Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL. - Wikidata - awgldk - TriplyDB

Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL.

Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL.

http://www.wikidata.org/entity/Q34069986

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Antioxidant c-FLIP inhibits Fas ligand-induced NF-kB activation in a phosphatidylinositol 3-kinase/Akt-dependent manner FLIP the Switch: Regulation of Apoptosis and Necroptosis by cFLIP Regulation of CD95/Fas signaling at the DISC Death-defining immune responses after apoptosis Modulation of apoptosis sensitivity through the interplay with autophagic and proteasomal degradation pathways Molecular architecture of the DED chains at the DISC: regulation of procaspase-8 activation by short DED proteins c-FLIP and procaspase-8 prodomain Hyperthermia enhances mapatumumab-induced apoptotic death through ubiquitin-mediated degradation of cellular FLIP(long) in human colon cancer cells STL-based analysis of TRAIL-induced apoptosis challenges the notion of type I/type II cell line classification Modulating cell-to-cell variability and sensitivity to death ligands by co-drugging.Constitutive expression of murine c-FLIPR causes autoimmunity in aged mice Rocaglamide breaks TRAIL resistance in HTLV-1-associated adult T-cell leukemia/lymphoma by translational suppression of c-FLIP expression.FLASH knockdown sensitizes cells to Fas-mediated apoptosis via down-regulation of the anti-apoptotic proteins, MCL-1 and Cflip short Galangin induces apoptosis in hepatocellular carcinoma cells through the caspase 8/t-Bid mitochondrial pathway.Programming biological models in Python using PySB Intra- and interdimeric caspase-8 self-cleavage controls strength and timing of CD95-induced apoptosis.Measuring and modeling apoptosis in single cells.The role of c-FLIP splice variants in urothelial tumours.Fractional killing arises from cell-to-cell variability in overcoming a caspase activity threshold Regulation of chemoresistance via alternative messenger RNA splicing On the TRAIL to successful cancer therapy? Predicting and counteracting resistance against TRAIL-based therapeutics.Proteasome inhibition can impair caspase-8 activation upon submaximal stimulation of apoptotic tumor necrosis factor-related apoptosis inducing ligand (TRAIL) signaling.Balance between short and long isoforms of cFLIP regulates Fas-mediated apoptosis in vivo Tumor Necrosis Factor-α: Life and Death of Hepatocytes During Liver Ischemia/Reperfusion Injury.Cells surviving fractional killing by TRAIL exhibit transient but sustainable resistance and inflammatory phenotypes.Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF).Death ligand concentration and the membrane proximal signaling module regulate the type 1/type 2 choice in apoptotic death signaling.Monte carlo study elucidates the type 1/type 2 choice in apoptotic death signaling in healthy and cancer cells.Sensitization of glycoengineered interferon-β1a-resistant cancer cells by cFLIP inhibition for enhanced anti-cancer therapy.The secrets of the Bcl-2 family.Life in the Fas lane: differential outcomes of Fas signaling.FLIP: molecular switch between apoptosis and necroptosis.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.Surviving apoptosis: life-death signaling in single cells.Cell death at the intestinal epithelial front line.cFLIPL Interrupts IRF3-CBP-DNA Interactions To Inhibit IRF3-Driven Transcription.The C-terminal domain of the long form of cellular FLICE-inhibitory protein (c-FLIPL) inhibits the interaction of the caspase 8 prodomain with the receptor-interacting protein 1 (RIP1) death domain and regulates caspase 8-dependent nuclear factor κB Upregulation of c-FLIP-short in response to TRAIL promotes survival of NSCLC cells, which could be suppressed by inhibition of Ca2+/calmodulin signaling

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Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL.

http://www.wikidata.org/entity/Q34069986

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@ast

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@en

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@nl

type

label

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@ast

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@en

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@nl

prefLabel

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@ast

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@en

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@nl

P1433

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P1433

Journal of Cell Biology

P1476

Model-based dissection of CD95 ...... antiapoptotic role of c-FLIPL.

@en

P2093

Inna N Lavrik

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

Joel Beaudouin

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

Nicolai Fricker

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

Peter H Krammer

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

Petra Richter

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

P2860

Mathematical modeling identifies inhibitors of apoptosis as mediators of positive feedback and bistability

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.

Caspases: pharmacological manipulation of cell death

Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor

Mechanism of procaspase-8 activation by c-FLIPL

The caspase-8 inhibitor FLIP promotes activation of NF-kappaB and Erk signaling pathways

Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex

The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex

FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).

FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex

P304

377-389

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scholarly article

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10.1083/JCB.201002060

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3

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190

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P577

2010-08-01T00:00:00Z

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45583152

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20696707

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2922645

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