The HSP70 chaperone machinery: J proteins as drivers of functional specificity

HH Kampinga, EA Craig - Nature reviews Molecular cell biology, 2010 - nature.com
Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in
a myriad of biological processes, modulating polypeptide folding, degradation and …

Heat shock proteins: cellular and molecular mechanisms in the central nervous system

RA Stetler, Y Gan, W Zhang, AK Liou, Y Gao… - Progress in …, 2010 - Elsevier
Emerging evidence indicates that heat shock proteins (HSPs) are critical regulators in
normal neural physiological function as well as in cell stress responses. The functions of …

[HTML][HTML] A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation

J Hageman, MA Rujano, MAWH Van Waarde, V Kakkar… - Molecular cell, 2010 - cell.com
Misfolding and aggregation are associated with cytotoxicity in several protein folding
diseases. A large network of molecular chaperones ensures protein quality control. Here, we …

CDK12 regulates alternative last exon mRNA splicing and promotes breast cancer cell invasion

JF Tien, A Mazloomian, SWG Cheng… - Nucleic acids …, 2017 - academic.oup.com
Abstract CDK12 (cyclin-dependent kinase 12) is a regulatory kinase with evolutionarily
conserved roles in modulating transcription elongation. Recent tumor genome studies of …

DNAJ Proteins in neurodegeneration: essential and protective factors

C Zarouchlioti, DA Parfitt, W Li… - … of the Royal …, 2018 - royalsocietypublishing.org
Maintenance of protein homeostasis is vitally important in post-mitotic cells, particularly
neurons. Neurodegenerative diseases such as polyglutamine expansion disorders—like …

HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones

MJ Vos, MP Zijlstra, B Kanon… - Human molecular …, 2010 - academic.oup.com
A small number of heat-shock proteins have previously been shown to act protectively on
aggregation of several proteins containing an extended polyglutamine (polyQ) stretch, which …

Exome sequencing reveals DNAJB6 mutations in dominantly‐inherited myopathy

MB Harms, RB Sommerville, P Allred, S Bell… - Annals of …, 2012 - Wiley Online Library
Objective: To identify the causative gene in an autosomal dominant limb‐girdle muscular
dystrophy (LGMD) with skeletal muscle vacuoles. Methods: Exome sequencing was used to …

[HTML][HTML] Neuromuscular diseases due to chaperone mutations: a review and some new results

J Sarparanta, PH Jonson, S Kawan, B Udd - International journal of …, 2020 - mdpi.com
Skeletal muscle and the nervous system depend on efficient protein quality control, and they
express chaperones and cochaperones at high levels to maintain protein homeostasis …

[HTML][HTML] DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios

C Månsson, V Kakkar, E Monsellier, Y Sourigues… - Cell stress and …, 2014 - Elsevier
Expanded polyglutamine (polyQ) stretches lead to protein aggregation and severe
neurodegenerative diseases. A highly efficient suppressor of polyQ aggregation was …

Suppression of protein aggregation by chaperone modification of high molecular weight complexes

J Labbadia, SS Novoselov, JS Bett, A Weiss… - Brain, 2012 - academic.oup.com
Protein misfolding and aggregation are associated with many neurodegenerative diseases,
including Huntington's disease. The cellular machinery for maintaining proteostasis includes …