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Volumn 2015, Issue , 2015, Pages

HSP90 and HSP70: Implication in Inflammation Processes and Therapeutic Approaches for Myeloproliferative Neoplasms

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 70 INHIBITOR; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; UNCLASSIFIED DRUG; AUTACOID;

EID: 84946053539     PISSN: 09629351     EISSN: 14661861     Source Type: Journal    
DOI: 10.1155/2015/970242     Document Type: Review
Times cited : (66)

References (81)
  • 1
    • 20144363192 scopus 로고    scopus 로고
    • Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders
    • E. J. Baxter, L. M. Scott, P. J. Campbell et al., "Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders," The Lancet, vol. 365, no. 9464, pp. 1054-1061, 2005.
    • (2005) The Lancet , vol.365 , Issue.9464 , pp. 1054-1061
    • Baxter, E.J.1    Scott, L.M.2    Campbell, P.J.3
  • 2
    • 17844383458 scopus 로고    scopus 로고
    • A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera
    • C. James, V. Ugo, J.-P. Le Couédic et al., "A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera," Nature, vol. 434, no. 7037, pp. 1144-1148, 2005.
    • (2005) Nature , vol.434 , Issue.7037 , pp. 1144-1148
    • James, C.1    Ugo, V.2    Le Couédic, J.-P.3
  • 3
    • 9644275709 scopus 로고    scopus 로고
    • Molecular pathogenesis of Philadelphia chromosome negative myeloproliferative disorders
    • R. Kralovics and R. C. Skoda, "Molecular pathogenesis of Philadelphia chromosome negative myeloproliferative disorders," Blood Reviews, vol. 19, no. 1, pp. 1-13, 2005.
    • (2005) Blood Reviews , vol.19 , Issue.1 , pp. 1-13
    • Kralovics, R.1    Skoda, R.C.2
  • 4
    • 20244369569 scopus 로고    scopus 로고
    • Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, andmyeloidmetaplasia withmyelofibrosis
    • R. L. Levine, M. Wadleigh, J. Cools et al., "Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, andmyeloidmetaplasia withmyelofibrosis," Cancer Cell, vol. 7, no. 4, pp. 387-397, 2005.
    • (2005) Cancer Cell , vol.7 , Issue.4 , pp. 387-397
    • Levine, R.L.1    Wadleigh, M.2    Cools, J.3
  • 5
    • 77956670899 scopus 로고    scopus 로고
    • LNK mutations in JAK2 mutation-negative erythrocytosis
    • T. L. Lasho, A. Pardanani, and A. Tefferi, "LNK mutations in JAK2 mutation-negative erythrocytosis," The New England Journal of Medicine, vol. 363, no. 12, pp. 1189-1190, 2010.
    • (2010) The New England Journal of Medicine , vol.363 , Issue.12 , pp. 1189-1190
    • Lasho, T.L.1    Pardanani, A.2    Tefferi, A.3
  • 7
    • 79960210747 scopus 로고    scopus 로고
    • DNMT3A mutations in myeloproliferative neoplasms
    • F. Stegelmann, L. Bullinger, R. F. Schlenk et al., "DNMT3A mutations in myeloproliferative neoplasms," Leukemia, vol. 25, no. 7, pp. 1217-1219, 2011.
    • (2011) Leukemia , vol.25 , Issue.7 , pp. 1217-1219
    • Stegelmann, F.1    Bullinger, L.2    Schlenk, R.F.3
  • 8
    • 34250561475 scopus 로고
    • Anewpuffing pattern induced by temperature shock and DNP in Drosophila
    • F. Ritossa, "Anewpuffing pattern induced by temperature shock and DNP in Drosophila," Experientia, vol. 18, no. 12, pp. 571-573, 1962.
    • (1962) Experientia , vol.18 , Issue.12 , pp. 571-573
    • Ritossa, F.1
  • 10
    • 0030025526 scopus 로고    scopus 로고
    • Heat shock proteins: Applications in health and disease
    • S. Jindal, "Heat shock proteins: applications in health and disease," Trends in Biotechnology, vol. 14, no. 1, pp. 17-20, 1996.
    • (1996) Trends in Biotechnology , vol.14 , Issue.1 , pp. 17-20
    • Jindal, S.1
  • 13
    • 42149128194 scopus 로고    scopus 로고
    • Interaction of heatshock protein 90β isoform (HSP90β) with cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell differentiation
    • C. Didelot, D. Lanneau, M. Brunet et al., "Interaction of heatshock protein 90β isoform (HSP90β) with cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell differentiation," Cell Death and Differentiation, vol. 15, no. 5, pp. 859-866, 2008.
