Author

S. P. Matthews

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 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Research Focus:development & morphogenesis· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Organism:mouse· 1

Frequent Co-Authors

Y. Kulathu· 3 shared D. Millrine· 2 shared F. Lamoliatte· 2 shared J. J. Peter· 2 shared A. Hope· 1 shared A. I. I. Lamond· 1 shared A. J. Brenes· 1 shared A. J. M. Howden· 1 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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3 shared papersBiochemistry

Y. Kulathu

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The Immunological Proteome Resource

A. J. Brenes, J. L. Hukelmann, L. Spinelli, A. J. M. Howden, J. M. Marchingo, L. V. Sinclair, C. Rollings, O. J. James, I. R. Phair, S. P. Matthews, S. H. Ross, S. C. Arthur, M. Swamy, D. K. Finlay, A. I. I. Lamond, D. A. Cantrell

The paper introduces ImmPRes, a proteomic resource integrating mass-spectrometry data from murine hematopoietic cells to study immune activation and signaling.

bioRxiv · Aug 29, 2022Immunology

Human UFSP1 is an active protease that regulates UFM1 maturation and UFMylation

D. Millrine, T. Cummings, S. P. Matthews, J. J. Peter, H. Magnussen, T. Macartney, F. Lamoliatte, A. Knebel, Y. Kulathu

The paper identifies UFSP1 as an active protease that matures UFM1 and regulates UFMylation, distinguishing it from UFSP2 in substrate specificity and function.

bioRxiv · Feb 28, 2022Biochemistry

Non canonical scaffold-type ligase complex mediates protein UFMylation

J. J. Peter, H. M. Magnussen, P. A. DaRosa, D. Millrine, S. P. Matthews, F. Lamoliatte, R. Sundaramoorthy, R. R. Kopito, Y. Kulathu

The paper identifies the minimal requirements for protein UFMylation and reveals the regulatory mechanism of an atypical scaffold-type E3 ligase complex.

bioRxiv · Jan 31, 2022 · PreprintBiochemistry

Characterization of protease activity of Nsp3 from SARS-CoV-2 and its in vitro inhibition by nanobodies

L. Armstrong, S. M. Lange, V. de Cesare, S. P. Matthews, R. S. Nirujogi, I. Cole, A. Hope, F. Cunningham, R. Toth, R. Mukherjee, D. Bojkova, F. Gruber, D. Gray, P. G. Wyatt, J. Cinatl, , Y. Kulathu

This study characterizes Nsp3 protease activity from SARS-CoV-2 and identifies nanobodies that inhibit PLpro with nanomolar affinity.

bioRxiv · Dec 9, 2020Biochemistry