... molecular chaperones protein folding single-molecule force spectroscopy single-molecule FRET The 70-kDa heat shock proteins (Hsp70s) form the central hub of the proteostasis network, which is involved in a number of cellular processes, including assisting the folding of nascent peptide chains...

... Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) . EMC ion channel assembly molecular chaperones voltage-gated ion channel Ion channels are multisubunit protein complexes that create the spark of life by producing the electrical signals that drive our...

... chaperones oxidative stress protein aggregation proteostasis redox signalling Molecular chaperones are highly conserved proteins that assist polypeptides in acquiring or retaining their native, functional conformation. Client recognition and binding are typically based on a combination...

... by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) . cryo-electron microscopy molecular chaperones molecular mechanisms protein conformation All organisms depend on properly folded and functioning proteins...

... homeostasis. Consequently, ECM production must be carefully balanced with turnover to ensure homeostasis; ECM dysfunction culminates in disease. Hsp90 is a molecular chaperone central to protein homeostasis, including in the ECM. Intracellular and extracellular Hsp90 isoforms collaborate to regulate...

... molecular chaperones protein misfolding protein quality control ubiquitin ubiquitin proteasome system The proper functioning of proteins in cells is critical for all forms of life. Proteins serve as the molecular machines that facilitate a wide array of life-giving processes. The normal cellular...

... prone SOD1 also interacts with heat shock proteins and macrophage migration inhibitory factor to aid folding, refolding or degradation. Recognition of specific SOD1 structures by the molecular chaperone network and timely dissociation of SOD1-chaperone complexes are, therefore, important steps in SOD1...

... and NuA4/TIP60 complex assembly and recruitment to chromatin. We further discuss its evolutionary history within the PIKK family and highlight recent findings that reveal the importance of molecular chaperones in pseudokinase folding, function, and conservation. Correspondence: Dominique Helmlinger...

... isomerization of peptidyl-prolyl peptide bonds in unfolded and partially folded polypeptide chains and native state proteins. Originally, both proteins have been studied as molecular chaperones belonging to the steroid receptor heterocomplex, where they were first discovered. In addition to their expected role...

...Carol V. Robinson Twenty-five years ago, we obtained our first mass spectra of molecular chaperones in complex with protein ligands and entered a new field of gas-phase structural biology. It is perhaps now time to pause and reflect, and to ask how many of our initial structure predictions...