Author

L. A. Armstrong

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Assay:proteomics· 1

Frequent Co-Authors

Y. Kulathu· 3 shared A. Knebel· 2 shared S. M. Lange· 2 shared B. Canal· 1 shared C. Johnson· 1 shared C. T. Lim· 1 shared D. Kwasna· 1 shared D. Svergun· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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3 shared papersBiochemistry

Y. Kulathu

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivJan 10, 2023

Comprehensive approach to study branched ubiquitinchains reveals roles for K48-K63 branches inVCP/p97-related processes

S. M. Lange, M. R. McFarland, F. Lamoliatte…·Y. Kulathu

This paper develops a pipeline to study branched ubiquitin chains, identifies debranching enzymes, and reveals their roles in VCP/p97 processes and DNA damage responses.

DOI 10.1038/s41594-024-01354-y

humanproteomics

𝕏 PostBluesky

BiochemistrybioRxivApr 7, 2021

Identifying SARS-CoV-2 Antiviral Compounds by Screening for Small Molecule Inhibitors of Nsp3 Papain-like Protease

L. A. Armstrong, R. Beale, G. Bineva-Todd…·J. Zeng

This study identifies two small molecule inhibitors of SARS-CoV-2 Nsp3 PLpro that inhibit viral replication in cell culture.

DOI 10.1042/bcj20210244

experimental assaydrug response / drug discovery

𝕏 PostBluesky

BiochemistrybioRxivJan 27, 2021

Mechanism of activation and regulation of Deubiquitinase activity in MINDY1 and MINDY2

S. A. Abdul Rehman, L. A. Armstrong, S. M. Lange…·Y. Kulathu

This paper reveals the mechanism of MINDY1 and MINDY2 deubiquitinase activity, showing how substrate interaction relieves autoinhibition and enables cleavage of K48-linked ubiquitin chains.

DOI 10.1016/j.molcel.2021.08.024

structural biologyexperimental assay

𝕏 PostBluesky