Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces death receptor 5 networks that are highly organized.
about
Candidate gene study of TRAIL and TRAIL receptors: association with response to interferon beta therapy in multiple sclerosis patients.TWEAK-independent Fn14 self-association and NF-κB activation is mediated by the C-terminal region of the Fn14 cytoplasmic domainEfficient drug delivery and induction of apoptosis in colorectal tumors using a death receptor 5-targeted nanomedicine.TRAIL and TRAIL receptors splice variants during long-term interferon β treatment of patients with multiple sclerosis: evaluation as biomarkers for therapeutic responseQuinacrine induces apoptosis in cancer cells by forming a functional bridge between TRAIL-DR5 complex and modulating the mitochondrial intrinsic cascade.Preclinical Mouse Models for Analysis of the Therapeutic Potential of Engineered Oncolytic Herpes VirusesPiecing it together: Unraveling the elusive structure-function relationship in single-pass membrane receptors.Dominant negative effects of tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) receptor 4 on TRAIL receptor 1 signaling by formation of heteromeric complexesDeath Receptor 5 Networks Require Membrane Cholesterol for Proper Structure and Function.Open and closed conformations of the isolated transmembrane domain of death receptor 5 support a new model of activation.Quantitative single-molecule localization microscopy combined with rule-based modeling reveals ligand-induced TNF-R1 reorganization toward higher-order oligomers.Death Receptor 5 Activation Is Energetically Coupled to Opening of the Transmembrane Domain Dimer.Structural Insight for Roles of DR5 Death Domain Mutations on Oligomerization of DR5 Death Domain-FADD Complex in the Death-Inducing Signaling Complex Formation: A Computational Study.Regulation of TNF-Related Apoptosis-Inducing Ligand Signaling by Glycosylation.Relationship between the agonist activity of synthetic ligands of TRAIL-R2 and their cell surface binding modes.
P2860
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P2860
Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces death receptor 5 networks that are highly organized.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Tumor necrosis factor-related ...... rks that are highly organized.
@en
type
label
Tumor necrosis factor-related ...... rks that are highly organized.
@en
prefLabel
Tumor necrosis factor-related ...... rks that are highly organized.
@en
P2093
P2860
P50
P356
P1476
Tumor necrosis factor-related ...... orks that are highly organized
@en
P2093
Andrew K Lewis
Anthony R Braun
Christopher C Valley
Deepti J Mudaliar
Jonathan N Sachs
Jonathan R Brody
P2860
P304
21265-21278
P356
10.1074/JBC.M111.306480
P407
P577
2012-04-10T00:00:00Z