Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain.
about
The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosisRipped to deathNecroptosis in tumorigenesis, activation of anti-tumor immunity, and cancer therapyPost-translational modifications as key regulators of TNF-induced necroptosisMolecular crosstalk between apoptosis, necroptosis, and survival signalingPoly-ubiquitination in TNFR1-mediated necroptosisAn outline of necrosome triggersConverging roles of caspases in inflammasome activation, cell death and innate immunityDeath in the fast lane: what's next for necroptosis?Ubiquitin-Mediated Regulation of Cell Death, Inflammation, and Defense of HomeostasisFueling the flames: Mammalian programmed necrosis in inflammatory diseasesPhotoreceptor cell death and rescue in retinal detachment and degenerationsThe two faces of receptor interacting protein kinase-1Small-molecule SMAC mimetics as new cancer therapeuticsViral infection and the evolution of caspase 8-regulated apoptotic and necrotic death pathwaysNecroptosis: molecular signalling and translational implicationsRegulated necrotic cell death: the passive aggressive side of Bax and BakExecution of RIPK3-regulated necrosisRIPK-dependent necrosis and its regulation by caspases: a mystery in five actsProgrammed necrosis in the cross talk of cell death and inflammationRole of mitochondria in apoptotic and necroptotic cell death in the developing brainThe role of necroptosis in neurosurgical diseasesSphingolipids as cell fate regulators in lung development and diseaseNecroptosis: The Trojan horse in cell autonomous antiviral host defenseDie another way--non-apoptotic mechanisms of cell deathRegulation of tumour necrosis factor signalling: live or let dieTNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II membersComplementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunityMlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosisSurvival function of the FADD-CASPASE-8-cFLIP(L) complexThe Gβγ-Src signaling pathway regulates TNF-induced necroptosis via control of necrosome translocation5-Aminolevulinic Acid-Mediated Sonodynamic Therapy Inhibits RIPK1/RIPK3-Dependent Necroptosis in THP-1-Derived Foam Cells.Receptor interacting protein 3 suppresses vascular smooth muscle cell growth by inhibition of the phosphoinositide 3-kinase-Akt axis.MK2 Phosphorylates RIPK1 to Prevent TNF-Induced Cell Death.RIP3 overexpression sensitizes human breast cancer cells to parthenolide in vitro via intracellular ROS accumulationInducible dimerization and inducible cleavage reveal a requirement for both processes in caspase-8 activation.Cutting edge: RIPK1 Kinase inactive mice are viable and protected from TNF-induced necroptosis in vivoThe molecular regulation of programmed necrotic cell injury.Programmed cell death and its role in inflammationRIP3 expression induces a death profile change in U2OS osteosarcoma cells after 5-ALA-PDT.
P2860
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P2860
Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Cleavage of RIP3 inactivates i ...... y by removal of kinase domain.
@en
type
label
Cleavage of RIP3 inactivates i ...... y by removal of kinase domain.
@en
prefLabel
Cleavage of RIP3 inactivates i ...... y by removal of kinase domain.
@en
P2093
P1433
P1476
Cleavage of RIP3 inactivates i ...... ay by removal of kinase domain
@en
P2093
Mark Castanares
Naseruddin Hoti
Shanshan Feng
Yonghui Yang
P304
P356
10.1016/J.CELLSIG.2007.05.016
P50
P577
2007-06-14T00:00:00Z