PUBLICATIONS
Nuclear Armageddon
Proteins govern nuclear functions. If they lose their structures, the nucleus can become critical. We are interested in how the cell protects against protein misfolding armageddon...
Fredrickson, E. K., Gallagher, P. S., Clowes Candadai, S. V., and R. G. Gardner. 2013.
Substrate Recognition in Nuclear Protein Quality Control Degradation Is Governed by Exposed Hydrophobicity That Correlates with Aggregation and Insolubility.
The Journal of Biological Chemistry 288:6130-6139.
PDF (2.1M)
Rosenbaum, J. C. and R. G. Gardner. 2011.
How a disordered ubiquitin ligase maintains order in nuclear protein homeostasis.
Nucleus 2:264-270.
Abstract
PDF (2.0M)
Rosenbaum, J. C., Fredrickson, E. K., Oeser, M. L., Garrett-Engele, C. M., Locke, M. N., Richardson, L. A., Nelson, Z. W., Hetrick, E. D., Milac, T. I., Gottschling, D. E., and R. G. Gardner. 2011.
Disorder Targets Misorder in Nuclear Quality Control Degradation: A Disordered Ubiquitin Ligase Directly Recognizes Its Misfolded Substrates.
Molecular Cell 41:93-106.
PDF (3.1M)
Highlighted in a Preview in same issue.
More to come.
A conserved deubiquitinating enzyme uses intrinsic disordered regions to scaffold multiple protein-interaction sites. JBC 290: 20601-20612.
Dynamic sumoylation of a conserved transcription corepressor prevents persistent inclusion formation during hyperosmotic stress. PLoS Genetics 12: e1005809.
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