    • (2008) Cell Death and Differentiation , vol.15 , Issue.5 , pp. 859-866
    • Didelot, C.1    Lanneau, D.2    Brunet, M.3
  • 14
    • 84905674542 scopus 로고    scopus 로고
    • Dual regulation of SPI1/PU.1 transcription factor by heat shock factor 1 (HSF1) during macrophage differentiation of monocytes
    • G. Jego, D. Lanneau, A. De Thonel et al., "Dual regulation of SPI1/PU.1 transcription factor by heat shock factor 1 (HSF1) during macrophage differentiation of monocytes," Leukemia, vol. 28, no. 8, pp. 1676-1686, 2014.
    • (2014) Leukemia , vol.28 , Issue.8 , pp. 1676-1686
    • Jego, G.1    Lanneau, D.2    De Thonel, A.3
  • 15
    • 18244401639 scopus 로고    scopus 로고
    • Loss of Hspa9b in zebrafish recapitulates the ineffective hematopoiesis of the myelodysplastic syndrome
    • S. E. Craven, D. French, W. Ye, F. De Sauvage, and A. Rosenthal, "Loss of Hspa9b in zebrafish recapitulates the ineffective hematopoiesis of the myelodysplastic syndrome," Blood, vol. 105, no. 9, pp. 3528-3534, 2005.
    • (2005) Blood , vol.105 , Issue.9 , pp. 3528-3534
    • Craven, S.E.1    French, D.2    Ye, W.3    De Sauvage, F.4    Rosenthal, A.5
  • 16
    • 33846087085 scopus 로고    scopus 로고
    • Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1
    • J.-A. Ribeil, Y. Zermati, J. Vandekerckhove et al., "Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1," Nature, vol. 445, no. 7123, pp. 102-105, 2007.
    • (2007) Nature , vol.445 , Issue.7123 , pp. 102-105
    • Ribeil, J.-A.1    Zermati, Y.2    Vandekerckhove, J.3
  • 17
    • 77955877483 scopus 로고    scopus 로고
    • HSP27 controls GATA- 1 protein level during erythroid cell differentiation
    • A. de Thonel, J. Vandekerckhove, D. Lanneau et al., "HSP27 controls GATA- 1 protein level during erythroid cell differentiation," Blood, vol. 116, no. 1, pp. 85-96, 2010.
    • (2010) Blood , vol.116 , Issue.1 , pp. 85-96
    • De Thonel, A.1    Vandekerckhove, J.2    Lanneau, D.3
  • 18
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • W. B. Pratt and D. O. Toft, "Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery," Experimental Biology and Medicine, vol. 228, no. 2, pp. 111-133, 2003.
    • (2003) Experimental Biology and Medicine , vol.228 , Issue.2 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 19
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • L. Whitesell and S. L. Lindquist, "HSP90 and the chaperoning of cancer," Nature Reviews Cancer, vol. 5, no. 10, pp. 761-772, 2005.
    • (2005) Nature Reviews Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 20
    • 0032403161 scopus 로고    scopus 로고
    • Abundance of heat shock proteins (hsp89, hsp60, and hsp27) in malignant cells of Hodgkin's disease
    • P.-L. Hsu and S.-M. Hsu, "Abundance of heat shock proteins (hsp89, hsp60, and hsp27) in malignant cells of Hodgkin's disease," Cancer Research, vol. 58, no. 23, pp. 5507-5513, 1998.
    • (1998) Cancer Research , vol.58 , Issue.23 , pp. 5507-5513
    • Hsu, P.-L.1    Hsu, S.-M.2
  • 21
    • 2442695516 scopus 로고    scopus 로고
    • Cotreatment with 17-allylamino-demethoxygeldanamycin and FLT-3 kinase inhibitor PKC412 is highly effective against human acute myelogenous leukemia cells with mutant FLT-3
    • P. George, P. Bali, P. Cohen et al., "Cotreatment with 17-allylamino-demethoxygeldanamycin and FLT-3 kinase inhibitor PKC412 is highly effective against human acute myelogenous leukemia cells with mutant FLT-3," Cancer Research, vol. 64, no. 10, pp. 3645-3652, 2004.
    • (2004) Cancer Research , vol.64 , Issue.10 , pp. 3645-3652
    • George, P.1    Bali, P.2    Cohen, P.3
  • 22
    • 33644871636 scopus 로고    scopus 로고
    • The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferons
    • L. Shang and T. B. Tomasi, "The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferons," The Journal of Biological Chemistry, vol. 281, no. 4, pp. 1876-1884, 2006.
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 1876-1884
    • Shang, L.1    Tomasi, T.B.2
  • 23
    • 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
    • L. Whitesell, E. G. Mimnaugh, B. De Costa, C. E. Myers, and L. M. Neckers, "Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation," Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 18, pp. 8324-8328, 1994.
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.18 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 24
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of Hsp90 function results in degradation of the death domain kinase, receptorinteracting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-κB activation
    • J. Lewis, A. Devin, A. Miller et al., "Disruption of Hsp90 function results in degradation of the death domain kinase, receptorinteracting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-κB activation," The Journal of Biological Chemistry, vol. 275, no. 14, pp. 10519-10526, 2000.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3
  • 25
    • 77953446392 scopus 로고    scopus 로고
    • Dual role of heat shock proteins as regulators of apoptosis and innate immunity
    • A.-L. Joly, G. Wettstein, G. Mignot, F. Ghiringhelli, and C. Garrido, "Dual role of heat shock proteins as regulators of apoptosis and innate immunity," Journal of Innate Immunity, vol. 2, no. 3, pp. 238-247, 2010.
