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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...
Articles
Essays Biochem (2016) 60 (2): 143–151.
Published: 15 October 2016
... E3A)/E6-AP (E6-associated protein) E3 ligase Angelman syndrome [ 44 ] ATXN3/ataxin 3 DUB Spinocerebellar ataxia 3 [ 45 ] SACS/sacsin UBL domain (chaperone) Spastic ataxia [ 46 ] DNAJB2/HSJ1 Ubiquitin-binding (chaperone) Distal hereditary motor neuropathy [ 47 ] UBA1/UBE1 E1...
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
... 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
... chaperone (−)-epigallocatechin gallate (EGCG) Huntington's disease inclusion body nucleation-dependent polymerization polyglutamine disease protein aggregation PolyQ (polyglutamine) tracts with lengths of between five and 30 glutamine residues are conserved and found in 0.34% of all human...