DNAJB6 is a member of the HSP40 family of heat shock proteins (HSPs), a family of proteins
that canonically acts as co-chaperones for the refolding of misfolded and damaged proteins …

Previous studies performed in cell lines have shown that the heat shock protein, DNAJB6,
protects against the proteotoxic effects of mutant huntingtin (mut-Htt) via direct interaction …

HSP40, also known as DNAJ, belongs to a family of co-chaperones responsible for
delivering client proteins to HSP70 and stimulating HSP70 ATPase activity. The …

Several neurodegenerative diseases like Huntington's disease are initiated by protein
aggregation in neurons. These diseases are also associated with a multitude of responses …

Misfolding and aggregation are associated with cytotoxicity in polyglutamine diseases.
Molecular chaperones have been implied against disease progression although with …

Several neurodegenerative diseases like Huntington's, a polyglutamine (PolyQ) disease,
are initiated by protein aggregation in neurons. Furthermore, these diseases are also …

J-domain chaperones are involved in the efficient handover of misfolded/partially folded
proteins to Hsp70 but also function independently to protect against cell death. Due to their …

Many neurodegenerative diseases are characterized by the accumulation of misfolded
proteins, which results in loss of function of the particular proteins and may lead to neuronal …

DNAJB6 also known as mammalian relative of DnaJ (MRJ) encodes a highly conserved
member of the DnaJ/Hsp40 family of co-chaperone proteins that function with Hsp70 …

In order to be biologically active, every nascent polypeptide emerging from the ribosomes
should fold and acquire its native conformation. Non-native conformations lead to drastic …