Cardiolipin provides an essential activating platform for caspase-8 on mitochondria. - Wikidata - wikimedia - TriplyDB

Cardiolipin provides an essential activating platform for caspase-8 on mitochondria.

Cardiolipin provides an essential activating platform for caspase-8 on mitochondria.

http://www.wikidata.org/entity/Q36972627

about

Human trifunctional protein alpha links cardiolipin remodeling to beta-oxidation Mass-spectrometry based oxidative lipidomics and lipid imaging: applications in traumatic brain injury Dual function of mitochondrial Nm23-H4 protein in phosphotransfer and intermembrane lipid transfer: a cardiolipin-dependent switch Cytochrome c/cardiolipin relations in mitochondria: a kiss of death Cardiolipin signaling mechanisms: collapse of asymmetry and oxidation Mitochondria targeting of non-peroxidizable triphenylphosphonium conjugated oleic acid protects mouse embryonic cells against apoptosis: role of cardiolipin remodeling Caspase-2: killer, savior and safeguard--emerging versatile roles for an ill-defined caspase Cardiac and skeletal muscle defects in a mouse model of human Barth syndrome Making heads or tails of phospholipids in mitochondria Barth Syndrome: From Mitochondrial Dysfunctions Associated with Aberrant Production of Reactive Oxygen Species to Pluripotent Stem Cell Studies Altered Traffic of Cardiolipin during Apoptosis: Exposure on the Cell Surface as a Trigger for "Antiphospholipid Antibodies"Successful management of Barth syndrome: a systematic review highlighting the importance of a flexible and multidisciplinary approach RIPK-dependent necrosis and its regulation by caspases: a mystery in five acts A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP phosphatase Gep4.Deacylation on the matrix side of the mitochondrial inner membrane regulates cardiolipin remodeling.Sending Out an SOS: Mitochondria as a Signaling Hub Initiation and perpetuation of NLRP3 inflammasome activation and assembly Defining functional classes of Barth syndrome mutation in humans Disorders of phospholipid metabolism: an emerging class of mitochondrial disease due to defects in nuclear genes Cardiolipin Interactions with Proteins Specific interaction with cardiolipin triggers functional activation of Dynamin-Related Protein 1 Permeabilization 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 apoptosis The complexity of cardiolipin in health and disease Role of phosphatidylethanolamine in the biogenesis of mitochondrial outer membrane proteins Essential versus accessory aspects of cell death: recommendations of the NCCD 2015.New insights into mitochondrial structure during cell death.Mechanistic issues of the interaction of the hairpin-forming domain of tBid with mitochondrial cardiolipin.VDAC2 is required for truncated BID-induced mitochondrial apoptosis by recruiting BAK to the mitochondria A new caspase-8 isoform caspase-8s increased sensitivity to apoptosis in Jurkat cells Voltage dependent anion channel-1 regulates death receptor mediated apoptosis by enabling cleavage of caspase-8.Mechanism of NLRP3 inflammasome activation Redox control of liver function in health and disease Cholesterol and peroxidized cardiolipin in mitochondrial membrane properties, permeabilization and cell death Mitochondrial protection restores renal function in swine atherosclerotic renovascular disease.The caspase-8 dimerization/dissociation balance is a highly potent regulator of caspase-8, -3, -6 signaling Mitochondrial Ca(2+) influx targets cardiolipin to disintegrate respiratory chain complex II for cell death induction Caspase-8 binding to cardiolipin in giant unilamellar vesicles provides a functional docking platform for bid.Barth syndrome mutations that cause tafazzin complex lability.Mitochondrial cardiolipin involved in outer-membrane protein biogenesis: implications for Barth syndrome.Interaction of enterocyte FABPs with phospholipid membranes: clues for specific physiological roles

P2860

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P2860

Cardiolipin provides an essential activating platform for caspase-8 on mitochondria.

http://www.wikidata.org/entity/Q36972627

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

Cardiolipin provides an essential activating platform for caspase-8 on mitochondria.

@en

type

label

Cardiolipin provides an essential activating platform for caspase-8 on mitochondria.

@en

prefLabel

Cardiolipin provides an essential activating platform for caspase-8 on mitochondria.

@en

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P1433

Journal of Cell Biology

P1476

Cardiolipin provides an essential activating platform for caspase-8 on mitochondria.

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P2093

David G Brooks

http://www.w3.org/2001/XMLSchema#string

Elaine D MacKenzie

http://www.w3.org/2001/XMLSchema#string

Eyal Gottlieb

http://www.w3.org/2001/XMLSchema#string

Francois Gonzalvez

http://www.w3.org/2001/XMLSchema#string

Frédéric M Vaz

http://www.w3.org/2001/XMLSchema#string

Patrice X Petit

http://www.w3.org/2001/XMLSchema#string

Riekelt H Houtkooper

http://www.w3.org/2001/XMLSchema#string

Ronald J A Wanders

http://www.w3.org/2001/XMLSchema#string

Zachary T Schug

http://www.w3.org/2001/XMLSchema#string

P2860

Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner

An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9

BAR: An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins

Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis

Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors

Defective remodeling of cardiolipin and phosphatidylglycerol in Barth syndrome

FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies

The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta

Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

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681-696

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scholarly article

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10.1083/JCB.200803129

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P433

4

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183

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2008-11-10T00:00:00Z

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23465611

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19001123

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2582890

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