Author

Lorraine Glennie

University of DundeeORCID 0000-0002-5097-4570Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

Brune Le Chatelier· 2 shared Gopal P. SapkotaiD· 2 shared Thomas MacartneyiD· 2 shared Christina M. WooiD· 1 shared Diane Lee Zhi Xuan· 1 shared Freya Goff· 1 shared Gajanan Sathe· 1 shared Geoffrey J. BartoniD· 1 shared

Activity by Year

2026-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersCell Biology

Brune Le Chatelier

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

The contribution of native protein complexes to targeted protein degradation

Lorraine Glennie, Nicole Curnutt, Gajanan Sathe, Brune Le Chatelier, Freya Goff, Jin-Feng Zhao, Tyrell N. Cartwright, Karen J. Dunbar, Nicola T. Wood, Thomas Macartney, Christina M. Woo, Gopal P. Sapkota

This study shows that molecular glue degraders targeting CK1 can co-degrade multiple SACK1 proteins, highlighting the role of protein complex context in targeted protein degradation.

ACS Chemical Biology · Apr 9, 2026Peer-reviewedCell Biology

Mutations within the predicted fragment-binding region of FAM83G/SACK1G abolish its interaction with the Ser/Thr kinase CK1α

Javier S. Utgés, Diane Lee Zhi Xuan, Brune Le Chatelier, Lorraine Glennie, Thomas Macartney, Nicola Wood, Geoffrey J. Barton, Gopal P. Sapkota

The paper identifies mutations in SACK1G that disrupt its interaction with CK1α, using computational modeling and experimental validation.

Open Biology · Jan 7, 2026Peer-reviewedCell Biology