Author

V. Kotov

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· 1 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 2 Approach:deep learning· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Organism:bacteria (other)· 1 Assay:bulk RNA-seq· 1 Research Focus:differential expression· 1

Frequent Co-Authors

J. Strauss· 2 shared K. E. J. Jungnickel· 2 shared A. Ejima· 1 shared A. R. Mehdipour· 1 shared A.-S. Humm· 1 shared B. Gasnier· 1 shared C. Debacker· 1 shared C. Loew· 1 shared

Activity by Year

2023-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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2 shared papersCell Biology

J. Strauss

Mutual co-authors in cluster

Author profile →

3 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

Iron transport pathways in the human malaria parasite Plasmodium falciparum revealed by RNA-sequencing

J. Wunderlich, V. Kotov, L. Votborg-Novel, C. Ntalla, M. Geffken, S. Peine, S. Portugal, J. Strauss

This study identifies six iron transport proteins in Plasmodium falciparum using RNA-sequencing and functional assays, revealing a new model of iron homeostasis in the parasite.

bioRxiv · Apr 18, 2024 · PreprintCell Biology

Plasticity of the binding pocket in peptide transporters underpins promiscuous substrate recognition

V. Kotov, M. Killer, K. E. J. Jungnickel, J. Lei, G. Finocchio, J. Steinke, K. Bartels, J. Strauss, F. Dupeux, A.-S. Humm, I. Cornaciu, J. A. Marquez, E. Pardon, J. Steyaert, C. Loew

The paper investigates the substrate recognition mechanism of the bacterial POT DtpB using structural and biochemical analyses, revealing that compact hydrophobic peptides are optimal binders.

bioRxiv · Feb 14, 2023Biophysics