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Items: 7

1.

Tau local structure shields an amyloid-forming motif and controls aggregation propensity.

Chen D, Drombosky KW, Hou Z, Sari L, Kashmer OM, Ryder BD, Perez VA, Woodard DR, Lin MM, Diamond MI, Joachimiak LA.

Nat Commun. 2019 Jun 7;10(1):2493. doi: 10.1038/s41467-019-10355-1.

2.

Mutational analysis implicates the amyloid fibril as the toxic entity in Huntington's disease.

Drombosky KW, Rode S, Kodali R, Jacob TC, Palladino MJ, Wetzel R.

Neurobiol Dis. 2018 Dec;120:126-138. doi: 10.1016/j.nbd.2018.08.019. Epub 2018 Aug 30.

PMID:
30171891
3.

Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer.

Sahoo B, Arduini I, Drombosky KW, Kodali R, Sanders LH, Greenamyre JT, Wetzel R.

PLoS One. 2016 Jun 6;11(6):e0155747. doi: 10.1371/journal.pone.0155747. eCollection 2016.

4.

Fluorescence Correlation Spectroscopy: A Tool to Study Protein Oligomerization and Aggregation In Vitro and In Vivo.

Sahoo B, Drombosky KW, Wetzel R.

Methods Mol Biol. 2016;1345:67-87. doi: 10.1007/978-1-4939-2978-8_5.

PMID:
26453206
5.

Phosphorylation of ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50) by Akt promotes stability and mitogenic function of S-phase kinase-associated protein-2 (Skp2).

Song GJ, Leslie KL, Barrick S, Mamonova T, Fitzpatrick JM, Drombosky KW, Peyser N, Wang B, Pellegrini M, Bauer PM, Friedman PA, Mierke DF, Bisello A.

J Biol Chem. 2015 Jan 30;290(5):2879-87. doi: 10.1074/jbc.M114.609768. Epub 2014 Dec 9.

6.

D-polyglutamine amyloid recruits L-polyglutamine monomers and kills cells.

Kar K, Arduini I, Drombosky KW, van der Wel PC, Wetzel R.

J Mol Biol. 2014 Feb 20;426(4):816-29. doi: 10.1016/j.jmb.2013.11.019. Epub 2013 Nov 28.

7.

β-hairpin-mediated nucleation of polyglutamine amyloid formation.

Kar K, Hoop CL, Drombosky KW, Baker MA, Kodali R, Arduini I, van der Wel PC, Horne WS, Wetzel R.

J Mol Biol. 2013 Apr 12;425(7):1183-97. doi: 10.1016/j.jmb.2013.01.016. Epub 2013 Jan 23.

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