Thomas R. Cotton

Melbourne, VIC, Australia

Last Updated: 09/26/2026

Save publications for later

Sign Up

Not sure about your diagnosis?

Check Your Symptoms

Found 9 publications

A tandem recruitment site in the pseudokinase scaffold PEAK3 is subject to phosphorylation-dependent regulation and cancer-associated mutations.

A tandem recruitment site in the pseudokinase scaffold PEAK3 is subject to phosphorylation-dependent regulation and cancer-associated mutations.

Journal: The Journal of biological chemistry

Published: August 03, 2025

Activation of CAMK2 by pseudokinase PEAK1 represents a targetable pathway in triple negative breast cancer.

Activation of CAMK2 by pseudokinase PEAK1 represents a targetable pathway in triple negative breast cancer.

Journal: Nature communications

Published: March 07, 2024

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

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

Journal: bioRxiv : the preprint server for biology

Published: February 26, 2024

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

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

Journal: Nature communications

Published: September 09, 2022

Structural mapping of PEAK pseudokinase interactions identifies 14-3-3 as a molecular switch for PEAK3 signaling.

Structural mapping of PEAK pseudokinase interactions identifies 14-3-3 as a molecular switch for PEAK3 signaling.

Journal: Nature communications

Published: August 24, 2022

Publisher Correction: Activation mechanism of PINK1.

Publisher Correction: Activation mechanism of PINK1.

Journal: Nature

Published: March 16, 2022

Activation mechanism of PINK1.

Activation mechanism of PINK1.

Journal: Nature

Published: August 22, 2021

Structural basis of K63-ubiquitin chain formation by the Gordon-Holmes syndrome RBR E3 ubiquitin ligase RNF216.

Structural basis of K63-ubiquitin chain formation by the Gordon-Holmes syndrome RBR E3 ubiquitin ligase RNF216.

Journal: Molecular cell

Published: March 27, 2021

Chain reactions: molecular mechanisms of RBR ubiquitin ligases.

Chain reactions: molecular mechanisms of RBR ubiquitin ligases.

Journal: Biochemical Society transactions

Published: May 31, 2020

Showing 1-9 of 9

Last Updated: 09/26/2026