An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
about
The Fas death signaling pathway connecting reactive oxygen species generation and FLICE inhibitory protein down-regulationFrom death receptor to reactive oxygen species and c-Jun N-terminal protein kinase: the receptor-interacting protein 1 odysseyFLIP the Switch: Regulation of Apoptosis and Necroptosis by cFLIPFLIP and the death effector domain familyc-FLIP, a master anti-apoptotic regulatorNovel phosphorylation and ubiquitination sites regulate reactive oxygen species-dependent degradation of anti-apoptotic c-FLIP proteinRSK2 mediates NF-{kappa}B activity through the phosphorylation of IkappaBalpha in the TNF-R1 pathway.The NF (Nuclear factor)-κB inhibitor parthenolide interacts with histone deacetylase inhibitors to induce MKK7/JNK1-dependent apoptosis in human acute myeloid leukaemia cells.Roles of c-FLIP in Apoptosis, Necroptosis, and Autophagy.FLIP: a novel regulator of macrophage differentiation and granulocyte homeostasisRASSF7 negatively regulates pro-apoptotic JNK signaling by inhibiting the activity of phosphorylated-MKK7The regulation and role of c-FLIP in human Th cell differentiationMitochondrial Extrusion through the cytoplasmic vacuoles during cell deathc-FLIP maintains tissue homeostasis by preventing apoptosis and programmed necrosisTargeting the Anti-Apoptotic Protein c-FLIP for Cancer Therapy.Cellular FLICE-like inhibitory protein (C-FLIP): a novel target for cancer therapy.TRAF2 exerts opposing effects on basal and TNFα-induced activation of the classic IKK complex in hematopoietic cells in micec-Jun N-terminal kinases as potential therapeutic targets.A Rising Cancer Prevention Target of RSK2 in Human Skin Cancer.Differential responses of FLIPLong and FLIPShort-overexpressing human myeloid leukemia cells to TNF-alpha and TRAIL-initiated apoptotic signalsA role for cFLIP in B cell proliferation and stress MAPK regulationTRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (tnf) to efficiently activate nf-{kappa}b and to prevent tnf-induced apoptosis.Harnessing of Programmed Necrosis for Fighting against Cancers.Cellular FLICE-Inhibitory Protein Regulates Tissue Homeostasis.Caspase-8 activity has an essential role in CD95/Fas-mediated MAPK activationInterleukin-11 links oxidative stress and compensatory proliferation.Cell-death-mode switch from necrosis to apoptosis in hydrogen peroxide treated macrophages.Identification of a novel transport-independent function of PiT1/SLC20A1 in the regulation of TNF-induced apoptosis.TNF-like weak inducer of apoptosis inhibits proinflammatory TNF receptor-1 signaling.TRAF2 suppresses basal IKK activity in resting cells and TNFalpha can activate IKK in TRAF2 and TRAF5 double knockout cells.Impairment of the ubiquitin-proteasome system by cellular FLIP.Critical Contribution of Nuclear Factor Erythroid 2-related Factor 2 (NRF2) to Electrophile-induced Interleukin-11 Production.KSHV reduces autophagy in THP-1 cells and in differentiating monocytes by decreasing CAST/calpastatin and ATG5 expression.Expression levels of heat shock protein 27 and cellular FLICE-like inhibitory protein in prostate cancer correlate with Gleason score sum and pathologic stage.Activation-induced degradation of FLIP(L) is mediated via the phosphatidylinositol 3-kinase/Akt signaling pathway in macrophagesThe RING domain of TRAF2 plays an essential role in the inhibition of TNFalpha-induced cell death but not in the activation of NF-kappaB.Cyclic AMP inhibits JNK activation by CREB-mediated induction of c-FLIP(L) and MKP-1, thereby antagonizing UV-induced apoptosis.Loss of cellular FLICE-inhibitory protein promotes acute cholestatic liver injury and inflammation from bile duct-ligation.Association of Increased F4/80high Macrophages With Suppression of Serum-Transfer Arthritis in Mice With Reduced FLIP in Myeloid Cells.Cellular FLIP long isoform transgenic mice overcome inherent Th2-biased immune responses to efficiently resolve Leishmania major infection.
