Inhibition of apoptosome formation by suppression of Hsp90beta phosphorylation in tyrosine kinase-induced leukemias.
about
Rsk-mediated phosphorylation and 14-3-3ɛ binding of Apaf-1 suppresses cytochrome c-induced apoptosisRegulation and function of the human HSP90AA1 genePrediction of Functionally Important Phospho-Regulatory Events in Xenopus laevis Oocytes.Hsp-90 and the biology of nematodes.Mitochondrial and postmitochondrial survival signaling in cancer.Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.Angiogenin-cleaved tRNA halves interact with cytochrome c, protecting cells from apoptosis during osmotic stress.Regulation of the Apaf-1-caspase-9 apoptosomeDifferential proteomic analysis of human erythroblasts undergoing apoptosis induced by epo-withdrawal.Protein-selective capture to analyze electrophile adduction of hsp90 by 4-hydroxynonenal.Stability of the human Hsp90-p50Cdc37 chaperone complex against nucleotides and Hsp90 inhibitors, and the influence of phosphorylation by casein kinase 2Post-translational modifications of Hsp90 and their contributions to chaperone regulationCasein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity.Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activityBortezomib interferes with C-KIT processing and transforms the t(8;21)-generated fusion proteins into tumor-suppressing fragments in leukemia cells.The mitochondrial death pathway: a promising therapeutic target in diseasesEngineering a BCR-ABL-activated caspase for the selective elimination of leukemic cellsA network of substrates of the E3 ubiquitin ligases MDM2 and HUWE1 control apoptosis independently of p53.Hsp90, an unlikely ally in the war on cancer.The levels of retinoic acid-inducible gene I are regulated by heat shock protein 90-alpha.Molecules that modulate Apaf-1 activity.Regulation of molecular chaperones through post-translational modifications: decrypting the chaperone code.Evading apoptosis in cancer.Heat shock protein 90 and role of its chemical inhibitors in treatment of hematologic malignanciesMechanisms of Resistance to Hsp90 Inhibitor Drugs: A Complex Mosaic Emerges.Alternative approaches to Hsp90 modulation for the treatment of cancer.FNDC4 acts as an anti-inflammatory factor on macrophages and improves colitis in mice.Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes.Quercetin enhances the effects of 5-fluorouracil-mediated growth inhibition and apoptosis of esophageal cancer cells by inhibiting NF-κB.Sally Kornbluth: Nature's incredible contraptions.Targeting c-KIT (CD117) by dasatinib and radotinib promotes acute myeloid leukemia cell death.Triptolide, a HSP90 middle domain inhibitor, induces apoptosis in triple manner.
P2860
Q24301885-F9443A66-985D-4521-A681-48E7CACD93CAQ28646043-8973531F-99D9-403B-8032-5CC1EF1AE570Q30378436-AC426358-55BB-43D4-997C-F2179FF4E2D1Q30491353-B7D2DC3E-A8BE-436F-9D63-D1312F218B21Q33645577-3EFF1F6A-AD9C-4EBC-9DB3-5611F64C6AF1Q33669025-300C4E27-A786-4B16-984F-F11D65B9758BQ33743668-30C301B8-8276-4F47-8176-591AB8FF3813Q34129476-E45BB660-3012-4F54-9C0D-CFEF9E6E5554Q34313842-392F0256-EB24-488C-A164-5F1134EC4E4EQ35164081-1D1996B2-3AC2-44E1-8120-7B1D6B6C8E90Q35546665-9B8231F0-45C3-4606-AD83-A4D22B83E609Q35581165-3B56DA0F-20B2-4367-8724-AEFD47AC03EFQ35640239-EED06FE2-69EC-4803-BA48-0D8C33D0FF81Q35779397-E2678F3F-303C-4273-89C2-6836AF2D6437Q35786902-B5511DBF-8732-4056-81FD-7978E071043EQ35831981-87FA77FC-ECD6-4AF1-9931-906A0381A608Q36598253-53962D4C-97D1-481B-8972-6C73399BEFFEQ37163577-E9D6E2B1-3072-4A54-BC55-BC851723E21CQ37274497-F0C6D9AE-485E-4671-89EC-DE6AD4126258Q37293018-E1F1019F-FBCE-4F86-B8CF-6ACB61359A31Q37680800-07BD0746-B459-4765-B9D1-6E3405BB761DQ38086397-C24330F0-62CE-4503-A258-82CD2E050B89Q38130013-A4BE8F3B-5F6C-46BA-8C4C-EAB436687633Q38166527-3B2ABA59-8940-47A8-A88A-F37E60408C89Q38976702-19674C9F-995D-4549-8319-B6C696F2E904Q39103704-B4A97856-4519-4E43-BE17-E93D27FD37B6Q40036306-E3748D01-1D7D-475B-9ADC-B5998C3FEE8CQ40530080-DD06F099-6F9B-4E6F-B468-12F45DDFD40AQ42354761-6856A9DE-74C6-49E6-A1EE-83C988959C5CQ42724015-90D2D51C-54BE-4BD5-BE98-66F3004D097CQ46038713-9BCE4322-20CB-45F1-BC71-577AC5A63B5FQ54977484-3E9C5104-2F94-438F-8AB0-30104899C275
P2860
Inhibition of apoptosome formation by suppression of Hsp90beta phosphorylation in tyrosine kinase-induced leukemias.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Inhibition of apoptosome forma ...... sine kinase-induced leukemias.
@en
Inhibition of apoptosome forma ...... sine kinase-induced leukemias.
@nl
type
label
Inhibition of apoptosome forma ...... sine kinase-induced leukemias.
@en
Inhibition of apoptosome forma ...... sine kinase-induced leukemias.
@nl
prefLabel
Inhibition of apoptosome forma ...... sine kinase-induced leukemias.
@en
Inhibition of apoptosome forma ...... sine kinase-induced leukemias.
@nl
P2093
P2860
P356
P1476
Inhibition of apoptosome forma ...... sine kinase-induced leukemias.
@en
P2093
Manabu Kurokawa
Sally Kornbluth
P2860
P304
P356
10.1128/MCB.00265-08
P407
P577
2008-06-30T00:00:00Z