The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization

An unfolded protein-induced conformational switch activates mammalian IRE1

(2017) G Elif Karagöz et al.   eLife

The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins

(2016) Peng Wang et al.   Acta Crystallographica Section D-Structural Biology

Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling

(2015) M. Carrara et al.   EMBO JOURNAL

The structure of the PERK kinase domain suggests the mechanism for its activation

(2011) Wenjun Cui et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex

(2011) Daniel R. Southworth et al.   MOLECULAR CELL

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

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Versatility of Trigger Factor Interactions with Ribosome-Nascent Chain Complexes

(2010) Sathish Kumar Lakshmipathy et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Crystal Structure of P58(IPK) TPR Fragment Reveals the Mechanism for its Molecular Chaperone Activity in UPR

(2010) Jiahui Tao et al.   JOURNAL OF MOLECULAR BIOLOGY

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

(2010) Mikko Taipale et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Substrate binding site flexibility of the small heat shock protein molecular chaperones

(2009) N. Jaya et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA