Author

S. M. Lange

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 Assay:proteomics· 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

Frequent Co-Authors

Y. Kulathu· 3 shared A. Knebel· 2 shared I. Cole· 2 shared L. A. Armstrong· 2 shared V. De Cesare· 2 shared A. Hope· 1 shared C. Johnson· 1 shared D. Bojkova· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiochemistry

Y. Kulathu

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Author profile →

3 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

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