Author

T. R. Cotton

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 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 4 Approach:biophysical modeling· 2 Research Focus:cancer & tumor microenvironment· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

R. J. Daly· 2 shared X. Ma· 2 shared A. C. Chueh· 1 shared A. Kropp· 1 shared A. M. Ellisdon· 1 shared B. C. Lechenberg· 1 shared B. C. Lechtenberg· 1 shared C. Bayly-Jones· 1 shared

Activity by Year

2017-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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2 shared papersCancer Biology

R. J. Daly

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Feed-forward stimulation of CAMK2 by the oncogenic pseudokinase PEAK1 generates a therapeutically "actionable" signalling axis in triple negative breast cancer

X. Yang, X. Ma, T. Zhao, D. R. Croucher, E. V. Nguyen, K. C. Clark, C. Hu, S. L. Latham, C. Bayly-Jones, V. C. B. Nguyen, S. Budnar, S. Shin, L. K. Nguyen, T. R. Cotton, A. C. Chueh, , R. J. Daly

This study identifies a novel feed-forward signalling axis between PEAK1 and CAMK2 in TNBC, showing that targeting CAMK2 can inhibit PEAK1-driven oncogenic processes.

bioRxiv · Feb 14, 2024Cancer Biology

The unifying catalytic mechanism of the RING-between-RING E3 ligase family

X. S. Wang, T. R. Cotton, S. J. Trevelyan, L. W. Richardson, W. T. Lee, J. Silke, B. C. Lechtenberg

This study defines the core catalytic mechanism of RBR E3 ligases through structural and biochemical analysis of HOIL-1 and RNF216, revealing conserved features and an allosteric mechanism.

bioRxiv · Oct 11, 2022Biochemistry

When two is a crowd - Structural mapping of PEAK pseudokinase interactions identifies 14 3 3 as a molecular switch for PEAK3/Crk signaling.

M. J. Roy, M. G. Surudoi, A. Kropp, J. Hou, W. Dai, J. M. Hardy, L.-Y. Liang, T. R. Cotton, B. C. Lechenberg, T. A. Dite, X. Ma, R. J. Daly, O. Patel, I. Lucet

The paper identifies 14-3-3 as a molecular switch for PEAK3/Crk signaling by mapping PEAK pseudokinase interactions and demonstrating a conserved high affinity 14-3-3 motif.

bioRxiv · Sep 1, 2022 · PreprintBiochemistry

Structure of the human pro-myostatin precursor and determinants of growth factor latency

T. R. Cotton, G. Fischer, X. Wang, J. C. McCoy, M. Czepnik, T. B. Thompson, M. Hyvonen

This study determines the structure of human pro-myostatin and identifies features responsible for its latent state, offering insights into myostatin activation and potential inhibitor design.

bioRxiv · Jul 28, 2017Biochemistry