Author

Katharina E. J. Jungnickel

European Molecular Biology LaboratoryORCID 0000-0002-2850-5911Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Assay:cryo-EM· 1 Organism:E. coli· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

Christian LoewiD· 3 shared Florian GabrieliD· 2 shared Ahmad Reza MehdipouriD· 1 shared Akika Ejima· 1 shared Antonia Fuhrmann· 1 shared Bruno GasnieriD· 1 shared Cécile DebackeriD· 1 shared David Massa LópeziD· 1 shared

Activity by Year

2024-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiochemistry

Christian LoewORCID

Mutual co-authors in cluster

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3 papers

Recent·Most cited

BiochemistrybioRxivPreprintMay 22, 2026

Structural basis of substrate recognition and transport in bacterial ACS transporters

Kim Bartels, Katharina E. J. Jungnickel, Josi Steinke…·Christian Loew

This study identifies substrate specificity of bacterial ACS transporters using genetics, biochemistry, and structural biology, revealing structural determinants of stereoselectivity in LgoT.

DOI 10.64898/2026.05.20.726482

E. colistructural biology

𝕏 PostBluesky

BiochemistryNature Cell BiologyPeer-reviewedJun 5, 2024

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

Katharina E. J. Jungnickel, Océane Guelle, Miharu Iguchi…·Markus Daμμe

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

16 citations

mousemetabolomics

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BiochemistrybioRxivPreprintMar 11, 2024

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

Florian Gabriel, Lea Spriestersbach, Antonia Fuhrmann…·Christian Löw

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

DOI 10.1101/2024.03.11.584396

humancryo-EM

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