@article{dcc5ffa04daa4ec98d76013cde226e18,
title = "Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates",
abstract = "Background: Hsp110s are considered as mere nucleotide exchange factors of the Hsp70s. Results: Human cytosolic Hsp110s can use ATP to unfold misfolded polypeptides and act as equal partner with Hsp70 to solubilize stable protein aggregates. Conclusion: Hsp110s are Hsp70-like polypeptide unfolding chaperones. Significance: Hsp110s are powerful disaggregating chaperones that can collaborate with Hsp70s to detoxify misfolding proteins in degenerative diseases.",
author = "Mattoo, \{Rayees U.H.\} and Sharma, \{Sandeep K.\} and Smriti Priya and Andrija Finka and Pierre Goloubinoff",
year = "2013",
month = jul,
day = "19",
doi = "10.1074/jbc.M113.479253",
language = "אנגלית",
volume = "288",
pages = "21399--21411",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "29",
}