Activation and specificity of human caspase-10. - Test2 - elhamkhani - TriplyDB

Activation and specificity of human caspase-10.

Activation and specificity of human caspase-10.

http://www.wikidata.org/entity/Q42423646

about

Inhibition of vacuolar ATPase attenuates the TRAIL-induced activation of caspase-8 and modulates the trafficking of TRAIL receptosomes Control of autophagic cell death by caspase-10 in multiple myeloma DED or alive: assembly and regulation of the death effector domain complexes Involvement of TGF-β1/Smad3 Signaling in Carbon Tetrachloride-Induced Acute Liver Injury in Mice Proteome-wide covalent ligand discovery in native biological systems Bi-specific molecule against EGFR and death receptors simultaneously targets proliferation and death pathways in tumors A multipronged approach for compiling a global map of allosteric regulation in the apoptotic caspases.Caspase-10 is the key initiator caspase involved in tributyltin-mediated apoptosis in human immune cells.Small Molecule Active Site Directed Tools for Studying Human Caspases Mechanism of Action of Two Flavone Isomers Targeting Cancer Cells with Varying Cell Differentiation Status.Trauma patients' elevated tumor necrosis related apoptosis inducing ligand (TRAIL) contributes to increased T cell apoptosis.Highly sensitive and adaptable fluorescence-quenched pair discloses the substrate specificity profiles in diverse protease families.Brahma is essential for Drosophila intestinal stem cell proliferation and regulated by Hippo signaling Proliferative versus apoptotic functions of caspase-8 Hetero or homo: the caspase-8 dimer controls cell fate.Cellular mechanisms controlling caspase activation and function.Targeting apoptosis in autoimmune hepatitis.Caspase-10 Negatively Regulates Caspase-8-Mediated Cell Death, Switching the Response to CD95L in Favor of NF-κB Activation and Cell Survival.Caspases and their substrates.Individual caspase-10 isoforms play distinct and opposing roles in the initiation of death receptor-mediated tumour cell apoptosis.Caspase-8 cleaves its substrates from the plasma membrane upon CD95-induced apoptosis.Synthesis of a HyCoSuL peptide substrate library to dissect protease substrate specificity.Differential response of head and neck cancer cell lines to TRAIL or Smac mimetics is associated with the cellular levels and activity of caspase-8 and caspase-10 Intrinsic cleavage of receptor-interacting protein kinase-1 by caspase-6.Expression of pro-apoptotic markers is increased along the osteochondral junction in naturally occurring osteochondrosis.

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P2860

Activation and specificity of human caspase-10.

http://www.wikidata.org/entity/Q42423646

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

Activation and specificity of human caspase-10.

@en

Activation and specificity of human caspase-10.

@nl

type

label

Activation and specificity of human caspase-10.

@en

Activation and specificity of human caspase-10.

@nl

prefLabel

Activation and specificity of human caspase-10.

@en

Activation and specificity of human caspase-10.

@nl

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P1476

Activation and specificity of human caspase-10.

@en

P2093

Cristina Pop

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

Guy S Salvesen

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

Katherine Wachmann

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

Marcin Drag

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

Robert Schwarzenbacher

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

Scott J Snipas

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

Stefan J Riedl

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

P2860

Inherited human Caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II

Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis

Caspase-10 is an initiator caspase in death receptor signaling

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.

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

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

In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains

Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death

A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis

P304

8307-8315

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scholarly article

P356

10.1021/BI100968M

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P433

38

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P478

49

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P50

Christian M Zmasek

Bram J van Raam

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2010-09-01T00:00:00Z

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46007946

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20795673

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2943529

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