Heterodimerization-independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells.
about
Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.PUMA Dissociates Bax and Bcl-X(L) to induce apoptosis in colon cancer cellsProtection of SH-SY5Y neuronal cells from glutamate-induced apoptosis by 3,6'-disinapoyl sucrose, a bioactive compound isolated from Radix PolygalaCell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosisBax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6A splicing variant of the Bcl-2 member Bok with a truncated BH3 domain induces apoptosis but does not dimerize with antiapoptotic Bcl-2 proteins in vitroIntracellular localization of the BCL-2 family member BOK and functional implicationsSusceptibility to drug-induced apoptosis correlates with differential modulation of Bad, Bcl-2 and Bcl-xL protein levels.A novel plant glutathione S-transferase/peroxidase suppresses Bax lethality in yeast.Bax expression in benign and malignant thyroid tumours: dysregulation of wild-type P53 is associated with a high Bax and P21 expression in thyroid carcinoma.The N-terminus and alpha-5, alpha-6 helices of the pro-apoptotic protein Bax, modulate functional interactions with the anti-apoptotic protein Bcl-xL.Antitumor activity and mechanisms of action of total glycosides from aerial part of Cimicifuga dahurica targeted against hepatoma.A secretory phospholipase A2-mediated neuroprotection and anti-apoptosis.Bcl-2 and Bax interact via the BH1-3 groove-BH3 motif interface and a novel interface involving the BH4 motifcGMP-dependent protein kinases and cGMP phosphodiesterases in nitric oxide and cGMP action.Signalling apoptosis: a radical approach.Study of PTPC composition during apoptosis for identification of viral protein target.Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria.Mitigation of H(2)O(2)-Induced Mitochondrial-Mediated Apoptosis in NG108-15 Cells by Novel Mesuagenin C from Mesua kunstleri (King) Kosterm.Inhibition of apoptotic signaling and neointimal hyperplasia by tempol and nitric oxide synthase following vascular injury.Combined inhibition of Notch signaling and Bcl-2/Bcl-xL results in synergistic antimyeloma effect.Bcl-2 is a monomeric protein: prevention of homodimerization by structural constraints.Identification of a drought-induced rice gene, OsSAP, that suppresses Bax-induced cell death in yeast.BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and BakPrognostic value of Bax, Bcl-2, p53, and TUNEL staining in patients with radically resected ampullary carcinoma.Bax-induced apoptotic cell death.Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations.Molecular mechanisms of Bombyx batryticatus ethanol extract inducing gastric cancer SGC-7901 cells apoptosis.Bax-induced cell death in tobacco is similar to the hypersensitive response.Proapoptotic multidomain Bcl-2/Bax-family proteins: mechanisms, physiological roles, and therapeutic opportunities.Anti-Her-2/neu antibody induces apoptosis in Her-2/neu overexpressing breast cancer cells independently from p53 statusProapoptotic genes BAX and CD40L are predictors of survival in transitional cell carcinoma of the bladder.Mimicking the BH3 domain to kill cancer cellsNew insights into cancer-related proteins provided by the yeast model.The BH3 domain of Bcl-x(S) is required for inhibition of the antiapoptotic function of Bcl-x(L).The putative pore-forming domain of Bax regulates mitochondrial localization and interaction with Bcl-X(L).Biochemical and genetic analysis of the mitochondrial response of yeast to BAX and BCL-X(L)Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing.Role of bcl-2 in Epstein-Barr virus-induced malignant conversion of Burkitt's lymphoma cell line Akata.Epstein-Barr virus BALF1 is a BCL-2-like antagonist of the herpesvirus antiapoptotic BCL-2 proteins.
P2860
Q24302494-59E47C14-E5C4-4E3F-9263-73DAF2ED1C2DQ24316443-44C61A27-1CFB-4319-8681-28364612A9EEQ24622211-E182E75F-2306-451F-8402-9CED3E340C42Q24670370-5E5C22E5-468C-4F7A-96ED-E674EBB93203Q28509283-28DAD693-65F4-4D18-AD4B-4033DDE1AE7FQ28568262-3C703B94-EB87-4B96-B159-ABAC282C7120Q28586794-A9EDF009-F44A-46F2-A6F5-538FE793B939Q31384854-6AE5C72F-C68F-4A2A-8464-B13CB6EC9E9CQ33180560-82AA1161-C658-4DD5-A4BF-1E51E773E217Q33182004-965672B5-10EE-467F-9543-22D1FFD7A650Q33285445-26E0E214-1AE1-4672-B11A-280DE4796D4BQ33312872-53A08D37-10C3-41A8-9961-AC44A2B0448AQ33506180-CC1F9CC8-D863-44FF-9C4E-ABCE3C8C9A5EQ34121322-DD1DB9CC-CC37-4AC3-820B-EC46EA4CC481Q34244951-399F5907-7431-4D7A-8384-8E9B8F1AA7B8Q34307275-E3F3D9EF-F391-4914-8FFE-326D0CAC22E5Q34307368-522C69A4-2B44-4AAD-9392-51A4DFEBB91EQ34330920-8BC5EAB7-8E8E-4534-B4AC-320A20540E3EQ34407831-6C940CEF-25DE-468F-9AD5-860B1253E1B7Q34662166-28EBDED1-5219-4E30-940C-427CBDD9DEBDQ34683589-D5246800-B2C3-4DC4-BF21-FFB88A4DB2B1Q35007816-1BD04292-6D71-4669-BD3B-3579DD1EDEB2Q35008607-BDC6CE4B-78DB-42DD-A965-99B92507F0F2Q35079498-314780FB-6F82-48D5-8632-0FF4E40D36BCQ35588363-27B27927-616D-421A-9451-E53373912868Q36092477-FAE3C18D-AB9A-4E45-8976-C26FC3BAE754Q36353924-BF9312E5-634C-4731-8BB1-9794CCECF934Q36379641-A09C13F2-337C-408E-AF1E-984150D0D5BEQ36411566-B7BBB0BA-8CF3-44BB-A46A-29538FA36473Q36490192-F6AA79FD-5EB3-4DF5-AF43-82964D756D26Q36623220-AC1874EC-609C-435B-A037-412D4C8D3F80Q36649097-76F874B9-C8DF-4D37-9D41-D0C1D8A934CDQ37566211-994CD456-4D85-4441-974F-ADD3D662FB47Q37975326-8B259B38-CB55-4296-B839-0456F99D7FFAQ39447996-7F719C0E-D605-4288-BB45-A91EB72FCFB8Q39451362-118E1627-9EFD-4904-9576-5D4F3CC1AC7EQ39452632-30A11141-A0E7-485D-A3D3-127192EAA058Q39576297-74493DDC-3EAE-4679-959A-91C3233237DFQ39602040-C4F47A6B-9382-4BC6-91D4-5F58FCE85156Q39748049-38B87C0E-2E2E-4A2C-8F28-7600D5343F89
P2860
Heterodimerization-independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh-hant
name
Heterodimerization-independent ...... in yeast and mammalian cells.
@en
Heterodimerization-independent ...... in yeast and mammalian cells.
@nl
type
label
Heterodimerization-independent ...... in yeast and mammalian cells.
@en
Heterodimerization-independent ...... in yeast and mammalian cells.
@nl
prefLabel
Heterodimerization-independent ...... in yeast and mammalian cells.
@en
Heterodimerization-independent ...... in yeast and mammalian cells.
@nl
P2860
P356
P1476
Heterodimerization-independent ...... in yeast and mammalian cells.
@en
P2860
P304
31482-31488
P356
10.1074/JBC.272.50.31482
P407
P577
1997-12-01T00:00:00Z