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Keywords: molecular chaperones
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Articles
Biochem Soc Trans (2022) 50 (5): 1403–1414.
Published: 05 October 2022
... 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...
Articles
Biochem Soc Trans (2021) 49 (6): 2611–2625.
Published: 16 December 2021
... 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...
Articles
Biochem Soc Trans (2021) 49 (1): 365–377.
Published: 26 February 2021
... BY-NC-ND) . Open access for this article was enabled by the participation of the Walter and Eliza Hall Institute in an all-inclusive Read & Publish pilot with Portland Press and the Biochemical Society under a transformative agreement with CAUL. cytosolic proteins molecular chaperones...
Articles
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...
Articles
Biochem Soc Trans (2019) 47 (6): 1597–1608.
Published: 26 November 2019
... 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...
Articles
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...
Articles
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...