Author

Stefanie Bungert‐Plümke

Forschungszentrum JülichORCID 0000-0002-4650-3274Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:cell type annotation· 1

Frequent Co-Authors

Christoph M. FahlkeiD· 2 shared Bassam G. HaddadiD· 1 shared Benedikt T. KuhniD· 1 shared Bettina BöttcheriD· 1 shared Eric R. GeertsmaiD· 1 shared Jan‐Philipp MachtensiD· 1 shared Peter KovermanniD· 1 shared Raul E. GuzmaniD· 1 shared

Activity by Year

2024-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersBiochemistry

Christoph M. FahlkeORCID

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2 papers

Recent·Most cited

SLC26A11 is an atypical solute carrier with dual transport-channel function mediating lysosomal sulfate transport

Benedikt T. Kuhn, Peter Kovermann, Bassam G. Haddad, Tim Rasmussen, Tamsanqa Tafara Hove, Stefanie Bungert‐Plümke, Bettina Böttcher, Jan‐Philipp Machtens, Christoph M. Fahlke, Eric R. Geertsma

This study identifies SLC26A11 as a dual-function protein that acts as both a sulfate transporter and a chloride channel, with implications for treating brain edema and lysosomal storage diseases.

Nature Communications · Jul 27, 2026Peer-reviewedBiochemistry

Oligomerization and cellular localization of SLC26A11

Stefanie Bungert‐Plümke, Raul E. Guzman, Christoph M. Fahlke

This study investigates the oligomerization and cellular localization of SLC26A11, finding it does not heterodimerize with other SLC26 proteins and remains localized to lysosomes.

bioRxiv · Apr 29, 2024 · PreprintCell Biology