    • (2010) Journal of Innate Immunity , vol.2 , Issue.3 , pp. 238-247
    • Joly, A.-L.1    Wettstein, G.2    Mignot, G.3    Ghiringhelli, F.4    Garrido, C.5
  • 26
    • 0034713335 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits caspase-dependent and -independent apoptosis in Jurkat T cells
    • E.M. Creagh, R. J. Carmody, and T.G. Cotter, "Heat shock protein 70 inhibits caspase-dependent and -independent apoptosis in Jurkat T cells," Experimental Cell Research, vol. 257, no. 1, pp. 58-66, 2000.
    • (2000) Experimental Cell Research , vol.257 , Issue.1 , pp. 58-66
    • Creagh, E.M.1    Carmody, R.J.2    Cotter, T.G.3
  • 27
    • 10744227948 scopus 로고    scopus 로고
    • Chemosensitization by a non-apoptogenic heat shock protein 70-binding apoptosis-inducing factormutant
    • E. Schmitt, A. Parcellier, S. Gurbuxani et al., "Chemosensitization by a non-apoptogenic heat shock protein 70-binding apoptosis-inducing factormutant," Cancer Research, vol. 63, no. 23, pp. 8233-8240, 2003.
    • (2003) Cancer Research , vol.63 , Issue.23 , pp. 8233-8240
    • Schmitt, E.1    Parcellier, A.2    Gurbuxani, S.3
  • 28
    • 0031708908 scopus 로고    scopus 로고
    • Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy
    • L. M. Vargas-Roig, F. E. Gago, O. Tello, J. C. Aznar, and D. R. Ciocca, "Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy," International Journal of Cancer, vol. 79, no. 5, pp. 468-475, 1998.
    • (1998) International Journal of Cancer , vol.79 , Issue.5 , pp. 468-475
    • Vargas-Roig, L.M.1    Gago, F.E.2    Tello, O.3    Aznar, J.C.4    Ciocca, D.R.5
  • 29
    • 16644362403 scopus 로고    scopus 로고
    • Radioresistance is associated to increased Hsp70 content in human glioblastoma cell lines
    • A. Brondani Da Rocha, A. Regner, I. Grivicich et al., "Radioresistance is associated to increased Hsp70 content in human glioblastoma cell lines," International Journal of Oncology, vol. 25, no. 3, pp. 777-785, 2004.
    • (2004) International Journal of Oncology , vol.25 , Issue.3 , pp. 777-785
    • Brondani Da-Rocha, A.1    Regner, A.2    Grivicich, I.3
  • 30
    • 4143151967 scopus 로고    scopus 로고
    • Genomic mechanisms of p210BCR-ABL signaling: Induction of heat shock protein 70 through the GATA response element confers resistance to paclitaxel-induced apoptosis
    • S. Ray, Y. Lu, S. H. Kaufmann et al., "Genomic mechanisms of p210BCR-ABL signaling: induction of heat shock protein 70 through the GATA response element confers resistance to paclitaxel-induced apoptosis," Journal of Biological Chemistry, vol. 279, no. 34, pp. 35604-35615, 2004.
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35604-35615
    • Ray, S.1    Lu, Y.2    Kaufmann, S.H.3
  • 31
    • 84887656542 scopus 로고    scopus 로고
    • Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera?
    • article
    • M. Gallardo, S. Barrio, M. Fernandez et al., "Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera," Molecular Cancer, vol. 12, article 142, 2013.
    • (2013) Molecular Cancer , vol.12
    • Gallardo, M.1    Barrio, S.2    Fernandez, M.3
  • 32
    • 19944433616 scopus 로고    scopus 로고
    • Mechanistic role of heat shock protein 70 in Bcr-Abl-mediated resistance to apoptosis in human acute leukemia cells
    • F. Guo, C. Sigua, P. Bali et al., "Mechanistic role of heat shock protein 70 in Bcr-Abl-mediated resistance to apoptosis in human acute leukemia cells," Apoptosis, vol. 105, no. 3, pp. 1246-1255, 2005.
    • (2005) Apoptosis , vol.105 , Issue.3 , pp. 1246-1255
    • Guo, F.1    Sigua, C.2    Bali, P.3
  • 33
    • 84876084273 scopus 로고    scopus 로고
    • Targeting heat shock proteins in cancer
    • G. Jego, A. Hazoumé, R. Seigneuric, and C. Garrido, "Targeting heat shock proteins in cancer," Cancer Letters, vol. 332, no. 2, pp. 275-285, 2013.
