@article{c05bb1e161f949c7b342b28536ba8703,
title = "Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones",
abstract = "Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation through the binding and delivery of non-native proteins to heat shock protein 70 (Hsp70). The mechanism for substrate transfer from Hsp40s to Hsp70 is unknown. Two recent studies provide new details that shed light on novel mechanisms for substrate recognition by Hsp40s and a common mechanism for polypeptide transfer to Hsp70.",
author = "Summers, {Daniel W.} and Douglas, {Peter M.} and Ramos, {Carlos H.I.} and Cyr, {Douglas M.}",
note = "Funding Information: D.W.S. is funded by a predoctoral training grant from the National Institutes of Health (NIH; 5T32GM008581–09; www.nih.gov ). P.M.D. is supported by a predoctoral fellowship from the American Heart Association ( www.americanheart.org ). C.H.I.R. is supported by grants from Funda{\c c}{\~a}o de Amparo a Pesquisa do Estado de S{\~a}o Paulo, Minist{\'e}rio da Ci{\^e}ncia e Tecnologia/Conselho Nacional de Pesquisa e Desenvolvimento and NIH-R03TW007437 funded by the Fogarty International Center ( www.fic.nih.gov ). D.M.C. is supported by funds from the NIH (5R01GM067785-06).",
year = "2009",
month = may,
doi = "10.1016/j.tibs.2008.12.009",
language = "English (US)",
volume = "34",
pages = "230--233",
journal = "Trends in biochemical sciences",
issn = "0968-0004",
publisher = "Elsevier Limited",
number = "5",
}