Author

E. Rennella

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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Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:biophysical modeling· 2 Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:structural biology· 1

Frequent Co-Authors

L. E. Kay· 2 shared A. K. Mittermaier· 1 shared A. L. Goldberg· 1 shared C. R. Knoverek· 1 shared G. R. Bowman· 1 shared J. B. Juravsky· 1 shared J. L. Rubinstein· 1 shared S. Raavicharla· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersBiophysics

L. E. Kay

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2 papers

Recent·Most cited

Opening of a Cryptic Pocket in β-lactamase Increases Penicillinase Activity

C. R. Knoverek, U. L. Mallimadugula, S. Singh, E. Rennella, T. E. Frederick, T. Yuwen, S. Raavicharla, L. E. Kay, G. R. Bowman

The paper investigates how a cryptic pocket in β-lactamase, formed under the Ω-loop, enhances enzyme activity against penicillin, suggesting excited states can improve function.

bioRxiv · Apr 14, 2021Biophysics

An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR

S. Vahidi, Z. A. Ripstein, J. B. Juravsky, E. Rennella, A. L. Goldberg, A. K. Mittermaier, J. L. Rubinstein, L. E. Kay

This paper identifies an allosteric switch in Mycobacterium tuberculosis ClpP1P2 protease that regulates its activity through conformational changes, revealed by cryo-EM and methyl-TROSY NMR.

Proceedings of the National Academy of Sciences · Mar 2, 2020Peer-reviewedBiophysics