Fredrickson, E. K., Clowes Candadai, S. V., Tam, C. H., and R. G. Gardner. 2013.

Means of self-preservation: how an intrinsically disordered ubiquitin-protein ligase averts self-destruction.

Molecular Biology of the Cell 24:1041-1052.

 

 

PUBLICATIONS

Disorder: The Dark Matter of the Protein World

Proteins are typically imagined as having defined 3D structures. But ~30% of proteins are disordered and conformationally flexible. We are interested in how disorder confers protein function.

Reed, B.J., Locke, M.N., and R.G. Gardner. 2015.

A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites.

Journal of Biological Chemistry 290:20601–20612.

 

Abstract

PDF (3.6MB)

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.

Abstract

PDF (3.1M)

Highlighted in a Preview in same issue.

 

More to come.

 

RESEARCH

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.

OUR FUNDING

© 2020  Gardner Lab. All Rights Reserved

Richard Gardner

Department of Pharmacology

Box 357280

University of Washington

Seattle, WA 98195-7280