Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity.
about
Dual function of mitochondrial Nm23-H4 protein in phosphotransfer and intermembrane lipid transfer: a cardiolipin-dependent switchCardiolipin asymmetry, oxidation and signalingAltered Traffic of Cardiolipin during Apoptosis: Exposure on the Cell Surface as a Trigger for "Antiphospholipid Antibodies"BH3-only proteins: a 20-year stock-takePermeabilization of the mitochondrial outer membrane by Bax/truncated Bid (tBid) proteins as sensitized by cardiolipin hydroperoxide translocation: mechanistic implications for the intrinsic pathway of oxidative apoptosisSexual Differences in Cell Loss during the Post-Hatch Development of Song Control Nuclei in the Bengalese FinchMembrane deformation under local pH gradient: mimicking mitochondrial cristae dynamicsFull length Bid is sufficient to induce apoptosis of cultured rat hippocampal neurons.Translocation of p53 to mitochondria is regulated by its lipid binding property to anionic phospholipids and it participates in cell death control.Cholesterol and peroxidized cardiolipin in mitochondrial membrane properties, permeabilization and cell deathDeficiency of Bid protein reduces sepsis-induced apoptosis and inflammation, while improving septic survival.BH3-only proteins in apoptosis and beyond: an overview.Death receptor signals to mitochondria.The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet.Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranesAntiphospholipid reactivity against cardiolipin metabolites occurring during endothelial cell apoptosis.Cell biology of cardiac mitochondrial phospholipids.Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome C releaseOxidatively truncated phospholipids are required agents of tumor necrosis factor α (TNFα)-induced apoptosis.O-acetylation of GD3: an enigmatic modification regulating apoptosis?Hypoxia-mediated down-regulation of Bid and Bax in tumors occurs via hypoxia-inducible factor 1-dependent and -independent mechanisms and contributes to drug resistance.Death by committee: organellar trafficking and communication in apoptosis.Suppression of mitochondrial function by oxidatively truncated phospholipids is reversible, aided by bid, and suppressed by Bcl-XLBioactive oxidatively truncated phospholipids in inflammation and apoptosis: formation, targets, and inactivationBik subcellular localization in response to oxidative stress induced by chemotherapy, in Two different breast cancer cell lines and a Non-tumorigenic epithelial cell line.JNK1/2 regulate Bid by direct phosphorylation at Thr59 in response to ALDH1L1.The contribution of the programmed cell death machinery in innate immune cells to lupus nephritis.Apoptotic foci at mitochondria: in and around Bax pores.Indomethacin-induced activation of the death receptor-mediated apoptosis pathway circumvents acquired doxorubicin resistance in SCLC cellsPro-apoptotic Bid induces membrane perturbation by inserting selected lysolipids into the bilayer.Post-translational modification of Bid has differential effects on its susceptibility to cleavage by caspase 8 or caspase 3.Bid binding to negatively charged phospholipids may not be required for its pro-apoptotic activity in vivoMultiple partners can kiss-and-run: Bax transfers between multiple membranes and permeabilizes those primed by tBid.Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein.Lipids, cardiolipin and apoptosis: a greasy licence to kill.c-Myc induces cytochrome c release in Rat1 fibroblasts by increasing outer mitochondrial membrane permeability in a Bid-dependent manner.Proapoptotic Bid binds to monolysocardiolipin, a new molecular connection between mitochondrial membranes and cell death.tBid forms a pore in the liposome membrane.Cardiolipin and its metabolites move from mitochondria to other cellular membranes during death receptor-mediated apoptosis.Arabidopsis chloroplast lipid transport protein TGD2 disrupts membranes and is part of a large complex.
