cancer Res 2005, 65:8548-8557.
    • (2005) Cancer Res , vol.65 , pp. 8548-8557
    • Conaway, C.C.1    Wang, C.X.2    Pittman, B.3
  • 3
    • 0030931522 scopus 로고    scopus 로고
    • Broccoli sprouts: an exceptionally rich source of inducers of enzymes that protect against chemical carcinogens
    • Fahey J.W., Zhang Y., Talalay P. Broccoli sprouts: an exceptionally rich source of inducers of enzymes that protect against chemical carcinogens. Proc Natl Acad Sci U S A 1997, 94:10367-10372.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10367-10372
    • Fahey, J.W.1    Zhang, Y.2    Talalay, P.3
  • 4
    • 77951730125 scopus 로고    scopus 로고
    • Sulforaphane, a dietary component of broccoli/broccoli sprouts, inhibits breast cancer stem cells
    • Li Y., Zhang T., Korkaya H., et al. Sulforaphane, a dietary component of broccoli/broccoli sprouts, inhibits breast cancer stem cells. Clin Cancer Res 2010, 16:2580-2590.
    • (2010) Clin Cancer Res , vol.16 , pp. 2580-2590
    • Li, Y.1    Zhang, T.2    Korkaya, H.3
  • 5
    • 34247606510 scopus 로고    scopus 로고
    • Molecular basis for chemoprevention by sulforaphane: a comprehensive review
    • Juge N., Mithen R.F., Traka M. Molecular basis for chemoprevention by sulforaphane: a comprehensive review. Cell Mol Life Sci 2007, 64:1105-1127.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1105-1127
    • Juge, N.1    Mithen, R.F.2    Traka, M.3
  • 6
    • 34548445866 scopus 로고    scopus 로고
    • Discovery and development of sulforaphane as a cancer chemopreventive phytochemical
    • Zhang Y., Tang L. Discovery and development of sulforaphane as a cancer chemopreventive phytochemical. Acta Pharmacol Sin 2007, 28:1343-1354.
    • (2007) Acta Pharmacol Sin , vol.28 , pp. 1343-1354
    • Zhang, Y.1    Tang, L.2
  • 7
    • 33846798049 scopus 로고    scopus 로고
    • Antiproliferative activity of sulforaphane in Akt-overexpressing ovarian cancer cells
    • Chaudhuri D., Orsulic S., Ashok B.T. Antiproliferative activity of sulforaphane in Akt-overexpressing ovarian cancer cells. Mol Cancer Ther 2007, 6:334-345.
    • (2007) Mol Cancer Ther , vol.6 , pp. 334-345
    • Chaudhuri, D.1    Orsulic, S.2    Ashok, B.T.3
  • 8
    • 70349741087 scopus 로고    scopus 로고
    • Sulforaphane destabilizes the androgen receptor in prostate cancer cells by inactivating histone deacetylase 6
    • Gibbs A., Schwartzman J., Deng V., Alumkal J. Sulforaphane destabilizes the androgen receptor in prostate cancer cells by inactivating histone deacetylase 6. Proc Natl Acad Sci U S A 2009, 106:16663-16668.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16663-16668
    • Gibbs, A.1    Schwartzman, J.2    Deng, V.3    Alumkal, J.4
  • 9
    • 67651165192 scopus 로고    scopus 로고
    • D,l-Sulforaphane causes transcriptional repression of androgen receptor in human prostate cancer cells
    • Kim S.H., Singh S.V. d,l-Sulforaphane causes transcriptional repression of androgen receptor in human prostate cancer cells. Mol Cancer Ther 2009, 8:1946-1954.
    • (2009) Mol Cancer Ther , vol.8 , pp. 1946-1954
    • Kim, S.H.1    Singh, S.V.2
  • 10
    • 49749150144 scopus 로고    scopus 로고
    • Sulforaphane inhibited expression of hypoxia-inducible factor-1alpha in human tongue squamous cancer cells and prostate cancer cells
    • Yao H., Wang H., Zhang Z., Jiang B.H., Luo J., Shi X. Sulforaphane inhibited expression of hypoxia-inducible factor-1alpha in human tongue squamous cancer cells and prostate cancer cells. Int J Cancer 2008, 123:1255-1261.
