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Keywords: chaperone
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Articles
Essays Biochem (2019) 63 (1): 29–43.
Published: 22 March 2019
..., they require an extensive repertoire of interacting proteins collectively known as ‘histone chaperones’. At a fundamental level, it is believed that histone chaperones guide the assembly of nucleosomes through preventing non-productive charge-based aggregates between the basic histones and acidic cellular...
Articles
Essays Biochem (2016) 60 (2): 143–151.
Published: 15 October 2016
... by Portland Press Limited on behalf of the Biochemical Society 2016 autophagy chaperone DUB E3 proteasome protein aggregation protein misfolding proteostasis ubiquitin ubiquitin-like modifier UBL UPS The correct folding of cellular proteins to the native state is essential...
Articles
Essays Biochem (2016) 60 (2): 237–253.
Published: 15 October 2016
...Patricija van Oosten-Hawle; Yael Bar-Lavan; Netta Shemesh; Anat Ben-Zvi Quality control is an essential aspect of cellular function, with protein folding quality control being carried out by molecular chaperones, a diverse group of highly conserved proteins that specifically identify misfolded...
Articles
Essays Biochem (2014) 56: 53–68.
Published: 18 August 2014
... and folding proteins, called protein homoeostasis, is required for every aspect of cellular functionality. Protective proteins called chaperones are expressed under extreme conditions in order to prevent aggregation of cellular proteins and safeguard protein quality. These chaperones co-operate during de novo...
Articles
Essays Biochem (2014) 56: 167–180.
Published: 18 August 2014
... and in vivo . The potential implications of such studies for the development of novel therapeutic strategies are discussed. 1 To whom correspondence should be addressed (email ewanker@mdc-berlin.de ). © The Authors Journal compilation © 2014 Biochemical Society 2014 chaperone...