Endoplasmic reticulum stress regulation of the Kar2p/BiP chaperone alleviates proteotoxicity via dual degradation pathways

Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions

(2011) Heidi Olzscha et al.   CELL

Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response

(2011) B. M. Gardner et al.   SCIENCE

J Domain Co-chaperone Specificity Defines the Role of BiP during Protein Translocation

(2010) Shruthi S. Vembar et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Protein homeostasis and aging in neurodegeneration

(2010) Peter M. Douglas et al.   JOURNAL OF CELL BIOLOGY

Regulation of basal cellular physiology by the homeostatic unfolded protein response

(2010) D. Thomas Rutkowski et al.   JOURNAL OF CELL BIOLOGY

Evasion of Endoplasmic Reticulum Surveillance Makes Wsc1p an Obligate Substrate of Golgi Quality Control

(2010) Songyu Wang et al.   MOLECULAR BIOLOGY OF THE CELL

The Aging Stress Response

(2010) Marcia C. Haigis et al.   MOLECULAR CELL

Interplay of Substrate Retention and Export Signals in Endoplasmic Reticulum Quality Control

(2010) Shinichi Kawaguchi et al.   PLoS One

BiP Binding to the ER-Stress Sensor Ire1 Tunes the Homeostatic Behavior of the Unfolded Protein Response

(2010) David Pincus et al.   PLOS BIOLOGY

Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

(2009) Evan T. Powers et al.   Annual Review of Biochemistry

Signalling Pathways in the Unfolded Protein Response: Development from Yeast to Mammals

(2009) K. Mori   JOURNAL OF BIOCHEMISTRY

The unfolded protein response signals through high-order assembly of Ire1

(2008) Alexei V. Korennykh et al.   NATURE