    • (2013) Cancer Letters , vol.332 , Issue.2 , pp. 275-285
    • Jego, G.1    Hazoumé, A.2    Seigneuric, R.3    Garrido, C.4
  • 35
    • 0029056501 scopus 로고
    • Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent
    • J. G. Supko, R. L. Hickman, M. R. Grever, and L. Malspeis, "Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent," Cancer Chemotherapy and Pharmacology, vol. 36, no. 4, pp. 305-315, 1995.
    • (1995) Cancer Chemotherapy and Pharmacology , vol.36 , Issue.4 , pp. 305-315
    • Supko, J.G.1    Hickman, R.L.2    Grever, M.R.3    Malspeis, L.4
  • 37
    • 77950929054 scopus 로고    scopus 로고
    • Phase I study of the heat shock protein 90 inhibitor alvespimycin (KOS-1022, 17-DMAG) administered intravenously twice weekly to patients with acute myeloid leukemia
    • J. E. Lancet, I. Gojo, M. Burton et al., "Phase I study of the heat shock protein 90 inhibitor alvespimycin (KOS-1022, 17-DMAG) administered intravenously twice weekly to patients with acute myeloid leukemia," Leukemia, vol. 24, no. 4, pp. 699-705, 2010.
    • (2010) Leukemia , vol.24 , Issue.4 , pp. 699-705
    • Lancet, J.E.1    Gojo, I.2    Burton, M.3
  • 38
    • 0001251439 scopus 로고
    • A new antifungal substance of fungal origin?
    • article
    • P. Delmotte and J. Delmotte-Plaquee, "A new antifungal substance of fungal origin," Nature, vol. 171, no. 4347, article 344, 1953.
    • (1953) Nature , vol.171 , Issue.4347
    • Delmotte, P.1    Delmotte-Plaquee, J.2
  • 39
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • T. W. Schulte, S. Akinaga, S. Soga et al., "Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin," Cell Stress&Chaperones, vol. 3, no. 2, pp. 100-108, 1998.
    • (1998) Cell Stress&Chaperones , vol.3 , Issue.2 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3
  • 40
    • 38349157746 scopus 로고    scopus 로고
    • 4,5-diarylisoxazole Hsp90 chaperone inhibitors: Potential therapeutic agents for the treatment of cancer
    • P. A. Brough, W. Aherne, X. Barril et al., "4,5-Diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer," Journal of Medicinal Chemistry, vol. 51, no. 2, pp. 196-218, 2008.
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.2 , pp. 196-218
    • Brough, P.A.1    Aherne, W.2    Barril, X.3
  • 41
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • G. Chiosis, M. N. Timaul, B. Lucas et al., "A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells," Chemistry and Biology, vol. 8, no. 3, pp. 289-299, 2001.
    • (2001) Chemistry and Biology , vol.8 , Issue.3 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3
  • 42
    • 66249138886 scopus 로고    scopus 로고
    • Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models
    • E. Caldas-Lopes, L. Cerchietti, J.H. Ahn et al., "Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models," Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 20, pp. 8368-8373, 2009.
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , Issue.20 , pp. 8368-8373
    • Caldas-Lopes, E.1    Cerchietti, L.2    Ahn, J.H.3
  • 43
    • 77957374909 scopus 로고    scopus 로고
    • The novel Hsp-90 inhibitor SNX7081 is significantly more potent than 17-AAG against primary CLL cells and a range of haematological cell lines, irrespective of lesions in the TP53 pathway
    • O.G. Best, N. Singh, C. Forsyth, and S. P. Mulligan, "The novel Hsp-90 inhibitor SNX7081 is significantly more potent than 17-AAG against primary CLL cells and a range of haematological cell lines, irrespective of lesions in the TP53 pathway," British Journal of Haematology, vol. 151, no. 2, pp. 185-188, 2010.
    • (2010) British Journal of Haematology , vol.151 , Issue.2 , pp. 185-188
    • Best, O.G.1    Singh, N.2    Forsyth, C.3    Mulligan, S.P.4
  • 44
    • 67349255247 scopus 로고    scopus 로고
    • Transcriptomic and proteomic approach to studying SNX-2112-induced K562 cells apoptosis and anti-leukemia activity in K562-NOD/SCID mice
    • L. Jin, C.-L. Xiao, C.-H. Lu et al., "Transcriptomic and proteomic approach to studying SNX-2112-induced K562 cells apoptosis and anti-leukemia activity in K562-NOD/SCID mice," FEBS Letters, vol. 583, no. 12, pp. 1859-1866, 2009.
    • (2009) FEBS Letters , vol.583 , Issue.12 , pp. 1859-1866
    • Jin, L.1    Xiao, C.-L.2    Lu, C.-H.3
  • 45
    • 59649086503 scopus 로고    scopus 로고
    • SNX-2112, a selective Hsp90 inhibitor, potently inhibits tumor cell growth, angiogenesis, and osteoclastogenesis in multiple myeloma and other hematologic tumors by abrogating signaling via Akt and ERK
    • Y. Okawa, T. Hideshima, P. Steed et al., "SNX-2112, a selective Hsp90 inhibitor, potently inhibits tumor cell growth, angiogenesis, and osteoclastogenesis in multiple myeloma and other hematologic tumors by abrogating signaling via Akt and ERK," Blood, vol. 113, no. 4, pp. 846-855, 2009.
