Author

F. Gabriel

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Assay:metabolomics· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

K. E. J. Jungnickel· 2 shared A. Ejima· 1 shared A. Fuhrmann· 1 shared A. R. Mehdipour· 1 shared B. Gasnier· 1 shared C. Debacker· 1 shared C. Loew· 1 shared C. Low· 1 shared

Activity by Year

2024-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersBiochemistry

K. E. J. Jungnickel

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2 papers

Recent·Most cited

MFSD1 in complex with its accessory subunit GLMP functions as a general dipeptide uniporter in lysosomes

K. E. J. Jungnickel, O. Guelle, M. Iguchi, W. Dong, V. Kotov, F. Gabriel, C. Debacker, J. Dairou, I. McCort-Tranchepain, N. N. Laqtom, S. H. Chan, A. Ejima, K. Sato, D. Massa Lopez, P. Saftig, , M. Damme

The paper identifies MFSD1 as a lysosomal dipeptide uniporter that facilitates the transport of cationic and neutral dipeptides when amino acid exporters are overloaded.

Nature Cell Biology · Jun 5, 2024Peer-reviewedBiochemistry

Structural basis of substrate transport and drug recognition by the human thiamine transporter SLC19A3

F. Gabriel, L. Spriestersbach, A. Fuhrmann, K. E. J. Jungnickel, S. Mostafavi, E. Pardon, J. Steyaert, C. Loew

This study determines the cryo-EM structures of the human thiamine transporter SLC19A3 in complex with ligands, revealing its transport mechanism and drug interactions.

bioRxiv · Mar 11, 2024 · PreprintBiochemistry