Author

T. Karlberg

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

A.-G. Thorsell· 2 shared H. Schuler· 2 shared K. Nareoja· 2 shared A. A. Saei· 1 shared A. Chernobrovkin· 1 shared A. F. Pinto· 1 shared A. Nordstrom· 1 shared A. Vegvari· 1 shared

Activity by Year

2018-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersBiochemistry

A.-G. Thorsell

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Author profile →

2 papers

Recent·Most cited

System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA)

A. A. Saei, C. Beusch, P. Sabatier, J. Astorga Wells, A. Chernobrovkin, S. Rodin, K. Nareoja, A.-G. Thorsell, T. Karlberg, Q. Cheng, S. L. Lundstrom, M. Gaetani, A. Vegvari, E. S. J. Arner, H. Schuler, R. Zubarev

SIESTA identifies and prioritizes enzyme substrates by detecting thermal stability changes caused by post-translational modifications, demonstrating effectiveness across multiple enzyme systems.

bioRxiv · Jan 21, 2020Biochemistry

14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface

T. Karlberg, P. Hornyak, A. F. Pinto, S. Milanova, M. Ebrahimi, M. Lindberg, N. Pullen, A. Nordstrom, E. Loverli, R. Caraballo, E. V. Wong, K. Nareoja, A.-G. Thorsell, M. Elofsson, E. M. De La Cruz, , H. Schuler

This study identifies a novel hydrophobic interface between 14-3-3 proteins and Pseudomonas exotoxins-S and -T, showing 14-3-3 activates these toxins by preventing aggregation, independent of their C-terminal phosphopeptide binding motifs.

bioRxiv · Jun 8, 2018Biochemistry