NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells.
about
The role of HDAC6 in cancerPCI-24781, a Novel Hydroxamic Acid HDAC Inhibitor, Exerts Cytotoxicity and Histone Alterations via Caspase-8 and FADD in Leukemia CellsPCI-24781 induces caspase and reactive oxygen species-dependent apoptosis through NF-kappaB mechanisms and is synergistic with bortezomib in lymphoma cellsTrial Watch: Proteasomal inhibitors for anticancer therapyMechanisms of synergistic antileukemic interactions between valproic acid and cytarabine in pediatric acute myeloid leukemiaSynergistic apoptosis induction in leukemic cells by the phosphatase inhibitor salubrinal and proteasome inhibitorsDiscovery of novel proteasome inhibitors using a high-content cell-based screening systemProteasome inhibitors in glioblastomaDiscovery and development of the anticancer agent salinosporamide A (NPI-0052).Oxidative stress by targeted agents promotes cytotoxicity in hematologic malignancies.Antileukemic activity and mechanism of drug resistance to the marine Salinispora tropica proteasome inhibitor salinosporamide A (Marizomib).Paclitaxel promotes a caspase 8-mediated apoptosis through death effector domain association with microtubules.Bortezomib-induced sensitization of malignant human glioma cells to vorinostat-induced apoptosis depends on reactive oxygen species production, mitochondrial dysfunction, Noxa upregulation, Mcl-1 cleavage, and DNA damage.Generating a generation of proteasome inhibitors: from microbial fermentation to total synthesis of salinosporamide a (marizomib) and other salinosporamidesAntineoplastic effects of CPPTL via the ROS/JNK pathway in acute myeloid leukemia.Salinosporamide natural products: Potent 20 S proteasome inhibitors as promising cancer chemotherapeutics.The ubiquitin-proteasome system: opportunities for therapeutic intervention in solid tumorsBortezomib sensitizes non-small cell lung cancer to mesenchymal stromal cell-delivered inducible caspase-9-mediated cytotoxicity.Advances in and applications of proteasome inhibitorsProteasome inhibitors in cancer therapyIn vitro and in vivo interactions between the HDAC6 inhibitor ricolinostat (ACY1215) and the irreversible proteasome inhibitor carfilzomib in non-Hodgkin lymphoma cellsProteasome inhibitor patents (2010 - present).Proteasome inhibition can induce an autophagy-dependent apical activation of caspase-8.Antioxidants impair anti-tumoral effects of Vorinostat, but not anti-neoplastic effects of Vorinostat and caspase-8 downregulationInhibition of LSD1 sensitizes glioblastoma cells to histone deacetylase inhibitorsTreatment-induced oxidative stress and cellular antioxidant capacity determine response to bortezomib in mantle cell lymphoma.Specific and prolonged proteasome inhibition dictates apoptosis induction by marizomib and its analogs.Efficacy of panobinostat and marizomib in acute myeloid leukemia and bortezomib-resistant models.The 26S proteasome complex: an attractive target for cancer therapyProteasome inhibitor MG-132 enhances histone deacetylase inhibitor SAHA-induced cell death of chronic myeloid leukemia cells by an ROS-mediated mechanism and downregulation of the Bcr-Abl fusion protein.Bortezomib interacts synergistically with belinostat in human acute myeloid leukaemia and acute lymphoblastic leukaemia cells in association with perturbations in NF-κB and BimProteasome inhibition and combination therapy for non-Hodgkin's lymphoma: from bench to bedsideSalinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through down-modulation of NF-kappaB regulated gene products.EGCG antagonizes Bortezomib cytotoxicity in prostate cancer cells by an autophagic mechanismThe peptide derived from the Ig-like domain of human herpesvirus 8 K1 protein induces death in hematological cancer cells.Induction of cell death by the novel proteasome inhibitor marizomib in glioblastoma in vitro and in vivoDual targeting of the proteasome regulates survival and homing in Waldenstrom macroglobulinemiaRedox control of leukemia: from molecular mechanisms to therapeutic opportunities.From bortezomib to other inhibitors of the proteasome and beyond.Marizomib activity as a single agent in malignant gliomas: ability to cross the blood-brain barrier.
