Author

M. Gimenez-Andres

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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Cell Biology· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:cell type annotation· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:development & morphogenesis· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. Copic· 2 shared B. Antonny· 2 shared B. M. Collins· 2 shared B. Simonetti· 2 shared K.-E. Chen· 2 shared P. J. Cullen· 2 shared Q. Guo· 2 shared S. Antoine-Bally· 2 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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2 shared papersCell Biology

A. Copic

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Author profile →

4 papers

Recent·Most cited

Structural basis for coupling of the WASH subunit FAM21 with the endosomal SNX27-Retromer complex

Q. Guo, K.-E. Chen, M. Gimenez-Andres, A. Jellett, Y. Gao, B. Simonetti, M. Liu, C. Danson, K. J. Heesom, P. J. Cullen, B. M. Collins

This study defines how FAM21 couples SNX27-Retromer to the WASH complex through motif-based interactions essential for endosomal recycling.

bioRxiv · Aug 15, 2023Cell Biology

Mechanistic basis for SNX27-Retromer coupling to ESCPE-1 in promoting endosomal cargo recycling.

B. Simonetti, Q. Guo, M. Gimenez-Andres, K.-E. Chen, E. R. R. Moody, A. J. Evans, C. M. Danson, T. A. Williams, B. M. Collins, P. J. Cullen

This study identifies the molecular mechanism by which SNX27-Retromer interacts with ESCPE-1 to facilitate endosomal cargo recycling, revealing a conserved surface interaction and evolutionary pathway.

bioRxiv · Aug 28, 2021 · PreprintCell Biology

Exceptional stability of a perilipin on lipid droplets depends on its polar residues, suggesting multimeric assembly

M. Gimenez-Andres, T. Emersic, S. Antoine-Bally, B. Antonny, J. Derganc, A. Copic

This study shows that Plin4's amphipathic helix forms a stable layer on lipid droplets due to polar residues, unlike other perilipins.

bioRxiv · Jul 30, 2020Cell Biology

A giant amphipathic helix from a perilipin that is adapted for coating lipid droplets

A. Copic, S. Antoine-Bally, M. Gimenez-Andres, C. La Torre Garay, B. Antonny, M. M. Manni, S. Pagnotta, J. GUIHOT, C. L. Jackson

This study investigates how the amphipathic helix in Plin4 targets lipid droplets and shows its role in coating them by interacting with triglycerides.

bioRxiv · Mar 5, 2018Cell Biology