P2860
Q23923053-34136F12-ABAF-49DF-ADB3-AE434F84B7B5Q23923179-75A70676-A045-4DCB-B6E2-CCCB4AAEDFA9Q26780481-D350F349-40FF-493D-8E16-27A211CC667EQ28085220-F8312C40-83BE-4C22-90E8-7A1A910A509DQ28390599-516BFF4F-AB05-4055-A753-BA6AFD321203Q28648105-03B0E40A-CE48-4738-A7A5-E9BF4601B27DQ30484410-CACE4AA1-CBC2-4CAF-9A30-8723CD03F710Q33275853-121CD4D7-CD95-4749-A12E-4AC8C8D2579DQ33622581-4463CC4E-96D7-405E-AC3B-B97B2822ED5DQ33927481-FF8106A1-F5A6-4D7E-A78C-A6189C7AA1A0Q34017334-73836742-51AB-44B3-9579-08771045FD9BQ34085370-2841FCFF-66C7-40B0-A1BD-1B85D23F4F7BQ34139596-861F0405-C279-4F4E-84F7-094450AFAE62Q34859478-8548D999-129C-447D-8D0F-69F17A66D975Q35220127-BFCE4C24-CCDF-4AD9-8C16-E468E3D38F14Q35630097-9FB04B40-C32F-468A-B14E-0E7AC67EBDECQ35723436-5D7C42F9-E144-4DCE-8507-BF2C0E17A374Q35918372-FE95CB6F-641D-45E5-9FBA-0CEBB2964745Q36006794-B2D67099-5BC6-4798-AC9D-9DD3B479D808Q36376625-9D06938D-8FF9-4569-B53E-3CE2C36B55C8Q37011260-1D817A79-44E3-41D4-BABD-A4B7FF8E9CAFQ37353410-DBAD58C4-AF82-43B3-B926-926C31EF0867Q37446635-9CCEE020-69F2-4479-8264-E5E5B0948357Q37996771-56419089-5EC5-4135-A072-3827F975C381Q38865597-8D327BF8-127E-4FC6-8E39-BF52D03E0831Q38970185-356AA6A4-E225-4793-A24B-161C29AA22BCQ38990736-8F34A970-AEDC-418A-BF16-1F1C7B9E73CFQ39384348-FF564538-7D57-4570-BA7D-29B1BF91F2AEQ40438367-A2E37429-E261-4FC8-ABFD-D8A077FFE28DQ40500837-662752D6-08FF-492B-B7BA-D6BFC9DB0A5FQ40669025-A5D9977A-D165-432C-809A-42FAA407A632Q41892258-4DF9AD4F-0DC4-4857-B4A1-E7A3245CE412Q42593963-12D2A358-E82A-4FEF-8B67-9CF23B5EA429Q43002476-2480D36A-1DF3-4A97-BCF5-9FE33EEB49C2Q43891824-B24D3531-7953-4AAE-80AD-D7CBD15F4AF2Q44427683-4C6D19DA-4B1C-487A-B092-5194DCC79A1FQ44534501-1403B4CA-EA68-40EE-8D42-9E300881B990Q44693554-05F18E8C-1E7E-4B8A-91BB-E23B9322E64FQ44924644-0FCEDDAC-A89F-437C-B709-A65185F0722AQ45904594-AAA985EE-2336-4AE7-81FA-2E7AAFE1A775
P2860
Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity.
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Bid, a widely expressed proapo ...... plays lipid transfer activity.
@ast
Bid, a widely expressed proapo ...... plays lipid transfer activity.
@en
Bid, a widely expressed proapo ...... plays lipid transfer activity.
@nl
type
label
Bid, a widely expressed proapo ...... plays lipid transfer activity.
@ast
Bid, a widely expressed proapo ...... plays lipid transfer activity.
@en
Bid, a widely expressed proapo ...... plays lipid transfer activity.
@nl
prefLabel
Bid, a widely expressed proapo ...... plays lipid transfer activity.
@ast
Bid, a widely expressed proapo ...... plays lipid transfer activity.
@en
Bid, a widely expressed proapo ...... plays lipid transfer activity.
@nl
P2860
P1476
Bid, a widely expressed proapo ...... splays lipid transfer activity
@en
P2093
J A Hickman
M D Esposti
P2860
P304
P356
10.1128/MCB.21.21.7268-7276.2001
P407
P577
2001-11-01T00:00:00Z