Author

L. R. Kenner

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 1 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

A. A. Anand· 1 shared A. Frost· 1 shared A. G. Myasnikov· 1 shared C. J. Klose· 1 shared C. L. Gilchrist· 1 shared D. Kern· 1 shared D. Mavor· 1 shared D. S. Tawfik· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperBiochemistry

A. A. Anand

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Constitutive protein degradation induces acute cell death via proteolysis products

S.-H. Chen, S. Prakash, E. Helgason, C. L. Gilchrist, L. R. Kenner, R. Srinivasan, T. Sterne-Weiler, M. Hafner, R. Piskol, E. C. Dueber, H. Hamidi, N. Endres, X. Ye, W. J. Fairbrother, I. E. Wertz

This study shows proteasome-generated peptides from degraded proteins induce cell death by neutralizing IAPs, explaining the efficacy of proteolysis-modulating drugs like thalidomide analogs and bortezomib.

bioRxiv · Feb 6, 2023 · PreprintCell Biology

Structural basis of eIF2B-catalyzed GDP exchange and phosphoregulation by the integrated stress response

A. A. Anand, L. R. Kenner, H. C. Nguyen, A. G. Myasnikov, C. J. Klose, L. A. McGeever, J. C. Tsai, L. E. Miller-Vedam, P. Walter, A. Frost

The paper reports cryoEM structures of eIF2 bound to eIF2B, revealing the mechanism of GDP exchange and phosphoregulation in the integrated stress response.

bioRxiv · Dec 22, 2018Biochemistry

Rescue of Conformational Dynamics in Enzyme Catalysis by Directed Evolution

R. Otten, L. Liu, L. R. Kenner, M. W. Clarkson, D. Mavor, D. S. Tawfik, D. Kern, J. S. Fraser

This study uses directed evolution to identify mutations that restore catalytic activity in a mutant enzyme, revealing how conformational dynamics are shaped by evolutionary selection.

bioRxiv · Sep 5, 2017Biophysics