Keith D. Wilkinson

Affiliations: 
Emory University, Atlanta, GA 
Area:
Biochemistry
Google:
"Keith Wilkinson"
Mean distance: (not calculated yet)
 

Children

Sign in to add trainee
Nathaniel S. Russell grad student 2005 Emory
Francisca E. Reyes Turcu grad student 2008 Emory
Karen H. Ventii grad student 2008 Emory
Janetta A. Bryksin grad student 2011 Emory
BETA: Related publications

Publications

You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect.

Chernova TA, Yang Z, Karpova TS, et al. (2020) Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association. International Journal of Molecular Sciences. 21
Chernova TA, Chernoff YO, Wilkinson KD. (2019) Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery. Molecules (Basel, Switzerland). 24
Chernova TA, Chernoff YO, Wilkinson KD. (2017) Prion-based memory of heat stress in yeast. Prion. 1-11
Chernova TA, Kiktev DA, Romanyuk AV, et al. (2017) Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress. Cell Reports. 18: 751-761
Chernova TA, Wilkinson KD, Chernoff YO. (2016) Prions, Chaperones, and Proteostasis in Yeast. Cold Spring Harbor Perspectives in Biology
Balakirev MY, Mullally JE, Favier A, et al. (2015) Wss1 metalloprotease partners with Cdc48/Doa1 in processing genotoxic SUMO conjugates. Elife. 4
Eletr ZM, Wilkinson KD. (2015) Quantitative analysis of protein-protein interactions. Methods in Molecular Biology (Clifton, N.J.). 1278: 23-37
Ali M, Chernova TA, Newnam GP, et al. (2014) Stress-dependent proteolytic processing of the actin assembly protein Lsb1 modulates a yeast prion. The Journal of Biological Chemistry. 289: 27625-39
Chernova TA, Wilkinson KD, Chernoff YO. (2014) Physiological and environmental control of yeast prions. Fems Microbiology Reviews. 38: 326-44
Eletr ZM, Wilkinson KD. (2014) Regulation of proteolysis by human deubiquitinating enzymes. Biochimica Et Biophysica Acta. 1843: 114-28
See more...