    • (2009) Blood , vol.113 , Issue.4 , pp. 846-855
    • Okawa, Y.1    Hideshima, T.2    Steed, P.3
  • 46
    • 17944366977 scopus 로고    scopus 로고
    • Heat-shock protein 70 antagonizes apoptosis-inducing factor
    • L. Ravagnan, S. Gurbuxani, S. A. Susin et al., "Heat-shock protein 70 antagonizes apoptosis-inducing factor," Nature Cell Biology, vol. 3, no. 9, pp. 839-843, 2001.
    • (2001) Nature Cell Biology , vol.3 , Issue.9 , pp. 839-843
    • Ravagnan, L.1    Gurbuxani, S.2    Susin, S.A.3
  • 47
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • J. I.-J. Leu, J. Pimkina, A. Frank, M. E. Murphy, and D. L. George, "A small molecule inhibitor of inducible heat shock protein 70," Molecular Cell, vol. 36, no. 1, pp. 15-27, 2009.
    • (2009) Molecular Cell , vol.36 , Issue.1 , pp. 15-27
    • Leu, J.I.-J.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 48
    • 77954662908 scopus 로고    scopus 로고
    • A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells
    • A. J. Massey, D. S. Williamson, H. Browne et al., "A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells," Cancer Chemotherapy and Pharmacology, vol. 66, no. 3, pp. 535-545, 2010.
    • (2010) Cancer Chemotherapy and Pharmacology , vol.66 , Issue.3 , pp. 535-545
    • Massey, A.J.1    Williamson, D.S.2    Browne, H.3
  • 49
    • 78751478982 scopus 로고    scopus 로고
    • Peptides and aptamers targeting HSP70: A novel approach for anticancer chemotherapy
    • A.-L. Rérole, J. Gobbo, A. De Thonel et al., "Peptides and aptamers targeting HSP70: a novel approach for anticancer chemotherapy," Cancer Research, vol. 71, no. 2, pp. 484-495, 2011.
    • (2011) Cancer Research , vol.71 , Issue.2 , pp. 484-495
    • Rérole, A.-L.1    Gobbo, J.2    De Thonel, A.3
  • 50
    • 77958019101 scopus 로고    scopus 로고
    • Targeting heat shock protein 72 enhances Hsp90 inhibitor-induced apoptosis in myeloma
    • E. L. Davenport, A. Zeisig, L. I. Aronson et al., "Targeting heat shock protein 72 enhances Hsp90 inhibitor-induced apoptosis in myeloma," Leukemia, vol. 24, no. 10, pp. 1804-1807, 2010.
    • (2010) Leukemia , vol.24 , Issue.10 , pp. 1804-1807
    • Davenport, E.L.1    Zeisig, A.2    Aronson, L.I.3
  • 51
    • 4344674482 scopus 로고    scopus 로고
    • Targeting multiple signal transduction pathways through inhibition of Hsp90
    • H. Zhang and F. Burrows, "Targeting multiple signal transduction pathways through inhibition of Hsp90," Journal of Molecular Medicine, vol. 82, no. 8, pp. 488-499, 2004.
    • (2004) Journal of Molecular Medicine , vol.82 , Issue.8 , pp. 488-499
    • Zhang, H.1    Burrows, F.2
  • 52
    • 33646394074 scopus 로고    scopus 로고
    • Transcription factor and kinase-mediated signaling in atherosclerosis and vascular injury
    • N. Adhikari, N. Charles, U. Lehmann, and J. L. Hall, "Transcription factor and kinase-mediated signaling in atherosclerosis and vascular injury," Current Atherosclerosis Reports, vol. 8, no. 3, pp. 252-260, 2006.
    • (2006) Current Atherosclerosis Reports , vol.8 , Issue.3 , pp. 252-260
    • Adhikari, N.1    Charles, N.2    Lehmann, U.3    Hall, J.L.4
  • 53
    • 40649123232 scopus 로고    scopus 로고
    • Innate immunity meetswith cellular stress at the IKK complex: Regulation of the IKKcomplex by HSP70 and HSP90
    • A. Salminen, T. Paimela, T. Suuronen, and K. Kaarniranta, "Innate immunity meetswith cellular stress at the IKK complex: regulation of the IKKcomplex by HSP70 and HSP90," Immunology Letters, vol. 117, no. 1, pp. 9-15, 2008.
