The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis
under both physiological and stress conditions in eukaryotic cells. As HSP90 has several …

The 14-3-3 proteins are a family of conserved regulatory molecules expressed in all
eukaryotic cells. A striking feature of the 14-3-3 proteins is their ability to bind a multitude of …

The tetratricopeptide repeat (TPR) motif is a protein‐protein interaction module found in
multiple copies in a number of functionally different proteins that facilitates specific …

The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and
Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of …

Magnetotactic bacteria were discovered almost 30 years ago, and for many years and many
different reasons, the number of researchers working in this field was few and progress was …

The power of molecular genetics has dramatically advanced our understanding of all
aspects of gibberellin (GA) signaling. Many genes encoding GA response pathway …

Tetratrico peptide repeat (TPR) proteins have several interesting properties, including their
folding characteristics, modular architecture and range of binding specificities. In the past …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating
many signaling proteins in the eukaryotic cell. Biochemical and structural analysis of Hsp90 …

Intraflagellar transport (IFT) is a rapid movement of multi-subunit protein particles along
flagellar microtubules and is required for assembly and maintenance of eukaryotic flagella …

The chaperone function of the mammalian 70-kDa heat shock proteins Hsc70 and Hsp70 is
modulated by physical interactions with four previously identified chaperone cofactors …