The Hsp90 Cochaperones Cpr6, Cpr7, and Cns1 Interact with the Intact Ribosome

Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones

(2014) Jill L. Johnson et al.   CURRENT GENETICS

The Ribosomal Biogenesis Protein Utp21 Interacts with Hsp90 and Has Differing Requirements for Hsp90-Associated Proteins

(2014) Victoria R. Tenge et al.   PLoS One

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

(2014) T. Saio et al.   SCIENCE

Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity

(2013) Annerleim Walton-Diaz et al.   Future Medicinal Chemistry

Interaction of Heat Shock Protein 90 and the Co-chaperone Cpr6 with Ura2, a Bifunctional Enzyme Required for Pyrimidine Biosynthesis

(2013) Abbey D. Zuehlke et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Cotranslational Response to Proteotoxic Stress by Elongation Pausing of Ribosomes

(2013) Botao Liu et al.   MOLECULAR CELL

Widespread Regulation of Translation by Elongation Pausing in Heat Shock

(2013) Reut Shalgi et al.   MOLECULAR CELL

Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle

(2013) Jing Li et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Structure of the TPR Domain of AIP: Lack of Client Protein Interaction with the C-Terminal α-7 Helix of the TPR Domain of AIP Is Sufficient for Pituitary Adenoma Predisposition

(2013) Rhodri M. L. Morgan et al.   PLoS One

A Lysine-Rich Region within Fungal BAG Domain-Containing Proteins Mediates a Novel Association with Ribosomes

(2012) Jacob Verghese et al.   EUKARYOTIC CELL

Chaperoning the Chaperone: A Role for the Co-chaperone Cpr7 in Modulating Hsp90 Function in Saccharomyces cerevisiae

(2012) Abbey D. Zuehlke et al.   GENETICS

Uncovering a Region of Heat Shock Protein 90 Important for Client Binding in E. coli and Chaperone Function in Yeast

(2012) Olivier Genest et al.   MOLECULAR CELL

Structural characterization of a eukaryotic chaperone—the ribosome-associated complex

(2012) Christoph Leidig et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Ribosome-associated chaperones as key players in proteostasis

(2012) Steffen Preissler et al.   TRENDS IN BIOCHEMICAL SCIENCES

The TPR Domain in the Host Cyp40-like Cyclophilin Binds to the Viral Replication Protein and Inhibits the Assembly of the Tombusviral Replicase

(2012) Jing-Yi Lin et al.   PLoS Pathogens

The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones

(2011) Jing Li et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

Cyclophilin 40 facilitates HSP90-mediated RISC assembly in plants

(2011) Taichiro Iki et al.   EMBO JOURNAL

Structure of Minimal Tetratricopeptide Repeat Domain Protein Tah1 Reveals Mechanism of Its Interaction with Pih1 and Hsp90

(2011) Beatriz Jiménez et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Global Functional Map of the p23 Molecular Chaperone Reveals an Extensive Cellular Network

(2011) Frank J. Echtenkamp et al.   MOLECULAR CELL

Heterozygous Yeast Deletion Collection Screens Reveal Essential Targets of Hsp90

(2011) Eric A. Franzosa et al.   PLoS One

Inhibition of cyclophilins alters lipid trafficking and blocks hepatitis C virus secretion

(2011) Leah J Anderson et al.   Virology Journal

PPIase domain of trigger factor acts as auxiliary chaperone site to assist the folding of protein substrates bound to the crevice of trigger factor

(2010) Chuan-Peng Liu et al.   INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY

Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle

(2010) Jing Li et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Nuclear transport of protein TTC4 depends on the cell cycle

(2009) Ruslan I. Dmitriev et al.   CELL AND TISSUE RESEARCH

The Human TPR Protein TTC4 Is a Putative Hsp90 Co-Chaperone Which Interacts with CDC6 and Shows Alterations in Transformed Cells

(2008) Gilles Crevel et al.   PLoS One