Author

P. Skowronek

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· 4

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Assay:proteomics· 3 Research Focus:benchmarking· 2 Approach:deep learning· 2 Approach:experimental assay· 2 Organism:human· 2 Approach:statistical model· 2 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

M. Mann· 3 shared M. Thielert· 3 shared F. Meier· 2 shared M. Wahle· 2 shared S. Willems· 2 shared A. Klein· 1 shared A.-D. Brunner· 1 shared E. Itang· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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3 shared papersBiochemistry

M. Mann

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4 papers

Recent·Most cited

The potential of plasma HLA peptides beyond neoepitopes

M. Wahle, M. Thielert, M. Zwiebel, P. Skowronek, W.-F. Zeng, M. Mann

The paper develops a sensitive method to analyze HLA peptides in plasma, revealing stable and tissue-representative immunopeptidomes with potential for biomarker discovery.

bioRxiv · Sep 5, 2023 · PreprintBiochemistry

Synchro-PASEF allows precursor-specific fragment ion extraction and interference removal in data-independent acquisition

P. Skowronek, F. Krohs, M. Lubeck, G. Wallmann, E. Itang, P. Koval, M. Wahle, M. Thielert, F. Meier, S. Willems, O. Raether, M. Mann

This paper introduces synchro-PASEF, a method that improves fragment ion extraction and interference removal in DIA proteomics by synchronizing ion mobility and mass dimensions.

bioRxiv · Nov 1, 2022Biochemistry

Rapid and in-depth coverage of the (phospho-)proteome with deep libraries and optimal window design for dia-PASEF

P. Skowronek, M. Thielert, E. Voytik, M. C. Tanzer, F. M. Hansen, S. Willems, O. Karayel, A.-D. Brunner, F. Meier, M. Mann

This paper introduces an optimized dia-PASEF method with variable isolation windows to enhance proteome and phosphoproteome coverage in mass spectrometry.

bioRxiv · May 31, 2022Biochemistry

Residue-specific insights into (2x)72 kDa tryptophan synthase obtained from fast-MAS 1H-detected solid-state NMR

A. Klein, P. Rovó, V. V. Sakhrani, Y. Wang, J. Holmes, V. Liu, P. Skowronek, L. Kukuk, S. K. Vasa, P. Güntert, L. J. Mueller, R. Linser

This study uses solid-state NMR to characterize a 72 kDa tryptophan synthase, overcoming size limitations and providing insights into catalytic residues.

bioRxiv · May 12, 2021 · PreprintBiochemistry