    • (2008) Int J Cancer , vol.123 , pp. 1255-1261
    • Yao, H.1    Wang, H.2    Zhang, Z.3    Jiang, B.H.4    Luo, J.5    Shi, X.6
  • 11
    • 59449107850 scopus 로고    scopus 로고
    • Targeting CDC37: an alternative, kinase-directed strategy for disruption of oncogenic chaperoning
    • Smith J.R., Workman P. Targeting CDC37: an alternative, kinase-directed strategy for disruption of oncogenic chaperoning. Cell Cycle 2009, 8:362-372.
    • (2009) Cell Cycle , vol.8 , pp. 362-372
    • Smith, J.R.1    Workman, P.2
  • 12
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of Hsp90 activation
    • Kamal A., Boehm M.F., Burrows F.J. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol Med 2004, 10:283-290.
    • (2004) Trends Mol Med , vol.10 , pp. 283-290
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 13
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L., Lindquist S.L. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005, 5:761-772.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 14
    • 79551666466 scopus 로고    scopus 로고
    • N-terminal domain of human Hsp90 triggers binding to the cochaperone p23
    • Karagoz G.E., Duarte A.M., Ippel H., et al. N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proc Natl Acad Sci U S A 2011, 108:580-585.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 580-585
    • Karagoz, G.E.1    Duarte, A.M.2    Ippel, H.3
  • 15
    • 3943074512 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins
    • Tugarinov V., Hwang P.M., Kay L.E. Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annu Rev Biochem 2004, 73:107-146.
    • (2004) Annu Rev Biochem , vol.73 , pp. 107-146
    • Tugarinov, V.1    Hwang, P.M.2    Kay, L.E.3
  • 16
    • 3042604470 scopus 로고    scopus 로고
    • Characterization of mutations and loss of heterozygosity of p53 and K-ras2 in pancreatic cancer cell lines by immobilized polymerase chain reaction
    • Butz J., Wickstrom E., Edwards J. Characterization of mutations and loss of heterozygosity of p53 and K-ras2 in pancreatic cancer cell lines by immobilized polymerase chain reaction. BMC Biotechnol 2003, 3:11.
    • (2003) BMC Biotechnol , vol.3 , pp. 11
    • Butz, J.1    Wickstrom, E.2    Edwards, J.3
  • 17
    • 0036249661 scopus 로고    scopus 로고
    • Influence of p53 status on radiation and 5-flourouracil synergy in pancreatic cancer cells
    • Mohiuddin M., Chendil D., Dey S., Alcock R.A., Regine W., Ahmed M.M. Influence of p53 status on radiation and 5-flourouracil synergy in pancreatic cancer cells. Anticancer Res 2002, 22:825-830.
    • (2002) Anticancer Res , vol.22 , pp. 825-830
    • Mohiuddin, M.1    Chendil, D.2    Dey, S.3    Alcock, R.A.4    Regine, W.5    Ahmed, M.M.6
  • 18
    • 0037038684 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitor (L-744,832) restores TGF-beta type II receptor expression and enhances radiation sensitivity in K-ras mutant pancreatic cancer cell line MIA PaCa-2
    • Alcock R.A., Dey S., Chendil D., et al. Farnesyltransferase inhibitor (L-744,832) restores TGF-beta type II receptor expression and enhances radiation sensitivity in K-ras mutant pancreatic cancer cell line MIA PaCa-2. Oncogene 2002, 21:7883-7890.
    • (2002) Oncogene , vol.21 , pp. 7883-7890
    • Alcock, R.A.1    Dey, S.2    Chendil, D.3
  • 19
    • 0037265586 scopus 로고    scopus 로고
    • Development of small molecule Hsp90 inhibitors: utilizing both forward and reverse chemical genomics for drug identification
    • Neckers L. Development of small molecule Hsp90 inhibitors: utilizing both forward and reverse chemical genomics for drug identification. Curr Med Chem 2003, 10:733-739.