    • (2008) Immunology Letters , vol.117 , Issue.1 , pp. 9-15
    • Salminen, A.1    Paimela, T.2    Suuronen, T.3    Kaarniranta, K.4
  • 55
    • 57349131655 scopus 로고    scopus 로고
    • Small molecule inhibitors of Hsp90 potently affect inflammatory disease pathways and exhibit activity in models of rheumatoid arthritis
    • J. W. Rice, J. M. Veal, R. P. Fadden et al., "Small molecule inhibitors of Hsp90 potently affect inflammatory disease pathways and exhibit activity in models of rheumatoid arthritis," Arthritis and Rheumatism, vol. 58, no. 12, pp. 3765-3775, 2008.
    • (2008) Arthritis and Rheumatism , vol.58 , Issue.12 , pp. 3765-3775
    • Rice, J.W.1    Veal, J.M.2    Fadden, R.P.3
  • 56
    • 77951680995 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibitors attenuate inflammatory responses in atherosclerosis
    • J. Madrigal-Matute, O. López-Franco, L. M. Blanco-Colio et al., "Heat shock protein 90 inhibitors attenuate inflammatory responses in atherosclerosis," Cardiovascular Research, vol. 86, no. 2, pp. 330-337, 2010.
    • (2010) Cardiovascular Research , vol.86 , Issue.2 , pp. 330-337
    • Madrigal-Matute, J.1    López-Franco, O.2    Blanco-Colio, L.M.3
  • 57
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • G. Chen, P. Cao, and D. V. Goeddel, "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90," Molecular Cell, vol. 9, no. 2, pp. 401-410, 2002.
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 58
    • 79251588744 scopus 로고    scopus 로고
    • EC144, a synthetic inhibitor of heat shock protein 90, blocks innate and adaptive immune responses in models of inflammation and autoimmunity
    • T. J. Yun, E. K. Harning, K. Giza et al., "EC144, a synthetic inhibitor of heat shock protein 90, blocks innate and adaptive immune responses in models of inflammation and autoimmunity," Journal of Immunology, vol. 186, no. 1, pp. 563-575, 2011.
    • (2011) Journal of Immunology , vol.186 , Issue.1 , pp. 563-575
    • Yun, T.J.1    Harning, E.K.2    Giza, K.3
  • 59
    • 0035210971 scopus 로고    scopus 로고
    • Protective functions of intracellular heat-shock protein (HSP) 70-expression in patients with severe sepsis
    • S. Bruemmer-Smith, F. Stüber, and S. Schroeder, "Protective functions of intracellular heat-shock protein (HSP) 70-expression in patients with severe sepsis," Intensive Care Medicine, vol. 27, no. 12, pp. 1835-1841, 2001.
    • (2001) Intensive Care Medicine , vol.27 , Issue.12 , pp. 1835-1841
    • Bruemmer-Smith, S.1    Stüber, F.2    Schroeder, S.3
  • 60
    • 33646580045 scopus 로고    scopus 로고
    • Hsp70 inhibits lipopolysaccharide-induced NF-κB activation by interacting with TRAF6 and inhibiting its ubiquitination
    • H. Chen, Y. Wu, Y. Zhang et al., "Hsp70 inhibits lipopolysaccharide-induced NF-κB activation by interacting with TRAF6 and inhibiting its ubiquitination," FEBS Letters, vol. 580, no. 13, pp. 3145-3152, 2006.
    • (2006) FEBS Letters , vol.580 , Issue.13 , pp. 3145-3152
    • Chen, H.1    Wu, Y.2    Zhang, Y.3
  • 61
    • 76649097628 scopus 로고    scopus 로고
    • Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells
    • F. Chalmin, S. Ladoire, G. Mignot et al., "Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells," Journal of Clinical Investigation, vol. 120, no. 2, pp. 457-471, 2010.
    • (2010) Journal of Clinical Investigation , vol.120 , Issue.2 , pp. 457-471
    • Chalmin, F.1    Ladoire, S.2    Mignot, G.3
  • 62
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes
    • S. S. Mambula and S. K. Calderwood, "Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes," Journal of Immunology, vol. 177, no. 11, pp. 7849-7857, 2006.
    • (2006) Journal of Immunology , vol.177 , Issue.11 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 63
    • 0036512171 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in innate and adaptive immunity
    • P. Srivastava, "Roles of heat-shock proteins in innate and adaptive immunity," Nature Reviews Immunology, vol. 2, no. 3, pp. 185-194, 2002.
    • (2002) Nature Reviews Immunology , vol.2 , Issue.3 , pp. 185-194
    • Srivastava, P.1
  • 64
    • 0344012568 scopus 로고    scopus 로고
    • Stress-induced extracellular Hsp72 is a functionally significant danger signal to the immune system
    • J. Campisi, T. H. Leem, and M. Fleshner, "Stress-induced extracellular Hsp72 is a functionally significant danger signal to the immune system," Cell Stress and Chaperones, vol. 8, no. 3, pp. 272-286, 2003.
