Author

L. Wieteska

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· 1 Cancer Biology· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Approach:biophysical modeling· 1 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1 Assay:protein sequence· 1 Assay:protein structure· 1

Frequent Co-Authors

C.-C. Lin· 3 shared J. E. Ladbury· 3 shared K. M. Suen· 3 shared Z. Ahmed· 3 shared A. Kalverda· 1 shared A. Stainthorp· 1 shared C. Molina-Paris· 1 shared C. Seiler· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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3 shared papersCell Biology

C.-C. Lin

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Author profile →

3 papers

Recent·Most cited

Cell BiologyMolecular CellPeer-reviewedMar 1, 2022

Receptor tyrosine kinases regulate signal transduction through a liquid-liquid phase separated state

C.-C. Lin, K. M. Suen, P.-A. Jeffrey…·J. E. Ladbury

This study shows that RTKs form liquid-liquid phase-separated states with downstream effectors to enhance signaling fidelity.

DOI 10.1016/j.molcel.2022.02.005

experimental assaycell signaling & trafficking

𝕏 PostBluesky

BiochemistrybioRxivPreprintOct 1, 2020

Regulation of kinase activity by combined action of juxtamembrane and C-terminal regions of receptors

C.-C. Lin, L. Wieteska, G. Poncet-Montange…·J. E. Ladbury

The paper investigates how juxtamembrane and C-terminal regions regulate kinase activity in RTKs, identifying key interactions and mutations linked to disease.

DOI 10.1101/2020.10.01.322123

protein structureprotein sequence

𝕏 PostBluesky

Cancer BiologybioRxivNov 29, 2019

Grb2 binding induces phosphorylation-independent activation of Shp2

C.-C. Lin, L. Wieteska, K. M. Suen…·J. E. Ladbury

This study shows Grb2 binding activates Shp2 independently of phosphorylation, and identifies a peptide that blocks this interaction, reducing Shp2 activity and MAPK signaling.

DOI 10.1038/s42003-021-01969-7

proteomicsexperimental assay

𝕏 PostBluesky