Yaohui Chai

Analysis of the Role of Heat Shock Protein (Hsp) Molecular Chaperones in Polyglutamine Disease

H. Paulson, N. Bonini, Y. Chai, 1999, The Journal of Neuroscience.

Poly-ubiquitin Binding by the Polyglutamine Disease Protein Ataxin-3 Links Its Normal Function to Protein Surveillance Pathways*

H. Paulson, Y. Chai, R. Cohen, 2004, Journal of Biological Chemistry.

CREB-binding protein sequestration by expanded polyglutamine.

K. Fischbeck, H. Paulson, G. Sobue, 2000, Human molecular genetics.

Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70

H. Paulson, N. Bonini, Y. Chai, 1999, Nature Genetics.

Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro.

H. Paulson, Y. Chai, Y Chai, 1999, Human molecular genetics.

Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis

H. Paulson, Y. Chai, J. Shao, 2002, Proceedings of the National Academy of Sciences of the United States of America.

The Role of Protein Composition in Specifying Nuclear Inclusion Formation in Polyglutamine Disease*

H. Paulson, J. Griffin, Y. Chai, 2001, The Journal of Biological Chemistry.

Defining the Role of Ubiquitin-interacting Motifs in the Polyglutamine Disease Protein, Ataxin-3*

H. Paulson, Y. Chai, Ginger L Marrs, 2005, Journal of Biological Chemistry.