    • (2003) Cell Stress and Chaperones , vol.8 , Issue.3 , pp. 272-286
    • Campisi, J.1    Leem, T.H.2    Fleshner, M.3
  • 65
    • 33646088155 scopus 로고    scopus 로고
    • Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
    • J. D. Johnson and M. Fleshner, "Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72," Journal of Leukocyte Biology, vol. 79, no. 3, pp. 425-434, 2006.
    • (2006) Journal of Leukocyte Biology , vol.79 , Issue.3 , pp. 425-434
    • Johnson, J.D.1    Fleshner, M.2
  • 66
    • 0038458956 scopus 로고    scopus 로고
    • The induction of heat shock protein 70 in peripheral mononuclear blood cells in elderly patients: A role for inflammatory markers
    • R. Njemini, M. Lambert, C. Demanet, M. V. Abeele, S. Vandebosch, and T. Mets, "The induction of heat shock protein 70 in peripheral mononuclear blood cells in elderly patients: a role for inflammatory markers," Human Immunology, vol. 64, no. 6, pp. 575-585, 2003.
    • (2003) Human Immunology , vol.64 , Issue.6 , pp. 575-585
    • Njemini, R.1    Lambert, M.2    Demanet, C.3    Abeele, M.V.4    Vandebosch, S.5    Mets, T.6
  • 67
    • 0031770945 scopus 로고    scopus 로고
    • Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serumof normal individuals
    • A. G. Pockley, J. Shepherd, and J. M. Corton, "Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serumof normal individuals," Immunological Investigations, vol. 27, no. 6, pp. 367-377, 1998.
    • (1998) Immunological Investigations , vol.27 , Issue.6 , pp. 367-377
    • Pockley, A.G.1    Shepherd, J.2    Corton, J.M.3
  • 68
    • 73649130637 scopus 로고    scopus 로고
    • Heat shock proteins and immunity: Application of hyperthermia for immunomodulation
    • T. Torigoe, Y. Tamura, and N. Sato, "Heat shock proteins and immunity: application of hyperthermia for immunomodulation," International Journal of Hyperthermia, vol. 25, no. 8, pp. 610-616, 2009.
    • (2009) International Journal of Hyperthermia , vol.25 , Issue.8 , pp. 610-616
    • Torigoe, T.1    Tamura, Y.2    Sato, N.3
  • 69
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD 14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • A. Asea, S.-K. Kraeft, E. A. Kurt-Jones et al., "HSP70 stimulates cytokine production through a CD 14-dependant pathway, demonstrating its dual role as a chaperone and cytokine," Nature Medicine, vol. 6, no. 4, pp. 435-442, 2000.
    • (2000) Nature Medicine , vol.6 , Issue.4 , pp. 435-442
    • Asea, A.1    Kraeft, S.-K.2    Kurt-Jones, E.A.3
  • 70
    • 82555173115 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibitor is synergistic with JAK2 inhibitor and overcomes resistance to JAK2-TKI in human myeloproliferative neoplasm cells
    • W. Fiskus, S. Verstovsek, T. Manshouri et al., "Heat shock protein 90 inhibitor is synergistic with JAK2 inhibitor and overcomes resistance to JAK2-TKI in human myeloproliferative neoplasm cells," Clinical Cancer Research, vol. 17, no. 23, pp. 7347-7358, 2011.
    • (2011) Clinical Cancer Research , vol.17 , Issue.23 , pp. 7347-7358
    • Fiskus, W.1    Verstovsek, S.2    Manshouri, T.3
  • 71
    • 0033863883 scopus 로고    scopus 로고
    • The heat shockprotein 90 antagonist geldanamycin alters chaperone association with p210(bcr-abl) and v-src proteins before their degradation by the proteasome
    • W.G. An, T.W. Schulte, and L.M. Neckers, "The heat shockprotein 90 antagonist geldanamycin alters chaperone association with p210(bcr-abl) and v-src proteins before their degradation by the proteasome," Cell Growth and Differentiation, vol. 11, no. 7, pp. 355-360, 2000.
    • (2000) Cell Growth and Differentiation , vol.11 , Issue.7 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 72
    • 0037108448 scopus 로고    scopus 로고
    • BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90
    • M. E. Gorre, K. Ellwood-Yen, G. Chiosis, N. Rosen, and C. L. Sawyers, "BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90," Blood, vol. 100, no. 8, pp. 3041-3044, 2002.
    • (2002) Blood , vol.100 , Issue.8 , pp. 3041-3044
    • Gorre, M.E.1    Ellwood-Yen, K.2    Chiosis, G.3    Rosen, N.4    Sawyers, C.L.5
  • 73
    • 36048967663 scopus 로고    scopus 로고
    • A potential role for HSP90 inhibitors in the treatment of JAK2 mutant-positive diseases as demonstrated using quantitative flowcytometry
    • J. Bareng, I. Jilani, M. Gorre et al., "A potential role for HSP90 inhibitors in the treatment of JAK2 mutant-positive diseases as demonstrated using quantitative flowcytometry," Leukemia and Lymphoma, vol. 48, no. 11, pp. 2189-2195, 2007.
