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FLIP(L) determines p53 induced life or death
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1016/0092-8674(92)90644-ropenalex-snapshot
The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
inferredcites →https://doi.org/10.1016/0092-8674(93)90499-gopenalex-snapshot
The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
inferredcites →https://doi.org/10.1016/0092-8674(93)90500-popenalex-snapshot
WAF1, a potential mediator of p53 tumor suppression
inferredcites →https://doi.org/10.1016/j.bbcan.2014.07.010openalex-snapshot
Histone deacetylase 2 controls p53 and is a critical factor in tumorigenesis
inferredcites →https://doi.org/10.1016/j.ccr.2004.08.012openalex-snapshot
Inhibition of NF-κB in cancer cells converts inflammation- induced tumor growth mediated by TNFα to TRAIL-mediated tumor regression
inferredcites →https://doi.org/10.1016/j.cell.2008.03.025openalex-snapshot
Acetylation Is Indispensable for p53 Activation
inferredcites →https://doi.org/10.1016/j.cell.2016.03.025openalex-snapshot
Cell-to-Cell Variation in p53 Dynamics Leads to Fractional Killing
inferredcites →https://doi.org/10.1016/j.celrep.2017.04.010openalex-snapshot
Caspase-10 Negatively Regulates Caspase-8-Mediated Cell Death, Switching the Response to CD95L in Favor of NF-κB Activation and Cell Survival
inferredcites →https://doi.org/10.1016/j.devcel.2010.10.015openalex-snapshot
Hdac1 and Hdac2 Act Redundantly to Control p63 and p53 Functions in Epidermal Progenitor Cells
inferredcites →https://doi.org/10.1016/j.dnarep.2011.10.014openalex-snapshot
The HDAC inhibitor depsipeptide transactivates the p53/p21 pathway by inducing DNA damage
inferredcites →https://doi.org/10.1016/j.molcel.2006.11.026openalex-snapshot
Acetylation of the p53 DNA-Binding Domain Regulates Apoptosis Induction
inferredcites →https://doi.org/10.1016/j.molcel.2013.08.048openalex-snapshot
BID Preferentially Activates BAK while BIM Preferentially Activates BAX, Affecting Chemotherapy Response
inferredcites →https://doi.org/10.1016/j.molcel.2015.02.015openalex-snapshot
The p53 C Terminus Controls Site-Specific DNA Binding and Promotes Structural Changes within the Central DNA Binding Domain
inferredcites →https://doi.org/10.1016/s0092-8674(00)80416-xopenalex-snapshot
DNA Damage-Induced Phosphorylation of p53 Alleviates Inhibition by MDM2
inferredcites →https://doi.org/10.1016/s1097-2765(01)00214-3openalex-snapshot
PUMA, a Novel Proapoptotic Gene, Is Induced by p53
inferredcites →https://doi.org/10.1016/s1535-6108(04)00114-xopenalex-snapshot
Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis
inferredcites →https://doi.org/10.1021/jm501092zopenalex-snapshot
Small-Molecule Inhibitors of the MDM2–p53 Protein–Protein Interaction (MDM2 Inhibitors) in Clinical Trials for Cancer Treatment
inferredcites →https://doi.org/10.1038/cdd.2012.89openalex-snapshot
Insights into p53 transcriptional function via genome-wide chromatin occupancy and gene expression analysis
inferredcites →https://doi.org/10.1038/cddis.2015.213openalex-snapshot
DED or alive: assembly and regulation of the death effector domain complexes
inferredcites →https://doi.org/10.1038/nchembio.313openalex-snapshot
Chemical phylogenetics of histone deacetylases
inferredcites →https://doi.org/10.1038/ncomms4350openalex-snapshot
Differential affinity of FLIP and procaspase 8 for FADD’s DED binding surfaces regulates DISC assembly
inferredcites →https://doi.org/10.1038/nrc2731openalex-snapshot
20 years studying p53 functions in genetically engineered mice
inferredcites →https://doi.org/10.1038/nrc2763openalex-snapshot
Awakening guardian angels: drugging the p53 pathway
inferredcites →https://doi.org/10.1038/nrc3430openalex-snapshot
MDM2, MDMX and p53 in oncogenesis and cancer therapy
inferredcites →https://doi.org/10.1038/nrd4236openalex-snapshot
Drugging the p53 pathway: understanding the route to clinical efficacy
inferredcites →https://doi.org/10.1038/nrd4288openalex-snapshot
Erratum: Drugging the p53 pathway: understanding the route to clinical efficacy
inferredcites →https://doi.org/10.1038/nrd4583openalex-snapshot
HDAC inhibitors still need a home run, despite recent approval
inferredcites →https://doi.org/10.1038/onc.2008.366openalex-snapshot
Combined inhibition of FLIP and XIAP induces Bax-independent apoptosis in type II colorectal cancer cells
inferredcites →https://doi.org/10.1038/onc.2014.86openalex-snapshot
Targeting colon cancer cell NF-κB promotes an anti-tumour M1-like macrophage phenotype and inhibits peritoneal metastasis
inferredcites →https://doi.org/10.1038/s41467-019-11046-7openalex-snapshot
Chemical genomics reveals histone deacetylases are required for core regulatory transcription
inferredcites →https://doi.org/10.1038/sj.leu.2404760openalex-snapshot
Apoptosis induced by histone deacetylase inhibitors in leukemic cells is mediated by Bim and Noxa
inferredcites →https://doi.org/10.1038/sj.onc.1203489openalex-snapshot
