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Keywords: molecular chaperones
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Biochem Soc Trans (2021) 49 (1): 365–377.
Published: 26 February 2021
... state, proteins must properly fold with the assistance of molecular chaperones and cofactors. Under normal conditions, this can already be challenging as protein biogenesis is an error-prone process [ 2 ]. Additional factors can also hinder protein folding such as mutations and environmental stresses...
Biochem Soc Trans (2020) 48 (4): 1795–1806.
Published: 14 August 2020
... 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...
Biochem Soc Trans (2019) 47 (6): 1597–1608.
Published: 26 November 2019
... SAGA 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...
Biochem Soc Trans (2019) 47 (6): 1815–1831.
Published: 22 November 2019
... 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...
Biochem Soc Trans (2017) 45 (1): 251–260.
Published: 15 February 2017
...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 and...