    • (2007) Leukemia and Lymphoma , vol.48 , Issue.11 , pp. 2189-2195
    • Bareng, J.1    Jilani, I.2    Gorre, M.3
  • 74
    • 77957854088 scopus 로고    scopus 로고
    • HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans
    • S. Marubayashi, P. Koppikar, T. Taldone et al., "HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans," The Journal of Clinical Investigation, vol. 120, no. 10, pp. 3578-3593, 2010.
    • (2010) The Journal of Clinical Investigation , vol.120 , Issue.10 , pp. 3578-3593
    • Marubayashi, S.1    Koppikar, P.2    Taldone, T.3
  • 75
    • 71549121697 scopus 로고    scopus 로고
    • A purine scaffold Hsp90 inhibitor destabilizes BCL-6 and has specific antitumor activity in BCL-6-dependent B cell lymphomas
    • L. C. Cerchietti, E. C. Lopes, S. N. Yang et al., "A purine scaffold Hsp90 inhibitor destabilizes BCL-6 and has specific antitumor activity in BCL-6-dependent B cell lymphomas," Nature Medicine, vol. 15, no. 12, pp. 1369-1376, 2009.
    • (2009) Nature Medicine , vol.15 , Issue.12 , pp. 1369-1376
    • Cerchietti, L.C.1    Lopes, E.C.2    Yang, S.N.3
  • 76
    • 84856932936 scopus 로고    scopus 로고
    • Genetic resistance to JAK2 enzymatic inhibitors is overcome by HSP90 inhibition
    • O. Weigert, A. A. Lane, L. Bird et al., "Genetic resistance to JAK2 enzymatic inhibitors is overcome by HSP90 inhibition," Journal of Experimental Medicine, vol. 209, no. 2, pp. 259-273, 2012.
    • (2012) Journal of Experimental Medicine , vol.209 , Issue.2 , pp. 259-273
    • Weigert, O.1    Lane, A.A.2    Bird, L.3
  • 77
    • 84897556667 scopus 로고    scopus 로고
    • Improved targeting of JAK2 leads to increased therapeutic efficacy in myeloproliferative neoplasms
    • N. Bhagwat, P. Koppikar, M. Keller et al., "Improved targeting of JAK2 leads to increased therapeutic efficacy in myeloproliferative neoplasms," Blood, vol. 123, no. 13, pp. 2075-2083, 2014.
    • (2014) Blood , vol.123 , Issue.13 , pp. 2075-2083
    • Bhagwat, N.1    Koppikar, P.2    Keller, M.3
  • 78
    • 49449105426 scopus 로고    scopus 로고
    • Signalling profile and antitumour activity of the novel Hsp90 inhibitor NVPAUY922 in multiple myeloma
    • T. Stühmer, A. Zöllinger, D. Siegmund et al., "Signalling profile and antitumour activity of the novel Hsp90 inhibitor NVPAUY922 in multiple myeloma," Leukemia, vol. 22, no. 8, pp. 1604-1612, 2008.
    • (2008) Leukemia , vol.22 , Issue.8 , pp. 1604-1612
    • Stühmer, T.1    Zöllinger, A.2    Siegmund, D.3
  • 79
    • 42349084306 scopus 로고    scopus 로고
    • NVP-AUY922: A novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis
    • S. A. Eccles, A. Massey, F. I. Raynaud et al., "NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis," Cancer Research, vol. 68, no. 8, pp. 2850-2860, 2008.
    • (2008) Cancer Research , vol.68 , Issue.8 , pp. 2850-2860
    • Eccles, S.A.1    Massey, A.2    Raynaud, F.I.3
  • 80
    • 84864029423 scopus 로고    scopus 로고
    • Antileukemic activity of the HSP70 inhibitor pifithrin-l in acute leukemia?
    • article
    • M. Kaiser, A. Kühnl, J. Reins et al., "Antileukemic activity of the HSP70 inhibitor pifithrin-l in acute leukemia," Blood Cancer Journal, vol. 1, no. 7, article e28, 2011.
    • (2011) Blood Cancer Journal , vol.1 , Issue.7
    • Kaiser, M.1    Kühnl, A.2    Reins, J.3
  • 81
    • 84877832281 scopus 로고    scopus 로고
    • Inhibition of related JAK/STAT pathways with molecular targeted drugs shows strong synergy with ruxolitinib in chronic myeloproliferative neoplasm
    • S. Barrio, M. Gallardo, A. Arenas et al., "Inhibition of related JAK/STAT pathways with molecular targeted drugs shows strong synergy with ruxolitinib in chronic myeloproliferative neoplasm," British Journal of Haematology, vol. 161, no. 5, pp. 667-676, 2013.
    • (2013) British Journal of Haematology , vol.161 , Issue.5 , pp. 667-676
    • Barrio, S.1    Gallardo, M.2    Arenas, A.3


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