    • (2003) Curr Med Chem , vol.10 , pp. 733-739
    • Neckers, L.1
  • 20
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • Bertelsen E.B., Chang L., Gestwicki J.E., Zuiderweg E.R. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci U S A 2009, 106:8471-8476.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.4
  • 21
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers R., Kay L.E. Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 2007, 445:618-622.
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 24
    • 0026334753 scopus 로고
    • Abnormalities of the p53 tumour suppressor gene in human pancreatic cancer
    • Barton C.M., Staddon S.L., Hughes C.M., et al. Abnormalities of the p53 tumour suppressor gene in human pancreatic cancer. Br J Cancer 1991, 64:1076-1082.
    • (1991) Br J Cancer , vol.64 , pp. 1076-1082
    • Barton, C.M.1    Staddon, S.L.2    Hughes, C.M.3
  • 25
    • 0348049845 scopus 로고    scopus 로고
    • Incidence, mechanism and prognostic value of activated AKT in pancreas cancer
    • Schlieman M.G., Fahy B.N., Ramsamooj R., Beckett L., Bold R.J. Incidence, mechanism and prognostic value of activated AKT in pancreas cancer. Br J Cancer 2003, 89:2110-2115.
    • (2003) Br J Cancer , vol.89 , pp. 2110-2115
    • Schlieman, M.G.1    Fahy, B.N.2    Ramsamooj, R.3    Beckett, L.4    Bold, R.J.5
  • 26
    • 0024292722 scopus 로고
    • Most human carcinomas of the exocrine pancreas contain mutant c-K-ras genes
    • Almoguera C., Shibata D., Forrester K., Martin J., Arnheim N., Perucho M. Most human carcinomas of the exocrine pancreas contain mutant c-K-ras genes. Cell 1988, 53:549-554.
    • (1988) Cell , vol.53 , pp. 549-554
    • Almoguera, C.1    Shibata, D.2    Forrester, K.3    Martin, J.4    Arnheim, N.5    Perucho, M.6
  • 27
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco I., Sawyers C.L. The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat Rev Cancer 2002, 2:489-501.
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 28
    • 34249335357 scopus 로고    scopus 로고
    • Phosphoinositide-3-kinase signaling controls S-phase kinase-associated protein 2 transcription via E2F1 in pancreatic ductal adenocarcinoma cells
    • Reichert M., Saur D., Hamacher R., Schmid R.M., Schneider G. Phosphoinositide-3-kinase signaling controls S-phase kinase-associated protein 2 transcription via E2F1 in pancreatic ductal adenocarcinoma cells. Cancer Res 2007, 67:4149-4156.
    • (2007) Cancer Res , vol.67 , pp. 4149-4156
    • Reichert, M.1    Saur, D.2    Hamacher, R.3    Schmid, R.M.4    Schneider, G.5
  • 29
    • 1542353932 scopus 로고    scopus 로고
    • Frequent activation of AKT2 kinase in human pancreatic carcinomas
    • Altomare D.A., Tanno S., De Rienzo A., et al. Frequent activation of AKT2 kinase in human pancreatic carcinomas. J Cell Biochem 2002, 87:470-476.
    • (2002) J Cell Biochem , vol.87 , pp. 470-476
    • Altomare, D.A.1    Tanno, S.2    De Rienzo, A.3
  • 30
    • 0037518134 scopus 로고    scopus 로고
    • Absorption/metabolism of sulforaphane and quercetin, and regulation of phase II enzymes, in human jejunum in vivo
    • Petri N., Tannergren C., Holst B., et al. Absorption/metabolism of sulforaphane and quercetin, and regulation of phase II enzymes, in human jejunum in vivo. Drug Metab Dispos 2003, 31:805-813.
    • (2003) Drug Metab Dispos , vol.31 , pp. 805-813
    • Petri, N.1    Tannergren, C.2    Holst, B.3
  • 31
    • 0036135910 scopus 로고    scopus 로고
    • Quantitative determination of dithiocarbamates in human plasma, serum, erythrocytes and urine: pharmacokinetics of broccoli sprout isothiocyanates in humans
    • Ye L., Dinkova-Kostova A.T., Wade K.L., Zhang Y., Shapiro T.A., Talalay P. Quantitative determination of dithiocarbamates in human plasma, serum, erythrocytes and urine: pharmacokinetics of broccoli sprout isothiocyanates in humans. Clin Chim Acta 2002, 316:43-53.
