A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death. - Wikidata - thesis-toulmin - TriplyDB

A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death.

A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death.

http://www.wikidata.org/entity/Q34032310

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Inhibition of vacuolar ATPase attenuates the TRAIL-induced activation of caspase-8 and modulates the trafficking of TRAIL receptosomes XLS (c9orf142) is a new component of mammalian DNA double-stranded break repair Onto better TRAILs for cancer treatment FLIP the Switch: Regulation of Apoptosis and Necroptosis by cFLIP Principles of antibody-mediated TNF receptor activation DED or alive: assembly and regulation of the death effector domain complexes Marine Drugs Regulating Apoptosis Induced by Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL)Death receptor-ligand systems in cancer, cell death, and inflammation Modulation of apoptosis sensitivity through the interplay with autophagic and proteasomal degradation pathways Programmed necrosis in the cross talk of cell death and inflammation Getting TRAIL back on track for cancer therapy Structural architecture of the CARMA1/Bcl10/MALT1 signalosome: nucleation-induced filamentous assembly.Differential Impacts of Alternative Splicing Networks on Apoptosis Molecular architecture of the DED chains at the DISC: regulation of procaspase-8 activation by short DED proteins c-FLIP and procaspase-8 prodomain Trailing TRAIL Resistance: Novel Targets for TRAIL Sensitization in Cancer Cells Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex.Caspase-8 mutations in head and neck cancer confer resistance to death receptor-mediated apoptosis and enhance migration, invasion, and tumor growth.Modeling dynamics of cell-to-cell variability in TRAIL-induced apoptosis explains fractional killing and predicts reversible resistance Intra- and interdimeric caspase-8 self-cleavage controls strength and timing of CD95-induced apoptosis.Rocaglamide overcomes tumor necrosis factor-related apoptosis-inducing ligand resistance in hepatocellular carcinoma cells by attenuating the inhibition of caspase-8 through cellular FLICE-like-inhibitory protein downregulation.TNF-related apoptosis-inducing ligand promotes human preadipocyte proliferation via ERK1/2 activation.Deficiency in the mitochondrial apoptotic pathway reveals the toxic potential of autophagy under ER stress conditions.Hyperthermia restores apoptosis induced by death receptors through aggregation-induced c-FLIP cytosolic depletion.The Inflammasome Adaptor ASC Induces Procaspase-8 Death Effector Domain Filaments Structural Basis and Functional Role of Intramembrane Trimerization of the Fas/CD95 Death Receptor.Insights into the mechanism of human papillomavirus E2-induced procaspase-8 activation and cell death The unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles.Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF).Structural basis of signal transduction in the TNF receptor superfamily Remodelling of a polypyrimidine tract-binding protein complex during apoptosis activates cellular IRESs TRAIL (TNF-related apoptosis-inducing ligand) inhibits human adipocyte differentiation via caspase-mediated downregulation of adipogenic transcription factors.Fas/CD95 prevents autoimmunity independently of lipid raft localization and efficient apoptosis induction.Selective CDK9 inhibition overcomes TRAIL resistance by concomitant suppression of cFlip and Mcl-1.FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes.It's not over until the FAT lady sings.Mathematical modeling of apoptosis.Harnessing system models of cell death signalling for cytotoxic chemotherapy: towards personalised medicine approaches?Systems biology of death receptor networks: live and let die.Cell death controlling complexes and their potential therapeutic role.Programmed necrosis and necroptosis signalling.

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A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death.

http://www.wikidata.org/entity/Q34032310

description

2012 nî lūn-bûn

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2012 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2012 թվականի հունիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

A death effector domain chain ...... ediating apoptotic cell death.

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A death effector domain chain ...... ediating apoptotic cell death.

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A death effector domain chain ...... ediating apoptotic cell death.

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type

label

A death effector domain chain ...... ediating apoptotic cell death.

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A death effector domain chain ...... ediating apoptotic cell death.

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A death effector domain chain ...... ediating apoptotic cell death.

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A death effector domain chain ...... ediating apoptotic cell death.

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A death effector domain chain ...... ediating apoptotic cell death.

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A death effector domain chain ...... ediating apoptotic cell death.

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J.MOLCEL.2012.05.004

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A death effector domain chain ...... ediating apoptotic cell death.

@en

P2093

Gemma L Robinson

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

John W R Schwabe

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Kelvin Cain

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

Laura S Dickens

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

Marion Macfarlane

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

Michelle A Hughes

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

Rebekah Jukes-Jones

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Robert S Boyd

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

P2860

Caspase-10 is an initiator caspase in death receptor signaling

The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations

Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.

Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling

The Fas-FADD death domain complex structure unravels signalling by receptor clustering

Inhibition of death receptor signals by cellular FLIP

Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling

Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha

Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation

The three-dimensional solution structure and dynamic properties of the human FADD death domain

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291-305

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10.1016/J.MOLCEL.2012.05.004

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2

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47

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2012-06-07T00:00:00Z

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225286310

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22683266

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apoptotic process

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3477315

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