Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein CH1 to initiate ER stress signaling

Crystal Structure of the Stress-Inducible Human Heat Shock Protein 70 Substrate-Binding Domain in Complex with Peptide Substrate

(2014) Pingfeng Zhang et al.   PLoS One

UPR Signal Activation by Luminal Sensor Domains

(2013) Marta Carrara et al.   INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

The impact of the unfolded protein response on human disease

(2012) Shiyu Wang et al.   JOURNAL OF CELL BIOLOGY

Conformational Selection in Substrate Recognition by Hsp70 Chaperones

(2012) Moritz Marcinowski et al.   JOURNAL OF MOLECULAR BIOLOGY

Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response

(2011) Maruf M U Ali et al.   EMBO JOURNAL

Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways

(2011) Thanyarat Promlek et al.   MOLECULAR BIOLOGY OF THE CELL

Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions

(2011) Moritz Marcinowski et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The Unfolded Protein Response: Integrating Stress Signals Through the Stress Sensor IRE1α

(2011) Claudio Hetz et al.   PHYSIOLOGICAL REVIEWS

The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation

(2011) P. Walter et al.   SCIENCE

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

(2011) B. M. Gardner et al.   SCIENCE

Activation of mammalian IRE1α upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins

(2009) Daisuke Oikawa et al.   EXPERIMENTAL CELL RESEARCH

An Unfolded CH1 Domain Controls the Assembly and Secretion of IgG Antibodies

(2009) Matthias J. Feige et al.   MOLECULAR CELL