Sort by
Items per page

Send to

Choose Destination

Search results

Items: 1 to 50 of 83


Full restoration of specific infectivity and strain properties from pure mammalian prion protein.

Burke CM, Walsh DJ, Steele AD, Agrimi U, Di Bari MA, Watts JC, Supattapone S.

PLoS Pathog. 2019 Mar 25;15(3):e1007662. doi: 10.1371/journal.ppat.1007662. eCollection 2019 Mar.


Rescue of Transgenic Alzheimer's Pathophysiology by Polymeric Cellular Prion Protein Antagonists.

Gunther EC, Smith LM, Kostylev MA, Cox TO, Kaufman AC, Lee S, Folta-Stogniew E, Maynard GD, Um JW, Stagi M, Heiss JK, Stoner A, Noble GP, Takahashi H, Haas LT, Schneekloth JS, Merkel J, Teran C, Naderi ZK, Supattapone S, Strittmatter SM.

Cell Rep. 2019 Jan 29;26(5):1368. doi: 10.1016/j.celrep.2019.01.064. No abstract available.


Rescue of Transgenic Alzheimer's Pathophysiology by Polymeric Cellular Prion Protein Antagonists.

Gunther EC, Smith LM, Kostylev MA, Cox TO, Kaufman AC, Lee S, Folta-Stogniew E, Maynard GD, Um JW, Stagi M, Heiss JK, Stoner A, Noble GP, Takahashi H, Haas LT, Schneekloth JS, Merkel J, Teran C, Naderi ZK, Supattapone S, Strittmatter SM.

Cell Rep. 2019 Jan 2;26(1):145-158.e8. doi: 10.1016/j.celrep.2018.12.021. Erratum in: Cell Rep. 2019 Jan 29;26(5):1368.


SEC24A identified as an essential mediator of thapsigargin-induced cell death in a genome-wide CRISPR/Cas9 screen.

Chidawanyika T, Sergison E, Cole M, Mark K, Supattapone S.

Cell Death Discov. 2018 Dec 18;4:115. doi: 10.1038/s41420-018-0135-5. eCollection 2018.


Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species.

Zhao Y, Zurawel AA, Jenkins NP, Duennwald ML, Cheng C, Kettenbach AN, Supattapone S.

Sci Rep. 2018 Jun 22;8(1):9554. doi: 10.1038/s41598-018-27900-5.


CAG Expansions Are Genetically Stable and Form Nontoxic Aggregates in Cells Lacking Endogenous Polyglutamine Proteins.

Zurawel AA, Kabeche R, DiGregorio SE, Deng L, Menon KM, Opalko H, Duennwald ML, Moseley JB, Supattapone S.

MBio. 2016 Sep 27;7(5). pii: e01367-16. doi: 10.1128/mBio.01367-16.


Interallelic Transcriptional Enhancement as an in Vivo Measure of Transvection in Drosophila melanogaster.

Noble GP, Dolph PJ, Supattapone S.

G3 (Bethesda). 2016 Oct 13;6(10):3139-3148. doi: 10.1534/g3.116.032300.


The effect of reducing agents on challenge of rainbow trout with Aeromonas salmonicida.

Supattapone SY, Supattapone S, Cramer RA.

J Fish Dis. 2017 Mar;40(3):437-441. doi: 10.1111/jfd.12511. Epub 2016 Jun 13. No abstract available.


Dissociation of recombinant prion autocatalysis from infectivity.

Noble GP, Supattapone S.

Prion. 2015;9(6):405-11. doi: 10.1080/19336896.2015.1123843.


Expanding the prion disease repertoire.

Supattapone S.

Proc Natl Acad Sci U S A. 2015 Sep 22;112(38):11748-9. doi: 10.1073/pnas.1515143112. Epub 2015 Sep 1. No abstract available.


A Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.

Noble GP, Wang DW, Walsh DJ, Barone JR, Miller MB, Nishina KA, Li S, Supattapone S.

PLoS Pathog. 2015 Jun 30;11(6):e1005017. doi: 10.1371/journal.ppat.1005017. eCollection 2015 Jun.


Requirements for mutant and wild-type prion protein misfolding in vitro.

Noble GP, Walsh DJ, Miller MB, Jackson WS, Supattapone S.

Biochemistry. 2015 Feb 10;54(5):1180-7. doi: 10.1021/bi501495j. Epub 2015 Jan 22.


Synthesis of high titer infectious prions with cofactor molecules.

Supattapone S.

J Biol Chem. 2014 Jul 18;289(29):19850-4. doi: 10.1074/jbc.R113.511329. Epub 2014 May 23. Review.


Elucidating the role of cofactors in mammalian prion propagation.

