Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1
about
Endoplasmic reticulum stress: cell life and death decisions.Genome wide analysis of common and specific stress responses in adult drosophila melanogasterTranscriptional signature of an adult brain tumor in DrosophilaInhibition of Translation and Induction of Apoptosis by Bunyaviral Nonstructural Proteins Bearing Sequence Similarity to ReaperMolecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitinationInhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding proteinA novel ubiquitin fusion system bypasses the mitochondria and generates biologically active Smac/DIABLOA fluorescent reporter of caspase activity for live imaging.Amsacta moorei Entomopoxvirus inhibitor of apoptosis suppresses cell death by binding Grim and Hidechinus, required for interommatidial cell sorting and cell death in the Drosophila pupal retina, encodes a protein with homology to ubiquitin-specific proteases.The role of ubiquitylation for the control of cell death in DrosophilaMechanisms of apoptosis in Crustacea: What conditions induce versus suppress cell death?Multiple mechanisms modulate distinct cellular susceptibilities toward apoptosis in the developing Drosophila eye.The dREAM/Myb-MuvB complex and Grim are key regulators of the programmed death of neural precursor cells at the Drosophila posterior wing margin.The domains of apoptosis: a genomics perspective.Apical deficiency triggers JNK-dependent apoptosis in the embryonic epidermis of DrosophilaTargeting endogenous inhibitors of apoptosis for treatment of cancer, stroke and multiple sclerosis.The protein structures that shape caspase activity, specificity, activation and inhibition.Fork head controls the timing and tissue selectivity of steroid-induced developmental cell death.The role of peroxiredoxin 4 in inflammatory response and aging.The role of mitochondria in apoptosis*.DIAP2 functions as a mechanism-based regulator of drICE that contributes to the caspase activity threshold in living cellsThe effect of peroxiredoxin 4 on fly physiology is a complex interplay of antioxidant and signaling functionsLack of involvement of mitochondrial factors in caspase activation in a Drosophila cell-free systemRegulation of apoptosis in Drosophila.Genetic control of programmed cell death (apoptosis) in Drosophila.Regulation of Apoptosis by Inhibitors of Apoptosis (IAPs)Apoptosis in Drosophila: which role for mitochondria?Drosophila Omi, a mitochondrial-localized IAP antagonist and proapoptotic serine protease.IAP-antagonists exhibit non-redundant modes of action through differential DIAP1 binding.Smac3, a novel Smac/DIABLO splicing variant, attenuates the stability and apoptosis-inhibiting activity of X-linked inhibitor of apoptosis protein.Predictive inference on cytoplasmic and mitochondrial thioredoxin peroxidases in the highly radioresistant Lepidopteran insect Spodoptera frugiperda.Reaper homologue IBM1 in silkworm Bombyx mori induces apoptosis upon baculovirus infection.IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms.Smac/DIABLO selectively reduces the levels of c-IAP1 and c-IAP2 but not that of XIAP and livin in HeLa cells.Changes in Neuronal Signaling and Cell Stress Response Pathways are Associated with a Multigenic Response of Drosophila melanogaster to DDT Selection.Review: BIR containing proteins (BIRPs): More than just cell death inhibitors
P2860
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P2860
Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1
@en
Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1.
@nl
type
label
Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1
@en
Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1.
@nl
prefLabel
Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1
@en
Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1.
@nl
P2093
P2860
P356
P1433
P1476
Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1
@en
P2093
Angela Paul
Anna Zachariou
Rebecca Wilson
Tencho Tenev
P2860
P304
P356
10.1093/EMBOJ/CDF530
P407
P50
P577
2002-10-01T00:00:00Z