The molecular chaperone CCT/TRiC: an essential component of proteostasis and a potential modulator of protein aggregation
J Grantham - Frontiers in genetics, 2020 - frontiersin.org
Chaperonin containing tailless complex polypeptide 1 (CCT) or tailless complex polypeptide
1 ring complex (TRiC) is an essential eukaryotic molecular chaperone. It is a multi-subunit …
1 ring complex (TRiC) is an essential eukaryotic molecular chaperone. It is a multi-subunit …
The TRiCky business of protein folding in health and disease
H Ghozlan, A Cox, D Nierenberg, S King… - Frontiers in Cell and …, 2022 - frontiersin.org
Maintenance of the cellular proteome or proteostasis is an essential process that when
deregulated leads to diseases like neurological disorders and cancer. Central to …
deregulated leads to diseases like neurological disorders and cancer. Central to …
CCT complex restricts neuropathogenic protein aggregation via autophagy
M Pavel, S Imarisio, FM Menzies… - Nature …, 2016 - nature.com
Aberrant protein aggregation is controlled by various chaperones, including CCT
(chaperonin containing TCP-1)/TCP-1/TRiC. Mutated CCT4/5 subunits cause sensory …
(chaperonin containing TCP-1)/TCP-1/TRiC. Mutated CCT4/5 subunits cause sensory …
Multi-scale 3D cryo-correlative microscopy for vitrified cells
Summary Three-dimensional (3D) visualization of vitrified cells can uncover structures of
subcellular complexes without chemical fixation or staining. Here, we present a pipeline …
subcellular complexes without chemical fixation or staining. Here, we present a pipeline …
TRiC subunits enhance BDNF axonal transport and rescue striatal atrophy in Huntington's disease
Corticostriatal atrophy is a cardinal manifestation of Huntington's disease (HD). However,
the mechanism (s) by which mutant huntingtin (mHTT) protein contributes to the …
the mechanism (s) by which mutant huntingtin (mHTT) protein contributes to the …
CryoET reveals organelle phenotypes in huntington disease patient iPSC-derived and mouse primary neurons
Huntington's disease (HD) is caused by an expanded CAG repeat in the huntingtin gene,
yielding a Huntingtin protein with an expanded polyglutamine tract. While experiments with …
yielding a Huntingtin protein with an expanded polyglutamine tract. While experiments with …
[HTML][HTML] Protofilament structure and supramolecular polymorphism of aggregated mutant huntingtin exon 1
Huntington's disease is a progressive neurodegenerative disease caused by expansion of
the polyglutamine domain in the first exon of huntingtin (HttEx1). The extent of expansion …
the polyglutamine domain in the first exon of huntingtin (HttEx1). The extent of expansion …
[HTML][HTML] Tadpole-like conformations of huntingtin exon 1 are characterized by conformational heterogeneity that persists regardless of polyglutamine length
Abstract Soluble huntingtin exon 1 (Httex1) with expanded polyglutamine (polyQ) engenders
neurotoxicity in Huntington's disease. To uncover the physical basis of this toxicity, we …
neurotoxicity in Huntington's disease. To uncover the physical basis of this toxicity, we …
Cryo-electron tomography provides topological insights into mutant huntingtin exon 1 and polyQ aggregates
Huntington disease (HD) is a neurodegenerative trinucleotide repeat disorder caused by an
expanded poly-glutamine (polyQ) tract in the mutant huntingtin (mHTT) protein. The …
expanded poly-glutamine (polyQ) tract in the mutant huntingtin (mHTT) protein. The …
Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract
Many neurodegenerative diseases are linked to amyloid aggregation. In Huntington's
disease (HD), neurotoxicity correlates with an increased aggregation propensity of a …
disease (HD), neurotoxicity correlates with an increased aggregation propensity of a …