Supattapone S.

Prion. 2014 Jan-Feb;8(1):100-5. Review.


Prion nucleation site unmasked by transient interaction with phospholipid cofactor.

Zurawel AA, Walsh DJ, Fortier SM, Chidawanyika T, Sengupta S, Zilm K, Supattapone S.

Biochemistry. 2014 Jan 14;53(1):68-76. doi: 10.1021/bi4014825. Epub 2014 Jan 2.


Cofactor molecules induce structural transformation during infectious prion formation.

Miller MB, Wang DW, Wang F, Noble GP, Ma J, Woods VL Jr, Li S, Supattapone S.

Structure. 2013 Nov 5;21(11):2061-8. doi: 10.1016/j.str.2013.08.025. Epub 2013 Oct 10.


Phosphatidylethanolamine as a prion cofactor: potential implications for disease pathogenesis.

Supattapone S.

Prion. 2012 Nov-Dec;6(5):417-9. doi: 10.4161/pri.21826. Epub 2012 Aug 16. Review.


The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc).

Turnbaugh JA, Unterberger U, Saá P, Massignan T, Fluharty BR, Bowman FP, Miller MB, Supattapone S, Biasini E, Harris DA.

J Neurosci. 2012 Jun 27;32(26):8817-30. doi: 10.1523/JNEUROSCI.1103-12.2012.


Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions.

Deleault NR, Walsh DJ, Piro JR, Wang F, Wang X, Ma J, Rees JR, Supattapone S.

Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):E1938-46. doi: 10.1073/pnas.1206999109. Epub 2012 Jun 18.


Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids.

Deleault NR, Piro JR, Walsh DJ, Wang F, Ma J, Geoghegan JC, Supattapone S.

Proc Natl Acad Sci U S A. 2012 May 29;109(22):8546-51. doi: 10.1073/pnas.1204498109. Epub 2012 May 14.


Non-reducing alkaline solubilization and rapid on-column refolding of recombinant prion protein.

Walsh DJ, Noble GP, Piro JR, Supattapone S.

Prep Biochem Biotechnol. 2012;42(1):77-86. doi: 10.1080/10826068.2011.564256.


Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.

Miller MB, Geoghegan JC, Supattapone S.

PLoS Pathog. 2011 Jul;7(7):e1002128. doi: 10.1371/journal.ppat.1002128. Epub 2011 Jul 14.


Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

Piro JR, Wang F, Walsh DJ, Rees JR, Ma J, Supattapone S.

Biochemistry. 2011 Aug 23;50(33):7111-6. doi: 10.1021/bi200786p. Epub 2011 Jul 21.


Photodegradation illuminates the role of polyanions in prion infectivity.

Piro JR, Supattapone S.

Prion. 2011 Apr-Jun;5(2):49-51. Epub 2011 Apr 1. Review.


In situ photodegradation of incorporated polyanion does not alter prion infectivity.

Piro JR, Harris BT, Supattapone S.

PLoS Pathog. 2011 Feb 3;7(2):e1002001. doi: 10.1371/journal.ppat.1002001.


Superparamagnetic nanoparticle capture of prions for amplification.

Miller MB, Supattapone S.

J Virol. 2011 Mar;85(6):2813-7. doi: 10.1128/JVI.02451-10. Epub 2011 Jan 12.


Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro.

Deleault NR, Kascsak R, Geoghegan JC, Supattapone S.

Biochemistry. 2010 May 11;49(18):3928-34. doi: 10.1021/bi100370b.


Biochemistry. What makes a prion infectious?

Supattapone S.

Science. 2010 Feb 26;327(5969):1091-2. doi: 10.1126/science.1187790. No abstract available.


Complex polyamines: unique prion disaggregating compounds.

Supattapone S, Piro JR, Rees JR.

CNS Neurol Disord Drug Targets. 2009 Nov;8(5):323-8. Review.


Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor.

Geoghegan JC, Miller MB, Kwak AH, Harris BT, Supattapone S.

PLoS Pathog. 2009 Jul;5(7):e1000535. doi: 10.1371/journal.ppat.1000535. Epub 2009 Jul 31.


Prion protein glycosylation is not required for strain-specific neurotropism.

Piro JR, Harris BT, Nishina K, Soto C, Morales R, Rees JR, Supattapone S.

J Virol. 2009 Jun;83(11):5321-8. doi: 10.1128/JVI.02502-08. Epub 2009 Mar 18.


The effects of prion protein proteolysis and disaggregation on the strain properties of hamster scrapie.

Deleault AM, Deleault NR, Harris BT, Rees JR, Supattapone S.

