Structural analysis of the Sil1–Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor

Direct inter-subdomain interactions switch between the closed and open forms of the Hsp70 nucleotide-binding domain in the nucleotide-free state

(2010) Meiri Shida et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Interactions between Kar2p and Its Nucleotide Exchange Factors Sil1p and Lhs1p Are Mechanistically Distinct

(2010) Sarah J. Hale et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The C-Terminal BAG Domain of BAG5 Induces Conformational Changes of the Hsp70 Nucleotide- Binding Domain for ADP-ATP Exchange

(2010) Akihiko Arakawa et al.   STRUCTURE

The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins

(2009) Günter Kramer et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Converging concepts of protein folding in vitro and in vivo

(2009) F Ulrich Hartl et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Heat Shock Protein 40: Structural Studies and Their Functional Implications

(2009) Jingzhi Li et al.   PROTEIN AND PEPTIDE LETTERS

Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding

(2008) Sigrun Polier et al.   CELL

Structure of the Hsp110:Hsc70 Nucleotide Exchange Machine

(2008) Jonathan P. Schuermann et al.   MOLECULAR CELL

Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2

(2008) Zhen Xu et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Marinesco-Sjögren syndrome with atrophy of the brain stem tegmentum and dysplastic cytoarchitecture in the cerebral cortex

(2008) Kenji Sakai et al.   NEUROPATHOLOGY