Author

J. F. Hancock

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· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Organism:human· 3 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

H. Liang· 3 shared Y. Zhou· 3 shared A. Naji· 2 shared K.-J. Cho· 2 shared A. A. Gorfe· 1 shared A. K. Gupta· 1 shared A. T. Bademosi· 1 shared B. Collins· 1 shared

Activity by Year

2018-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiochemistry

H. Liang

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Author profile →

3 papers

Recent·Most cited

MTMR regulates KRAS function by controlling plasma membrane levels of phospholipids

T. Lange, A. Naji, R. van der Hoeven, H. Liang, Y. Zhou, G. R. Hammond, J. F. Hancock, K.-J. Cho

The paper identifies MTMR proteins as regulators of KRAS function by controlling plasma membrane phospholipid levels, specifically PI4P and PtdSer.

bioRxiv · Jan 22, 2024Cell Biology

Dissecting the nanoscale lipid profile of caveolae

Y. Zhou, N. Ariotti, J. Rae, H. Liang, V. Tillu, S. Tee, M. Bastiani, A. T. Bademosi, B. Collins, F. A. Meunier, J. F. Hancock, R. G. Parton

This study defines the caveolar lipid profile using quantitative lipid mapping and simulations, showing how CAV1 and cavin1 sort distinct lipids and create a unique lipid environment.

bioRxiv · Jan 16, 2020Biochemistry

Discovery of allosteric non-covalent KRAS inhibitors that bind with sub-micromolar affinity and disrupt effector binding

M. J. McCarthy, C. V. Pagba, P. Prakash, A. Naji, D. van der Hoeven, H. Liang, A. K. Gupta, Y. Zhou, K.-J. Cho, J. F. Hancock, A. A. Gorfe

This study identifies a pyrazolopyrimidine-based allosteric KRAS inhibitor with sub-micromolar affinity that disrupts effector binding and inhibits cancer cell growth.

bioRxiv · Oct 11, 2018Biochemistry