J Gen Virol. 2008 Oct;89(Pt 10):2642-50. doi: 10.1099/vir.0.2008/002303-0.


Amplification of purified prions in vitro.

Supattapone S, Deleault NR, Rees JR.

Methods Mol Biol. 2008;459:117-30. doi: 10.1007/978-1-59745-234-2_9.


Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs.

Tribouillard-Tanvier D, Dos Reis S, Gug F, Voisset C, Béringue V, Sabate R, Kikovska E, Talarek N, Bach S, Huang C, Desban N, Saupe SJ, Supattapone S, Thuret JY, Chédin S, Vilette D, Galons H, Sanyal S, Blondel M.

PLoS One. 2008 May 14;3(5):e2174. doi: 10.1371/journal.pone.0002174.


Selective incorporation of polyanionic molecules into hamster prions.

Geoghegan JC, Valdes PA, Orem NR, Deleault NR, Williamson RA, Harris BT, Supattapone S.

J Biol Chem. 2007 Dec 14;282(50):36341-53. Epub 2007 Oct 16.


Efficient in vitro amplification of chronic wasting disease PrPRES.

Kurt TD, Perrott MR, Wilusz CJ, Wilusz J, Supattapone S, Telling GC, Zabel MD, Hoover EA.

J Virol. 2007 Sep;81(17):9605-8. Epub 2007 Jun 6.


Formation of native prions from minimal components in vitro.

Deleault NR, Harris BT, Rees JR, Supattapone S.

Proc Natl Acad Sci U S A. 2007 Jun 5;104(23):9741-6. Epub 2007 May 29. Erratum in: Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12636.


Immunodetection of glycophosphatidylinositol-anchored proteins following treatment with phospholipase C.

Nishina KA, Supattapone S.

Anal Biochem. 2007 Apr 15;363(2):318-20. Epub 2007 Jan 26. No abstract available.


Accelerated accumulation of misfolded prion protein and spongiform degeneration in a Drosophila model of Gerstmann-Sträussler-Scheinker syndrome.

Gavin BA, Dolph MJ, Deleault NR, Geoghegan JC, Khurana V, Feany MB, Dolph PJ, Supattapone S.

J Neurosci. 2006 Nov 29;26(48):12408-14.


The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro.

Nishina KA, Deleault NR, Mahal SP, Baskakov I, Luhrs T, Riek R, Supattapone S.

Biochemistry. 2006 Nov 28;45(47):14129-39.


Which criteria best support the diagnosis of VV1 sporadic Creutzfeldt-Jakob disease?

Supattapone S, Rees JR.

Nat Clin Pract Neurol. 2006 Jun;2(6):296-7. No abstract available.


What makes a good prion? Conference on Prion Biology.

Saupe SJ, Supattapone S.

EMBO Rep. 2006 Mar;7(3):254-8. Epub 2006 Feb 17. No abstract available.


On the horizon: a blood test for prions.

Supattapone S, Geoghegan JC, Rees JR.

Trends Microbiol. 2006 Apr;14(4):149-51. Epub 2006 Feb 17.


Copper (II) ions potently inhibit purified PrPres amplification.

Orem NR, Geoghegan JC, Deleault NR, Kascsak R, Supattapone S.

J Neurochem. 2006 Mar;96(5):1409-15. Epub 2006 Jan 17.


Inactivation of prions by acidic sodium dodecyl sulfate.

Peretz D, Supattapone S, Giles K, Vergara J, Freyman Y, Lessard P, Safar JG, Glidden DV, McCulloch C, Nguyen HO, Scott M, Dearmond SJ, Prusiner SB.

J Virol. 2006 Jan;80(1):322-31.


Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions.

Deleault NR, Geoghegan JC, Nishina K, Kascsak R, Williamson RA, Supattapone S.

J Biol Chem. 2005 Jul 22;280(29):26873-9. Epub 2005 May 24.


Ionic strength and transition metals control PrPSc protease resistance and conversion-inducing activity.

Nishina K, Jenks S, Supattapone S.

J Biol Chem. 2004 Sep 24;279(39):40788-94. Epub 2004 Jul 19.


Prion protein conversion in vitro.

Supattapone S.

J Mol Med (Berl). 2004 Jun;82(6):348-56. Epub 2004 Mar 10. Review.


In vitro prion protein conversion in detergent-solubilized membranes.

Nishina K, Deleault NR, Lucassen RW, Supattapone S.

Biochemistry. 2004 Mar 9;43(9):2613-21.


RNA molecules stimulate prion protein conversion.

Deleault NR, Lucassen RW, Supattapone S.

Nature. 2003 Oct 16;425(6959):717-20.


Supplemental Content

Loading ...
Support Center