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Direct observation of multiple misfolding pathways in a single prion protein molecule.

Yu H, Liu X, Neupane K, Gupta AN, Brigley AM, Solanki A, Sosova I, Woodside MT.

Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):5283-8. doi: 10.1073/pnas.1107736109. Epub 2012 Mar 15.


Single-molecule approaches to prion protein misfolding.

Yu H, Dee DR, Woodside MT.

Prion. 2013 Mar-Apr;7(2):140-6. doi: 10.4161/pri.23303. Epub 2013 Jan 28.


Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape.

Yu H, Dee DR, Liu X, Brigley AM, Sosova I, Woodside MT.

Proc Natl Acad Sci U S A. 2015 Jul 7;112(27):8308-13. doi: 10.1073/pnas.1419197112. Epub 2015 Jun 24.


Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins.

Silva JL, Vieira TC, Gomes MP, Bom AP, Lima LM, Freitas MS, Ishimaru D, Cordeiro Y, Foguel D.

Acc Chem Res. 2010 Feb 16;43(2):271-9. doi: 10.1021/ar900179t. Review.


Expansion of the octarepeat domain alters the misfolding pathway but not the folding pathway of the prion protein.

Leliveld SR, Stitz L, Korth C.

Biochemistry. 2008 Jun 10;47(23):6267-78. doi: 10.1021/bi800253c. Epub 2008 May 13.


Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion.

Elmallah MI, Borgmeyer U, Betzel C, Redecke L.

Prion. 2013 Sep-Oct;7(5):404-11. doi: 10.4161/pri.26745. Epub 2013 Oct 9.


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.


Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1.

Heidarsson PO, Naqvi MM, Otazo MR, Mossa A, Kragelund BB, Cecconi C.

Proc Natl Acad Sci U S A. 2014 Sep 9;111(36):13069-74. doi: 10.1073/pnas.1401065111. Epub 2014 Aug 25.


The Volumetric Diversity of Misfolded Prion Protein Oligomers Revealed by Pressure Dissociation.

Torrent J, Lange R, Rezaei H.

J Biol Chem. 2015 Aug 14;290(33):20417-26. doi: 10.1074/jbc.M115.661710. Epub 2015 Jun 30.


Introducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitro.

Kyle LM, John TR, Schätzl HM, Lewis RV.

PLoS One. 2013 Jun 25;8(6):e66715. doi: 10.1371/journal.pone.0066715. Print 2013.


Infrared microspectroscopy detects protein misfolding cyclic amplification (PMCA)-induced conformational alterations in hamster scrapie progeny seeds.

Daus ML, Wagenführ K, Thomzig A, Boerner S, Hermann P, Hermelink A, Beekes M, Lasch P.

J Biol Chem. 2013 Dec 6;288(49):35068-80. doi: 10.1074/jbc.M113.497131. Epub 2013 Oct 25.


Misfolding of luciferase at the single-molecule level.

Mashaghi A, Mashaghi S, Tans SJ.

Angew Chem Int Ed Engl. 2014 Sep 22;53(39):10390-3. doi: 10.1002/anie.201405566. Epub 2014 Aug 14.


Interaction between misfolded PrP and the ubiquitin-proteasome system in prion-mediated neurodegeneration.

Lin Z, Zhao D, Yang L.

Acta Biochim Biophys Sin (Shanghai). 2013 Jun;45(6):477-84. doi: 10.1093/abbs/gmt020. Epub 2013 Feb 28. Review.


Misfolding of the prion protein: linking biophysical and biological approaches.

Noinville S, Chich JF, Rezaei H.

Vet Res. 2008 Jul-Aug;39(4):48. doi: 10.1051/vetres:2008025. Epub 2008 Jun 5. Review.


De novo generation of infectious prions in vitro produces a new disease phenotype.

Barria MA, Mukherjee A, Gonzalez-Romero D, Morales R, Soto C.

PLoS Pathog. 2009 May;5(5):e1000421. doi: 10.1371/journal.ppat.1000421. Epub 2009 May 15. Erratum in: PLoS Pathog. 2013 Mar;9(3). doi:10.1371/annotation/4b55946a-edb5-4feb-aeb5-2ee160394d17.


Comparing the energy landscapes for native folding and aggregation of PrP.

Dee DR, Woodside MT.

Prion. 2016 May 3;10(3):207-20. doi: 10.1080/19336896.2016.1173297.


Y145Stop is sufficient to induce de novo generation prions using protein misfolding cyclic amplification.

Abdallah A, Wang P, Richt JA, Sreevatsan S.

Prion. 2012 Jan-Mar;6(1):81-8. doi: 10.4161/pri.6.1.18493.


Misfolding dynamics of human prion protein.

Zaman MH.

Mol Cell Biomech. 2005 Dec;2(4):179-90.


Generation of genuine prion infectivity by serial PMCA.

Weber P, Giese A, Piening N, Mitteregger G, Thomzig A, Beekes M, Kretzschmar HA.

Vet Microbiol. 2007 Aug 31;123(4):346-57. Epub 2007 Apr 7.


Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein.

Gupta AN, Neupane K, Rezajooei N, Cortez LM, Sim VL, Woodside MT.

Nat Commun. 2016 Jun 27;7:12058. doi: 10.1038/ncomms12058.

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