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

Click to filter author papers

Biochemistry· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:human· 3 Approach:biophysical modeling· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:protein structure· 1

Frequent Co-Authors

A. Kropp· 1 shared B. C. Lechenberg· 1 shared B. C. Lechtenberg· 1 shared G. Fischer· 1 shared I. Lucet· 1 shared J. C. McCoy· 1 shared J. Hou· 1 shared J. M. Hardy· 1 shared

Activity by Year

2017-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 14 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

1 shared paperBiochemistry

A. Kropp

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivOct 11, 2022

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

X. S. Wang, T. R. Cotton, S. J. Trevelyan…·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.

DOI 10.1038/s41467-023-35871-z

humanstructural biology

𝕏 PostBluesky

BiochemistrybioRxivPreprintSep 1, 2022

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…·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.

DOI 10.1101/2022.09.01.506260

humanproteomics

𝕏 PostBluesky

BiochemistrybioRxivJul 28, 2017

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

T. R. Cotton, G. Fischer, X. Wang…·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.

DOI 10.15252/embj.201797883

humanprotein structure

𝕏 PostBluesky