DR5 unfolds ER stress

Nature Reviews Molecular Cell Biology

Volumn 15, Issue 8, 2014, Pages 498-499

  Zlotorynski, Eytan ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 8; DEATH RECEPTOR 5; FAS ASSOCIATED DEATH DOMAIN PROTEIN; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; MESSENGER RNA; PROTEIN IRE1; PROTEIN IRE1 ALPHA; THAPSIGARGIN; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND RECEPTOR;

APOPTOSIS; ENDOPLASMIC RETICULUM STRESS; ENZYME ACTIVATION; HUMAN; NOTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; RNA DEGRADATION; UPREGULATION; ANIMAL; PHYSIOLOGY; UNFOLDED PROTEIN RESPONSE;

ANIMALS; APOPTOSIS; ENDOPLASMIC RETICULUM STRESS; HUMANS; RECEPTORS, TNF-RELATED APOPTOSIS-INDUCING LIGAND; UNFOLDED PROTEIN RESPONSE;

EID: 84904969450     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3843     Document Type: Note

References (2)

1. Lu, M. et al. Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis. Science 345, 98-101 (2014
2. Hetz, C. The unfolded protein response: Controlling cell fate decisions under ER stress and beyond. Nature Rev. Mol. Cell Biol. 13, 89-102 (2012