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Items: 8

1.

A lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with ribosomes.

Verghese J, Morano KA.

Eukaryot Cell. 2012 Aug;11(8):1003-11. doi: 10.1128/EC.00146-12. Epub 2012 May 25.

2.

GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones.

Bracher A, Verghese J.

Subcell Biochem. 2015;78:1-33. doi: 10.1007/978-3-319-11731-7_1. Review.

PMID:
25487014
3.

Ribosome-tethered molecular chaperones: the first line of defense against protein misfolding?

Craig EA, Eisenman HC, Hundley HA.

Curr Opin Microbiol. 2003 Apr;6(2):157-62. Review.

PMID:
12732306
4.

The control of spindle length by Hsp70 and Hsp110 molecular chaperones.

Makhnevych T, Houry WA.

FEBS Lett. 2013 Apr 17;587(8):1067-72. doi: 10.1016/j.febslet.2013.02.018. Epub 2013 Feb 19. Review.

5.

The ribosome-bound Hsp70 homolog Ssb of Saccharomyces cerevisiae.

Peisker K, Chiabudini M, Rospert S.

Biochim Biophys Acta. 2010 Jun;1803(6):662-72. doi: 10.1016/j.bbamcr.2010.03.005. Epub 2010 Mar 11. Review.

6.

The nucleotide exchange factors of Hsp70 molecular chaperones.

Bracher A, Verghese J.

Front Mol Biosci. 2015 Apr 7;2:10. doi: 10.3389/fmolb.2015.00010. eCollection 2015. Review.

7.

Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.

Verghese J, Abrams J, Wang Y, Morano KA.

Microbiol Mol Biol Rev. 2012 Jun;76(2):115-58. doi: 10.1128/MMBR.05018-11. Review.

8.

The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains.

Hübscher V, Mudholkar K, Rospert S.

Curr Genet. 2017 Feb;63(1):9-13. doi: 10.1007/s00294-016-0610-6. Epub 2016 May 26. Review.

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