Author

I. Cole

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· 2 Plant Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:imaging· 1

Frequent Co-Authors

S. M. Lange· 2 shared V. De Cesare· 2 shared Y. Kulathu· 2 shared A. Hope· 1 shared A. Knebel· 1 shared C. Brownlee· 1 shared C. Johnson· 1 shared D. Bojkova· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 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

2 shared papersBiochemistry

S. M. Lange

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Diatoms exhibit dynamic chloroplast calcium signals in response to high light and oxidative stress

s. flori, J. Dickenson, T. Gaikwad, I. Cole, N. Smirnoff, K. E. Helliwell, C. Brownlee, G. L. Wheeler

This study identifies dynamic chloroplast calcium signals in diatoms under high light and oxidative stress, showing distinct responses from cytosolic calcium.

bioRxiv · Aug 15, 2023Plant Biology

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

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