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Items: 1 to 20 of 61

1.

[PIN+]ing down the mechanism of prion appearance.

Serio TR.

FEMS Yeast Res. 2018 May 1;18(3). doi: 10.1093/femsyr/foy026.

2.

Nonsense-mediated mRNA decay factors cure most [PSI+] prion variants.

Son M, Wickner RB.

Proc Natl Acad Sci U S A. 2018 Feb 6;115(6):E1184-E1193. doi: 10.1073/pnas.1717495115. Epub 2018 Jan 22.

PMID:
29358398
3.

Curing of [PSI+] by Hsp104 Overexpression: Clues to solving the puzzle.

Greene LE, Zhao X, Eisenberg E.

Prion. 2018 Jan 2;12(1):9-15. doi: 10.1080/19336896.2017.1412911. Epub 2018 Feb 2.

PMID:
29227184
4.

Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase.

Lee J, Sung N, Yeo L, Chang C, Lee S, Tsai FTF.

Biosci Rep. 2017 Dec 22;37(6). pii: BSR20171399. doi: 10.1042/BSR20171399. Print 2017 Dec 22.

5.

[PSI+] prion propagation is controlled by inositol polyphosphates.

Wickner RB, Kelly AC, Bezsonov EE, Edskes HK.

Proc Natl Acad Sci U S A. 2017 Oct 3;114(40):E8402-E8410. doi: 10.1073/pnas.1714361114. Epub 2017 Sep 18.

6.

Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation.

Lee J, Sung N, Mercado JM, Hryc CF, Chang C, Lee S, Tsai FTF.

Sci Rep. 2017 Sep 11;7(1):11184. doi: 10.1038/s41598-017-11474-9.

7.

The life of [PSI].

Cox B, Tuite M.

Curr Genet. 2018 Feb;64(1):1-8. doi: 10.1007/s00294-017-0714-7. Epub 2017 Jun 26. Review.

8.

Hsp104 disaggregase at normal levels cures many [PSI+] prion variants in a process promoted by Sti1p, Hsp90, and Sis1p.

Gorkovskiy A, Reidy M, Masison DC, Wickner RB.

Proc Natl Acad Sci U S A. 2017 May 23;114(21):E4193-E4202. doi: 10.1073/pnas.1704016114. Epub 2017 May 8.

9.

Heat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs.

Zhao X, Rodriguez R, Silberman RE, Ahearn JM, Saidha S, Cummins KC, Eisenberg E, Greene LE.

J Biol Chem. 2017 May 26;292(21):8630-8641. doi: 10.1074/jbc.M116.770719. Epub 2017 Apr 3.

10.

Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.

Langlois CR, Pei F, Sindi SS, Serio TR.

PLoS Genet. 2016 Nov 4;12(11):e1006417. doi: 10.1371/journal.pgen.1006417. eCollection 2016 Nov.

11.

Molecular chaperones: guardians of the proteome in normal and disease states.

Jeng W, Lee S, Sung N, Lee J, Tsai FT.

F1000Res. 2015 Dec 15;4. pii: F1000 Faculty Rev-1448. doi: 10.12688/f1000research.7214.1. eCollection 2015. Review.

12.

Human J-protein DnaJB6b Cures a Subset of Saccharomyces cerevisiae Prions and Selectively Blocks Assembly of Structurally Related Amyloids.

Reidy M, Sharma R, Roberts BL, Masison DC.

J Biol Chem. 2016 Feb 19;291(8):4035-47. doi: 10.1074/jbc.M115.700393. Epub 2015 Dec 23.

13.

Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.

Sweeny EA, Shorter J.

J Mol Biol. 2016 May 8;428(9 Pt B):1870-85. doi: 10.1016/j.jmb.2015.11.016. Epub 2015 Dec 1. Review.

14.

Yeast prions are useful for studying protein chaperones and protein quality control.

Masison DC, Reidy M.

Prion. 2015;9(3):174-83. doi: 10.1080/19336896.2015.1027856. Review.

15.

Yeast prions: structure, biology, and prion-handling systems.

Wickner RB, Shewmaker FP, Bateman DA, Edskes HK, Gorkovskiy A, Dayani Y, Bezsonov EE.

Microbiol Mol Biol Rev. 2015 Mar;79(1):1-17. doi: 10.1128/MMBR.00041-14. Review.

16.

The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation.

Sweeny EA, Jackrel ME, Go MS, Sochor MA, Razzo BM, DeSantis ME, Gupta K, Shorter J.

Mol Cell. 2015 Mar 5;57(5):836-849. doi: 10.1016/j.molcel.2014.12.021. Epub 2015 Jan 22.

17.

Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.

Reidy M, Sharma R, Shastry S, Roberts BL, Albino-Flores I, Wickner S, Masison DC.

PLoS Genet. 2014 Oct 16;10(10):e1004720. doi: 10.1371/journal.pgen.1004720. eCollection 2014 Oct.

18.

Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds.

Park YN, Zhao X, Yim YI, Todor H, Ellerbrock R, Reidy M, Eisenberg E, Masison DC, Greene LE.

Eukaryot Cell. 2014 May;13(5):635-47. doi: 10.1128/EC.00300-13. Epub 2014 Mar 14.

19.

Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.

Dulle JE, Stein KC, True HL.

PLoS One. 2014 Jan 23;9(1):e87521. doi: 10.1371/journal.pone.0087521. eCollection 2014.

20.

The BAG homology domain of Snl1 cures yeast prion [URE3] through regulation of Hsp70 chaperones.

Kumar N, Gaur D, Masison DC, Sharma D.

G3 (Bethesda). 2014 Mar 20;4(3):461-70. doi: 10.1534/g3.113.009993.

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