    • (2002) Clin Chim Acta , vol.316 , pp. 43-53
    • Ye, L.1    Dinkova-Kostova, A.T.2    Wade, K.L.3    Zhang, Y.4    Shapiro, T.A.5    Talalay, P.6
  • 32
    • 33749165612 scopus 로고    scopus 로고
    • Safety, tolerance, and metabolism of broccoli sprout glucosinolates and isothiocyanates: a clinical phase I study
    • Shapiro T.A., Fahey J.W., Dinkova-Kostova A.T., et al. Safety, tolerance, and metabolism of broccoli sprout glucosinolates and isothiocyanates: a clinical phase I study. Nutr Cancer 2006, 55:53-62.
    • (2006) Nutr Cancer , vol.55 , pp. 53-62
    • Shapiro, T.A.1    Fahey, J.W.2    Dinkova-Kostova, A.T.3
  • 33
    • 28644450910 scopus 로고    scopus 로고
    • Effects of glucosinolate-rich broccoli sprouts on urinary levels of aflatoxin-DNA adducts and phenanthrene tetraols in a randomized clinical trial in He Zuo township, Qidong, People's Republic of China
    • Kensler T.W., Chen J.G., Egner P.A., et al. Effects of glucosinolate-rich broccoli sprouts on urinary levels of aflatoxin-DNA adducts and phenanthrene tetraols in a randomized clinical trial in He Zuo township, Qidong, People's Republic of China. Cancer Epidemiol Biomarkers Prev 2005, 14:2605-2613.
    • (2005) Cancer Epidemiol Biomarkers Prev , vol.14 , pp. 2605-2613
    • Kensler, T.W.1    Chen, J.G.2    Egner, P.A.3
  • 34
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 1997, 90:65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 35
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent
    • Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 1997, 89:239-250.
    • (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
  • 36
    • 35348890981 scopus 로고    scopus 로고
    • Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress
    • Workman P., Burrows F., Neckers L., Rosen N. Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann N Y Acad Sci 2007, 1113:202-216.
    • (2007) Ann N Y Acad Sci , vol.1113 , pp. 202-216
    • Workman, P.1    Burrows, F.2    Neckers, L.3    Rosen, N.4
  • 37
    • 33645975518 scopus 로고    scopus 로고
    • Chaperoning oncogenes: Hsp90 as a target of geldanamycin
    • Neckers L. Chaperoning oncogenes: Hsp90 as a target of geldanamycin. Handb Exp Pharmacol 2006, 259-277.
    • (2006) Handb Exp Pharmacol , pp. 259-277
    • Neckers, L.1
  • 38
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation
    • Whitesell L., Mimnaugh E.G., De Costa B., Myers C.E., Neckers L.M. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci U S A 1994, 91:8324-8328.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 39
    • 70350548428 scopus 로고    scopus 로고
    • 17 AAG for HSP90 inhibition in cancer - from bench to bedside
    • Usmani S.Z., Bona R., Li Z. 17 AAG for HSP90 inhibition in cancer - from bench to bedside. Curr Mol Med 2009, 9:654-664.
    • (2009) Curr Mol Med , vol.9 , pp. 654-664
    • Usmani, S.Z.1    Bona, R.2    Li, Z.3
  • 40
    • 38349153572 scopus 로고    scopus 로고
    • A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells
    • Zhang T., Hamza A., Cao X., et al. A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells. Mol Cancer Ther 2008, 7:162-170.
    • (2008) Mol Cancer Ther , vol.7 , pp. 162-170
    • Zhang, T.1    Hamza, A.2    Cao, X.3
  • 41
    • 71549153791 scopus 로고    scopus 로고
    • Withaferin A targets heat shock protein 90 in pancreatic cancer cells
    • Yu Y., Hamza A., Zhang T., et al. Withaferin A targets heat shock protein 90 in pancreatic cancer cells. Biochem Pharmacol 2009.
