Author

H. Mertens

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 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Organism:E. coli· 1

Frequent Co-Authors

C. Loew· 2 shared D. I. Svergun· 2 shared S. Pazicky· 2 shared T. Gilberger· 2 shared A. Alder· 1 shared A. Sonn-Segev· 1 shared C. Löw· 1 shared D. Debabrata· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiophysics

C. Loew

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Cryo-EM structure of an atypical proton-coupled peptide transporter: Di- and tripeptide permease C

M. Killer, G. Finocchio, H. Mertens, D. I. Svergun, E. Pardon, J. Steyaert, C. Loew

This study determines the cryo-EM structure of DtpC, an atypical proton-coupled peptide transporter, revealing structural insights into its ligand selectivity.

bioRxiv · Apr 12, 2022Biophysics

Protein Quaternary Structures in Solution are a Mixture of Multiple forms

S. Marciano, D. Debabrata, D. Listov, S. J. Fleishman, A. Sonn-Segev, H. Mertens, F. Busch, Y. Kim, S. R. Harvey, V. H. Wysocki, G. Schreiber

The paper assesses the oligomeric states of 17 bacterial proteins using multiple techniques, finding that most exist in multiple forms and that AlphaFold Multimer better predicts their quaternary structures than existing databases.

bioRxiv · Mar 30, 2022Biochemistry

N-terminal phosphorylation regulates the activity of Glycogen Synthase Kinase 3 from Plasmodium falciparum

S. Pazicky, A. Alder, H. Mertens, D. I. Svergun, T. Gilberger, C. Loew

This study identifies N-terminal phosphorylation sites in PfGSK3 that regulate its activity through conformational changes, offering insights into malarial parasite biology.

bioRxiv · Jun 18, 2021Biochemistry

Structural role of essential light chains in the apicomplexan glideosome

S. Pazicky, K. Dhamotharan, K. Kaszuba, H. Mertens, T. Gilberger, D. Svergun, J. Kosinski, U. Weininger, C. Löw

This study determines the structure of trimeric glideosome subcomplexes in Toxoplasma gondii, revealing conserved interactions and the role of essential light chains in stabilizing myosin A.

Communications Biology · Oct 13, 2020Peer-reviewedBiophysics