P2860
Q21296746-BAF9B2FC-4C4D-410A-A850-215052F0A4FEQ21328686-BC7CBD7D-0690-499E-9EEC-4454FAB12C6FQ24654958-4DD894AA-C093-4860-9A4E-57A718C22E5CQ28082910-2FFA4D69-583E-45BA-A13D-A05A797BDB79Q28385690-97786361-8AA2-4BF2-9914-73BD620D1828Q28474489-12CFE916-D20B-4EEF-A0D2-3BEF3B2C9AEDQ33521189-E783119C-856F-47B1-AEB5-AC8E80145BFBQ33598931-360EA47A-24FE-4FA7-A873-DF63455CCDA9Q33622960-2E293CCD-B6B5-4191-8E4A-C9904D0E69E4Q33741142-C2E66367-90A6-4ECC-9EBA-A3869396548DQ33742779-13C0EBD7-F96B-495D-ACD3-A4237E259C9CQ33775805-259EBA87-B9D8-4933-BAE2-4A897CF0C2E6Q33798624-C65021BF-0BD1-4A2D-B9F6-0171BCFDE5DAQ33836952-3657CB8A-1FA5-45F0-AEF3-0BB2EF81B591Q33889046-A383D3AD-C537-4EC7-9C1F-B0AC3D8ECC69Q34142223-95211631-0CCB-4F99-8ACF-3C8A63164889Q34218976-52E88B1C-C8A7-4470-8223-52F43BB5BAE8Q34576976-D72D5988-919A-4A67-BF0A-F8416784834EQ34594744-60374FD3-2956-4617-B9D4-182FFEBA30D8Q34939959-CBB688B1-6216-4E0D-AF8A-E747753DC7C6Q35007061-129E71BF-AF22-46A5-8029-8F32E1BE3A48Q35085938-7C8E8AB2-6C2D-43AA-B1EB-2B31DF523954Q35089766-A5AF76C3-2C6C-479E-A28B-EBB08A12DB0BQ35126359-CBF888E9-B876-4FE9-B6FE-6442012841ADQ35133399-5473C9AE-FC19-4CA5-91E8-B96463DA70CAQ35146262-32E93CC6-BB30-4CD8-A456-AA1CDF3CA506Q35269634-D6AE164C-7FAB-4B24-A506-5247A3589692Q35572018-572C4496-A3DB-422B-87E0-7A93FB25EFBBQ35624079-4465A3BC-A20A-403A-9DCA-4175A39F6D01Q35882968-4BF05077-253D-4050-8290-355BDC97473AQ35982670-DF5F862E-F409-4FEC-ACC7-12AA70EF7F8EQ35989980-21B5A5CD-F70E-46E2-B7CE-229B4B37BD1BQ36007617-27FE3EC9-B4D9-45FD-9CD6-7B3F0B88E447Q36168253-EE8AEF41-8C56-4EF3-9D10-63F02A1EB34AQ36453798-9D985BB2-0A1A-4BA0-B80C-4E1D9919C4CEQ36500531-4A1A6DC0-011A-4EB0-8214-C58BA5530D2EQ36591379-F6875810-2DE9-4ACD-8009-DCA884765AD4Q36646486-18EAEF12-7A34-44BA-9828-5CE2EA6B27A0Q36852277-C0DDDE49-797D-4035-8174-11C29B8A73FBQ36893244-38874097-D00A-42FD-B769-4103DC92F583
P2860
NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
NPI-0052, a novel proteasome i ...... inhibitors in leukemia cells.
@ast
NPI-0052, a novel proteasome i ...... inhibitors in leukemia cells.
@en
type
label
NPI-0052, a novel proteasome i ...... inhibitors in leukemia cells.
@ast
NPI-0052, a novel proteasome i ...... inhibitors in leukemia cells.
@en
prefLabel
NPI-0052, a novel proteasome i ...... inhibitors in leukemia cells.
@ast
NPI-0052, a novel proteasome i ...... inhibitors in leukemia cells.
@en
P2093
P2860
P1433
P1476
NPI-0052, a novel proteasome i ...... inhibitors in leukemia cells.
@en
P2093
Claudia P Miller
David J McConkey
Joya Chandra
Kechen Ban
Mark Munsell
Melanie E Dujka
Michael Palladino
P2860
P304
P356
10.1182/BLOOD-2006-03-013128
P407
P577
2007-03-13T00:00:00Z