    • (2009) Biochem Pharmacol
    • Yu, Y.1    Hamza, A.2    Zhang, T.3
  • 42
    • 72149125851 scopus 로고    scopus 로고
    • Characterization of celastrol to inhibit HSP90 and CDC37 interaction
    • Zhang T., Li Y., Yu Y., Zou P., Jiang Y., Sun D. Characterization of celastrol to inhibit HSP90 and CDC37 interaction. J Biol Chem 2009.
    • (2009) J Biol Chem
    • Zhang, T.1    Li, Y.2    Yu, Y.3    Zou, P.4    Jiang, Y.5    Sun, D.6
  • 43
    • 0034125712 scopus 로고    scopus 로고
    • Role of glutathione in the accumulation of anticarcinogenic isothiocyanates and their glutathione conjugates by murine hepatoma cells
    • Zhang Y. Role of glutathione in the accumulation of anticarcinogenic isothiocyanates and their glutathione conjugates by murine hepatoma cells. Carcinogenesis 2000, 21:1175-1182.
    • (2000) Carcinogenesis , vol.21 , pp. 1175-1182
    • Zhang, Y.1
  • 44
    • 70149093188 scopus 로고    scopus 로고
    • Inhibition of activator protein-1 by sulforaphane involves interaction with cysteine in the cFos DNA-binding domain: implications for chemoprevention of UVB-induced skin cancer
    • Dickinson S.E., Melton T.F., Olson E.R., Zhang J., Saboda K., Bowden G.T. Inhibition of activator protein-1 by sulforaphane involves interaction with cysteine in the cFos DNA-binding domain: implications for chemoprevention of UVB-induced skin cancer. Cancer Res 2009, 69:7103-7110.
    • (2009) Cancer Res , vol.69 , pp. 7103-7110
    • Dickinson, S.E.1    Melton, T.F.2    Olson, E.R.3    Zhang, J.4    Saboda, K.5    Bowden, G.T.6
  • 45
    • 29644443964 scopus 로고    scopus 로고
    • Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane
    • Hong F., Freeman M.L., Liebler D.C. Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane. Chem Res Toxicol 2005, 18:1917-1926.
    • (2005) Chem Res Toxicol , vol.18 , pp. 1917-1926
    • Hong, F.1    Freeman, M.L.2    Liebler, D.C.3
  • 46
    • 0742269688 scopus 로고    scopus 로고
    • The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)
    • Roe S.M., Ali M.M., Meyer P., et al. The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 2004, 116:87-98.
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1    Ali, M.M.2    Meyer, P.3
  • 47
    • 77954219912 scopus 로고    scopus 로고
    • Split Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions
    • Jiang Y., Bernard D., Yu Y., et al. Split Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions. J Biol Chem 2010, 285:21023-21036.
    • (2010) J Biol Chem , vol.285 , pp. 21023-21036
    • Jiang, Y.1    Bernard, D.2    Yu, Y.3
  • 48
    • 52649133274 scopus 로고    scopus 로고
    • HDAC6 inhibition enhances 17-AAG-mediated abrogation of hsp90 chaperone function in human leukemia cells
    • Rao R., Fiskus W., Yang Y., et al. HDAC6 inhibition enhances 17-AAG-mediated abrogation of hsp90 chaperone function in human leukemia cells. Blood 2008, 112:1886-1893.
    • (2008) Blood , vol.112 , pp. 1886-1893
    • Rao, R.1    Fiskus, W.2    Yang, Y.3
  • 49
    • 80054731134 scopus 로고    scopus 로고
    • Identification of potential protein targets of isothiocyanates by proteomics
    • Mi L., Hood B.L., Stewart N.A., et al. Identification of potential protein targets of isothiocyanates by proteomics. Chem Res Toxicol 2011, 24:1735-1743.
    • (2011) Chem Res Toxicol , vol.24 , pp. 1735-1743
    • Mi, L.1    Hood, B.L.2    Stewart, N.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.