Author

K. P. Locher

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· 4 Assay:cryo-EM· 3 Organism:human· 3 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:drug response / drug discovery· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1

Frequent Co-Authors

J. Kowal· 3 shared D. Ni· 2 shared H. Stahlberg· 2 shared I. Manolaridis· 2 shared R. N. Irobalieva· 2 shared A. A. Kossiakoff· 1 shared C.-w. Lin· 1 shared D. Glebe· 1 shared

Activity by Year

2021-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiophysics

J. Kowal

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structure of hepatitis B/D antiviral drug Bulevirtide bound to its receptor protein NTCP

H. Liu, D. Zakrzewicz, K. Nosol, R. N. Irobalieva, S. Mukherjee, R. Bang-Soerensen, N. Goldmann, S. Kunz, L. Rossi, A. A. Kossiakoff, S. Urban, D. Glebe, J. Geyer, K. P. Locher

The paper determines the cryo-EM structure of bulevirtide bound to NTCP, revealing its mechanism of inhibiting HBV/HDV entry and providing insights for drug development.

bioRxiv · Jan 22, 2024 · PreprintBiochemistry

Functional analysis of Ost3p and Ost6p containing yeast oligosaccharyltransferases

J. D. Neuhaus, R. Wild, J. Eyring, R. N. Irobalieva, J. Kowal, C.-w. Lin, K. P. Locher, M. Aebi

This study functionally analyzes Ost3p and Ost6p subunits in yeast OST, showing their roles in catalytic activity and substrate specificity.

bioRxiv · May 17, 2021Biochemistry

Structures of ABCG2 under turnover conditions reveal a key step in drug transport mechanism

Q. Yu, D. Ni, J. Kowal, I. Manolaridis, S. M. Jackson, H. Stahlberg, K. P. Locher

This study presents cryo-EM structures of ABCG2 under turnover conditions, revealing conformational changes that elucidate the transport mechanism and substrate specificity.

bioRxiv · Mar 3, 2021Biophysics

Structural basis of drug recognition by the multidrug transporter ABCG2

J. Kowal, D. Ni, S. Jackson, I. Manolaridis, H. Stahlberg, K. P. Locher

This study presents cryo-EM structures of ABCG2 bound to anticancer drugs, revealing how it recognizes and binds exogenous compounds and the structural basis for drug-induced ATPase activity.

bioRxiv · Feb 18, 2021Biophysics