Kenneth W. Drombosky

发表

Huntington’s Disease Studies at the Interface of Chemistry, Physics, and Biology

Kenneth W. Drombosky, 2016 .

β-hairpin-mediated nucleation of polyglutamine amyloid formation.

K. Kar, R. Wetzel, W. S. Horne, 2013, Journal of molecular biology.

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

R. Wetzel, Kenneth W. Drombosky, J. T. Greenamyre, 2016, PloS one.

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

R. Wetzel, M. Palladino, Kenneth W. Drombosky, 2018, Neurobiology of Disease.

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

R. Wetzel, Kenneth W. Drombosky, B. Sahoo, 2016, Methods in molecular biology.

Phosphorylation of Ezrin-Radixin-Moesin-binding Phosphoprotein 50 (EBP50) by Akt Promotes Stability and Mitogenic Function of S-phase Kinase-associated Protein-2 (Skp2)*

P. A. Friedman, Bin Wang, G. Song, 2014, The Journal of Biological Chemistry.

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

L. Joachimiak, M. Lin, M. Diamond, 2019, Nature Communications.

Native tau structure is disrupted by disease-associated mutations that promote aggregation

Milo M. Lin, L. Joachimiak, M. Lin, 2018, bioRxiv.

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

Milo M. Lin, L. Joachimiak, M. Lin, 2019, Nature Communications.

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

K. Kar, R. Wetzel, Kenneth W. Drombosky, 2014, Journal of molecular biology.

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

R. Wetzel, M. Palladino, Kenneth W. Drombosky, 2018, Neurobiology of Disease.