P2860
Q23917081-A3B09A7F-407A-4170-BAFD-AABED538E865Q24299330-8D3BCE1A-94F6-424B-81D9-1A9503BAA6B5Q26773368-10AB78E0-808E-4C56-9D39-14DB478050B6Q28297969-164F29F2-528D-41A5-81F9-F3E834A05B8FQ28391119-1701222E-3E80-48A7-9264-588A64646CD3Q28397635-F44AF830-A6F1-4B28-A709-BEF06A0A4CBDQ34072205-8C3AE745-E772-4EB5-A49A-D2FAEB4467E7Q34176804-0E107CBE-65A9-45DC-8BD6-A734089AECE1Q34449938-8A7C48D4-01D0-4C33-88C6-E3005F7E2817Q34450721-737E68C9-6149-4089-BF20-6914E772B6AAQ35092625-FA20FD3C-61F1-496E-9F0C-0545839EB47DQ35206314-1982AB7A-1DCA-4D97-8C50-241A54DA715EQ35676658-BEABEDD4-79A3-4517-80F2-F373ADA90847Q35735269-9E4552A3-831D-4D4D-9F86-7A88ED4F92D1Q35762274-71AEE769-6078-449D-91E2-6B833233677DQ35915103-8079A414-0B1A-4C01-B757-D14E5574BDC5Q36856751-39AA13F0-7FEE-4161-8099-B0FFFF2D04FCQ36956736-280C19D6-DEFD-435D-B897-4AA4EA05B298Q37068772-33092B29-BBF5-4126-A2D0-4E9311B6C790Q37103897-CEF2B724-5FCE-4B9D-9836-5F4C0D6A2E77Q37287191-7F7717FB-46F4-4C10-B91C-36DF56684DF4Q37467736-27D33984-63A6-49D5-9A77-6CF5D497930BQ38227878-5EF73942-3D5F-465D-8C41-F32375466ACAQ38544605-DD7C8ED2-3CAA-4F55-B506-4FDE92C74F39Q39191656-64C90549-4483-470A-92A2-6BCF236B4031Q39410701-2BFB46BD-FCBB-4D32-9DB0-E52B54F70690Q39643049-C1E4F340-8171-428A-A603-1558623CD4E8Q39659423-45FFB3A0-9327-46EF-9260-3F1F28351490Q39832953-90731565-23C1-48DF-A1F3-3D5E4A39744EQ39857832-331FCDFE-85BB-46D0-8946-C7798017699BQ40119047-3DD8435F-5C90-4574-82F5-78F7E912FD58Q40441611-B3A369D5-7AAE-443F-9114-ADB06C0D5D21Q40509197-A5BAD12D-F84D-493C-A5D5-1449F0CBF7CCQ41441456-544A92BB-CCB1-434A-9FD3-19AEDDD8D9E2Q41905308-4B127E71-9831-40EC-9EF0-964A6BDC4807Q42148237-794DE5DB-C438-45EE-BC71-6C4A80F31C2DQ42811539-D80FFF3E-9523-4807-A213-F1F059F78429Q46250690-87BF7864-6CFB-4A97-9081-34BC4E92AEE6Q50642955-BD87B897-D235-47D5-9F5F-AE7F6A843A41Q51971442-21C21F72-205C-47BC-813F-D88E91340580
P2860
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
description
2006 nî lūn-bûn
@nan
2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@ast
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@en
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@en-gb
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@nl
type
label
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@ast
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@en
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@en-gb
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@nl
prefLabel
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@ast
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@en
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@en-gb
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@nl
P2093
P2860
P356
P1433
P1476
An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
@en
P2093
Akihito Nakajima
Hideo Yagita
Ko Okumura
Mutsuhiro Takekawa
Sachiko Komazawa-Sakon
Tomonari Sasazuki
Wen-Chen Yeh
P2860
P304
P356
10.1038/SJ.EMBOJ.7601423
P407
P577
2006-11-16T00:00:00Z