Author

Enrico Rennella

University of TorontoORCID 0000-0002-2941-7155Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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

Frequent Co-Authors

Lewis E. KayiD· 2 shared Siavash VahidiiD· 2 shared Adwaith B. UdayiD· 1 shared Alex KangiD· 1 shared Algirdas VėlyvisiD· 1 shared Anisha HarisiD· 1 shared Asim K. BeraiD· 1 shared Bradley T. V. DavisiD· 1 shared

Activity by Year

2024-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersBiochemistry

Lewis E. KayORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Assembly and substrate engagement mechanism of the bacterial proteasome activator Boa

Bradley T. V. Davis, Enrico Rennella, Anisha Haris, Jakub Ujma, David Bruton, Keith Richardson, Kevin Giles, Lewis E. Kay, Siavash Vahidi

This study defines the temperature-sensitive oligomerization mechanism of Bpa and elucidates its interaction with a surrogate substrate using biophysical techniques.

bioRxiv · Oct 1, 2025 · PreprintBiochemistry

Structural basis for allosteric regulation of the proteasome core particle

Madison Turner, Adwaith B. Uday, Algirdas Vėlyvis, Enrico Rennella, Natalie Zeytuni, Siavash Vahidi

The paper presents the first high-resolution structure of Mycobacterium tuberculosis 20S core particle in an inactive state, revealing the structural basis for allosteric regulation.

Nature Communications · Apr 1, 2025Peer-reviewedBiochemistry

Design of amyloidogenic peptide traps

Danny D. Sahtoe, Ewa A. Andrzejewska, Hannah L. Han, Enrico Rennella, Matthias M. Schneider, Georg Meisl, Maggie Ahlrichs, Justin A. Decarreau, Hannah Nguyen, Alex Kang, Paul M. Levine, Mila Lamb, Xinting Li, Asim K. Bera, Lewis E. Kay, , David A. Baker

The paper designs peptide traps that bind amyloidogenic segments in {beta}-strand and {beta}-hairpin conformations, effectively blocking fibril assembly for A{beta}42.

Nature Chemical Biology · Mar 19, 2024Peer-reviewedSynthetic Biology