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Items: 1 to 20 of 146


Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.

O'Driscoll J, Clare D, Saibil H.

J Cell Biol. 2015 Oct 12;211(1):145-58. doi: 10.1083/jcb.201505104. Epub 2015 Oct 5.


Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.

Wear MP, Kryndushkin D, O'Meally R, Sonnenberg JL, Cole RN, Shewmaker FP.

PLoS One. 2015 Aug 28;10(8):e0136362. doi: 10.1371/journal.pone.0136362. eCollection 2015.


Sup35p in Its Soluble and Prion States Is Packaged inside Extracellular Vesicles.

Kabani M, Melki R.

MBio. 2015 Aug 18;6(4). pii: e01017-15. doi: 10.1128/mBio.01017-15.


The 26S Proteasome Degrades the Soluble but Not the Fibrillar Form of the Yeast Prion Ure2p In Vitro.

Wang K, Redeker V, Madiona K, Melki R, Kabani M.

PLoS One. 2015 Jun 26;10(6):e0131789. doi: 10.1371/journal.pone.0131789. eCollection 2015.


Hsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity.

Sporn ZA, Hines JK.

Prion. 2015;9(2):80-9. doi: 10.1080/19336896.2015.1020268.


Heterologous aggregates promote de novo prion appearance via more than one mechanism.

Arslan F, Hong JY, Kanneganti V, Park SK, Liebman SW.

PLoS Genet. 2015 Jan 8;11(1):e1004814. doi: 10.1371/journal.pgen.1004814. eCollection 2015 Jan.


Proteomic screening for amyloid proteins.

Nizhnikov AA, Alexandrov AI, Ryzhova TA, Mitkevich OV, Dergalev AA, Ter-Avanesyan MD, Galkin AP.

PLoS One. 2014 Dec 30;9(12):e116003. doi: 10.1371/journal.pone.0116003. eCollection 2014.


Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.

Klaips CL, Hochstrasser ML, Langlois CR, Serio TR.

Elife. 2014 Dec 9;3. doi: 10.7554/eLife.04288. Erratum in: Elife. 2015;4:e06494.


Prion propagation can occur in a prokaryote and requires the ClpB chaperone.

Yuan AH, Garrity SJ, Nako E, Hochschild A.

Elife. 2014 Aug 13;3:e02949. doi: 10.7554/eLife.02949.


Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selection.

Harris JM, Nguyen PP, Patel MJ, Sporn ZA, Hines JK.

PLoS Genet. 2014 Jul 24;10(7):e1004510. doi: 10.1371/journal.pgen.1004510. eCollection 2014 Jul.


Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype.

Pezza JA, Villali J, Sindi SS, Serio TR.

Nat Commun. 2014 Jul 15;5:4384. doi: 10.1038/ncomms5384.


Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding.

Holmes WM, Mannakee BK, Gutenkunst RN, Serio TR.

Nat Commun. 2014 Jul 15;5:4383. doi: 10.1038/ncomms5383.


Functional role of Tia1/Pub1 and Sup35 prion domains: directing protein synthesis machinery to the tubulin cytoskeleton.

Li X, Rayman JB, Kandel ER, Derkatch IL.

Mol Cell. 2014 Jul 17;55(2):305-18. doi: 10.1016/j.molcel.2014.05.027. Epub 2014 Jun 26.


Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.

Stein KC, Bengoechea R, Harms MB, Weihl CC, True HL.

J Biol Chem. 2014 Jul 25;289(30):21120-30.


Distinct tau prion strains propagate in cells and mice and define different tauopathies.

Sanders DW, Kaufman SK, DeVos SL, Sharma AM, Mirbaha H, Li A, Barker SJ, Foley AC, Thorpe JR, Serpell LC, Miller TM, Grinberg LT, Seeley WW, Diamond MI.

Neuron. 2014 Jun 18;82(6):1271-88. doi: 10.1016/j.neuron.2014.04.047. Epub 2014 May 22.


Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.

Stein KC, True HL.

PLoS Genet. 2014 May 8;10(5):e1004337. doi: 10.1371/journal.pgen.1004337. eCollection 2014 May.


Defining the limits: Protein aggregation and toxicity in vivo.

Holmes WM, Klaips CL, Serio TR.

Crit Rev Biochem Mol Biol. 2014 Jul-Aug;49(4):294-303. doi: 10.3109/10409238.2014.914151. Epub 2014 Apr 28. Review.


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.


Variant-specific prion interactions: Complicating factors.

Sharma J, Liebman SW.

Cell Logist. 2013 Jan 1;3(1):e25698. Epub 2013 Sep 12.


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.

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