Author

Y. Kulathu

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

Biology Disciplines

Click to filter author papers

Biochemistry· 6

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 6 Assay:proteomics· 3 Research Focus:cell type annotation· 2 Research Focus:drug response / drug discovery· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

A. Knebel· 3 shared F. Lamoliatte· 3 shared L. A. Armstrong· 3 shared S. M. Lange· 3 shared S. P. Matthews· 3 shared D. Millrine· 2 shared I. Cole· 2 shared J. J. Peter· 2 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

A. Knebel

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

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

S. M. Lange, M. R. McFarland, F. Lamoliatte, D. Kwasna, L. Shen, I. Wallace, I. Cole, L. A. Armstrong, A. Knebel, C. Johnson, V. De Cesare, 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.

bioRxiv · Jan 10, 2023Biochemistry

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

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, B. Canal, J. F. Diffley, L. S. Drury, M. Howell, Y. Kulathu, K. Labib, C. T. Lim, J. Milligan, N. O'Reilly, E. Ozono, K. W. Tan, R. Ulferts, , J. Zeng

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

bioRxiv · Apr 7, 2021Biochemistry

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

S. A. Abdul Rehman, L. A. Armstrong, S. M. Lange, Y. A. Kristariyanto, T. W. Grawert, A. Knebel, D. Svergun, 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.

bioRxiv · Jan 27, 2021Biochemistry

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