Systems biology of death receptor networks: live and let die.

scientific article published on 29 May 2014

Systems biology of death receptor networks: live and let die. is …
instance of (P31):
review articleQ7318358
scholarly articleQ13442814

External links are
P356DOI10.1038/CDDIS.2014.160
P932PMC publication ID4047881
P698PubMed publication ID24874731
P5875ResearchGate publication ID262787739

P2093author name stringI N Lavrik
P2860cites workMathematical modeling identifies inhibitors of apoptosis as mediators of positive feedback and bistabilityQ21563509
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Mathematical modelling of cell-fate decision in response to death receptor engagementQ28473094
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Bistability in apoptosis by receptor clusteringQ28475785
Two CD95 (APO-1/Fas) signaling pathwaysQ29619631
Systems analysis of apoptosis protein expression allows the case-specific prediction of cell death responsiveness of melanoma cellsQ30549646
Quantitative analysis of pathways controlling extrinsic apoptosis in single cellsQ33807797
Stoichiometry of the CD95 death-inducing signaling complex: experimental and modeling evidence for a death effector domain chain modelQ34032305
A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell deathQ34032310
Clinical application of a systems model of apoptosis execution for the prediction of colorectal cancer therapy responses and personalisation of therapy.Q50507805
A systems model of signaling identifies a molecular basis set for cytokine-induced apoptosis.Q51307059
A mathematical model of caspase function in apoptosis.Q52076640
Understanding life and death at CD95.Q53283511
Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL.Q34069986
Generation and physiological roles of linear ubiquitin chainsQ34197025
The many roles of FAS receptor signaling in the immune systemQ34205697
XIAP discriminates between type I and type II FAS-induced apoptosisQ34205704
The caspase-8 dimerization/dissociation balance is a highly potent regulator of caspase-8, -3, -6 signalingQ34236748
Measuring and modeling apoptosis in single cellsQ34921455
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Lyapunov exponents and phase diagrams reveal multi-factorial control over TRAIL-induced apoptosisQ35682077
Kinetics in signal transduction pathways involving promiscuous oligomerizing receptors can be determined by receptor specificity: apoptosis induction by TRAIL.Q35863285
Proteasome inhibition can impair caspase-8 activation upon submaximal stimulation of apoptotic tumor necrosis factor-related apoptosis inducing ligand (TRAIL) signaling.Q35922585
Life and death in peripheral T cellsQ36858872
Activation of executioner caspases is a predictor of progression-free survival in glioblastoma patients: a systems medicine approachQ36907121
Death receptor signal transducers: nodes of coordination in immune signaling networksQ37417486
Understanding apoptosis by systems biology approachesQ37597907
The role of the kinases RIP1 and RIP3 in TNF-induced necrosisQ37721675
Systems biology of apoptosis signaling networksQ37776839
It cuts both ways: reconciling the dual roles of caspase 8 in cell death and survivalQ37947994
Cellular FLICE-like inhibitory proteins (c-FLIPs): fine-tuners of life and death decisionsQ37981778
The emerging role of linear ubiquitination in cell signalingQ37989135
Mathematical modeling of apoptosisQ38117206
Caspase-8 activity has an essential role in CD95/Fas-mediated MAPK activationQ39191656
A modular model of the apoptosis machineryQ39429538
Modeling reveals that dynamic regulation of c-FLIP levels determines cell-to-cell distribution of CD95-mediated apoptosisQ39591517
c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosisQ39644966
Non-genetic origins of cell-to-cell variability in TRAIL-induced apoptosisQ39861453
Dynamics within the CD95 death-inducing signaling complex decide life and death of cellsQ40150581
Analysis of CD95 threshold signaling: triggering of CD95 (FAS/APO-1) at low concentrations primarily results in survival signalingQ40161643
The role of CAP3 in CD95 signaling: new insights into the mechanism of procaspase-8 activationQ40369810
Rapid turnover of c-FLIPshort is determined by its unique C-terminal tailQ40424237
Selective knockdown of the long variant of cellular FLICE inhibitory protein augments death receptor-mediated caspase-8 activation and apoptosis.Q40448034
Mathematical modeling reveals threshold mechanism in CD95-induced apoptosisQ40516096
Caspase-8 cleaves its substrates from the plasma membrane upon CD95-induced apoptosisQ41218122
Systems analysis of effector caspase activation and its control by X-linked inhibitor of apoptosis proteinQ41834899
A new C-terminal cleavage product of procaspase-8, p30, defines an alternative pathway of procaspase-8 activationQ41873399
The chains of death: a new view on caspase-8 activation at the DISC.Q43245304
Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3.Q43966285
Systems modelling methodology for the analysis of apoptosis signal transduction and cell death decisions.Q44087102
Fas/CD95-induced chemokines can serve as "find-me" signals for apoptotic cellsQ45834959
Dynamics of outer mitochondrial membrane permeabilization during apoptosis.Q46167523
tBid interaction with cardiolipin primarily orchestrates mitochondrial dysfunctions and subsequently activates Bax and Bak.Q46428278
Bistability analyses of a caspase activation model for receptor-induced apoptosisQ47316430
P275copyright licenseCreative Commons Attribution-NonCommercial-ShareAlike 3.0 UnportedQ15643954
P6216copyright statuscopyrightedQ50423863
P921main subjectpeptideQ172847
membrane proteinQ423042
systems biologyQ815297
signal transductionQ828130
apoptotic processQ14599311
transport proteinQ2111029
cell surface receptorQ2476074
biomedical investigative techniqueQ66648976
apoptosis regulatory proteinsQ76931142
P304page(s)e1259
P577publication date2014-05-29
P1433published inCell Death and DiseaseQ2197222
P1476titleSystems biology of death receptor networks: live and let die.
P478volume5

Reverse relations

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