Wild-type p53 transactivates the KILLER/DR5 gene through an intronic sequence-specific DNA-binding site
inferredcites →https://doi.org/10.1038/sj.onc.1209122openalex-snapshot
c-FLIP inhibits chemotherapy-induced colorectal cancer cell death
inferredcites →https://doi.org/10.1073/pnas.0507493103openalex-snapshot
Small-molecule MDM2 antagonists reveal aberrant p53 signaling in cancer: Implications for therapy
inferredcites →https://doi.org/10.1073/pnas.0813333106openalex-snapshot
A panel of isogenic human cancer cells suggests a therapeutic approach for cancers with inactivated p53
inferredcites →https://doi.org/10.1073/pnas.1008522107openalex-snapshot
Histone deacetylase inhibitor induces DNA damage, which normal but not transformed cells can repair
inferredcites →https://doi.org/10.1073/pnas.1417549111openalex-snapshot
Loss of p53 induces cell proliferation via Ras-independent activation of the Raf/Mek/Erk signaling pathway
inferredcites →https://doi.org/10.1073/pnas.241358198openalex-snapshot
Caspase-10 is an initiator caspase in death receptor signaling
inferredcites →https://doi.org/10.1074/jbc.m000202200openalex-snapshot
Histone Deacetylases Specifically Down-regulate p53-dependent Gene Activation
inferredcites →https://doi.org/10.1074/jbc.m110.184663openalex-snapshot
Deacetylation of the DNA-binding Domain Regulates p53-mediated Apoptosis
inferredcites →https://doi.org/10.1080/13543784.2017.1353077openalex-snapshot
Entinostat for the treatment of breast cancer
inferredcites →https://doi.org/10.1083/jcb.200512059openalex-snapshot
Distinct p53 acetylation cassettes differentially influence gene-expression patterns and cell fate
inferredcites →https://doi.org/10.1084/jem.188.11.2033openalex-snapshot
p53 Activates the CD95 (APO-1/Fas) Gene in Response to DNA Damage by Anticancer Drugs
inferredcites →https://doi.org/10.1093/emboj/cdf441openalex-snapshot
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
inferredcites →https://doi.org/10.1093/emboj/cdf616openalex-snapshot
MDM2–HDAC1‐mediated deacetylation of p53 is required for its degradation
inferredcites →https://doi.org/10.1093/nar/30.1.207openalex-snapshot
Gene Expression Omnibus: NCBI gene expression and hybridization array data repository
inferredcites →https://doi.org/10.1093/nar/gku299openalex-snapshot
Genome-wide characterization reveals complex interplay between TP53 and TP63 in response to genotoxic stress
inferredcites →https://doi.org/10.1093/nar/gkw377openalex-snapshot
Enrichr: a comprehensive gene set enrichment analysis web server 2016 update
inferredcites →https://doi.org/10.1093/nar/gkw523openalex-snapshot
Integration of TP53, DREAM, MMB-FOXM1 and RB-E2F target gene analyses identifies cell cycle gene regulatory networks
inferredcites →https://doi.org/10.1111/febs.14523openalex-snapshot
FLIP as a therapeutic target in cancer
inferredcites →https://doi.org/10.1126/science.1090072openalex-snapshot
p53- and Drug-Induced Apoptotic Responses Mediated by BH3-Only Proteins Puma and Noxa
inferredcites →https://doi.org/10.1126/science.1092472openalex-snapshot
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
inferredcites →https://doi.org/10.1126/science.1247005openalex-snapshot
Genome-Scale CRISPR-Cas9 Knockout Screening in Human Cells
inferredcites →https://doi.org/10.1128/mcb.00494-07openalex-snapshot
Role for Histone Deacetylase 1 in Human Tumor Cell Proliferation
inferredcites →https://doi.org/10.1158/0008-5472.can-06-4397openalex-snapshot
Histone Deacetylase 2 Modulates p53 Transcriptional Activities through Regulation of p53-DNA Binding Activity
inferredcites →https://doi.org/10.1186/s13059-014-0554-4openalex-snapshot
MAGeCK enables robust identification of essential genes from genome-scale CRISPR/Cas9 knockout screens
inferredcites →https://doi.org/10.1242/jcs.084723openalex-snapshot
p63 maintains keratinocyte proliferative capacity through regulation of Skp2–p130 levels
inferredcites →https://doi.org/10.1523/jneurosci.5214-12.2013openalex-snapshot
Specific Acetylation of p53 by HDAC Inhibition Prevents DNA Damage-Induced Apoptosis in Neurons
inferredcites →https://doi.org/10.1593/neo.81358openalex-snapshot
Acetylation of FoxO1 Activates Bim Expression to Induce Apoptosis in Response to Histone Deacetylase Inhibitor Depsipeptide Treatment
inferredcites →https://doi.org/10.18632/oncotarget.1436openalex-snapshot
Lysine-specific modifications of p53: a matter of life and death?
inferredcites →https://doi.org/10.4161/15384101.2014.949083openalex-snapshot
The transcription factor p53: Not a repressor, solely an activator
inferredcites →https://doi.org/10.4161/cc.6420openalex-snapshot
Multiple p53-independent gene silencing mechanisms define the cellular response to p53 activation
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.70675/1a8e6d5bzc60fz4d57z9f05zbbc81aeec00aopenalex-snapshot
Étude de l’origine moléculaire de l’hétérogénéité de réponse cellulaire à TRAIL et son rôle dans la résistance non-génétique
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