Leah A. Randles, Ph.D.
Affiliations: | 2012 | Biochemistry, Molecular Bio, and Biophysics | University of Minnesota, Twin Cities, Minneapolis, MN |
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Biochemistry, Molecular BiologyGoogle:
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Parents
Sign in to add mentor| Kylie J. Walters | grad student | 2012 | UMN | |
| (Defining How the 26S Proteasome Recognizes Ubiquitinated Substrates.) | ||||
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| Lu X, Nowicka U, Sridharan V, et al. (2017) Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets. Nature Communications. 8: 15540 |
| Chen X, Randles L, Shi K, et al. (2016) Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome. Structure (London, England : 1993) |
| Randles L, Anchoori RK, Roden RB, et al. (2016) Proteasome Ubiquitin Receptor hRpn13 and its Interacting Deubiquitinating Enzyme Uch37 are Required for Proper Cell Cycle Progression. The Journal of Biological Chemistry |
| Nowicka U, Hoffman M, Randles L, et al. (2015) Mycobacterium tuberculosis copper-regulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayer. Proteins |
| Hennig J, de Vries SJ, Hennig KD, et al. (2012) MTMDAT-HADDOCK: high-throughput, protein complex structure modeling based on limited proteolysis and mass spectrometry. Bmc Structural Biology. 12: 29 |
| Randles L, Walters KJ. (2012) Ubiquitin and its binding domains. Frontiers in Bioscience (Landmark Edition). 17: 2140-57 |
| Zhang N, Wang Q, Ehlinger A, et al. (2009) Structure of the s5a:k48-linked diubiquitin complex and its interactions with rpn13. Molecular Cell. 35: 280-90 |
| Schreiner P, Chen X, Husnjak K, et al. (2008) Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature. 453: 548-52 |
| Husnjak K, Elsasser S, Zhang N, et al. (2008) Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature. 453: 481-8 |