Author

K.-M. Kammer

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· 4 Assay:proteomics· 4 Approach:experimental assay· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell-cell communication· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:differential expression· 1

Frequent Co-Authors

F. Stengel· 4 shared J. Fuersch· 2 shared A. A. Hyman· 1 shared A. Pozniakovski· 1 shared C. Sailer· 1 shared C. Voormann· 1 shared D. Mateju· 1 shared E. E. Boczek· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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4 shared papersBiochemistry

F. Stengel

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Author profile →

4 papers

Recent·Most cited

Kinetic principles of chemical cross-link formation for protein-protein interactions

K.-M. Kammer, R. Pellarin, F. Stengel

This study develops a kinetic model to describe cross-link formation in protein-protein interactions and identifies optimal cross-linker concentrations for maximizing cross-link yield.

bioRxiv · Feb 19, 2024 · PreprintBiochemistry

A mono- and intralink filter (mi-filter) to improve false-discovery rates in cross-linking mass spectrometry data

X. Chen, C. Sailer, K.-M. Kammer, J. Fuersch, M. R. Eisele, E. Sakata, F. Stengel

The paper introduces a filter to reduce false-discovery rates in cross-linking mass spectrometry data by requiring monolink or intra-protein crosslinks for inter-protein link validation.

bioRxiv · Feb 3, 2022Biochemistry

Structural probing of Hsp26 activation and client binding by quantitative cross-linking mass spectrometry

J. Fuersch, C. Voormann, K.-M. Kammer, F. Stengel

This study uses cross-linking mass spectrometry to investigate the structural changes and client-binding mechanisms of yeast Hsp26 during activation and refolding.

bioRxiv · Jun 6, 2021Biochemistry

HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA binding domain

E. E. Boczek, J. Fursch, L. Jawerth, M. Jahnel, M. L. Niedermeier, M. Ruer-Gruss, K.-M. Kammer, L. Mediani, J. Wang, X. Yan, A. Pozniakovski, I. Poser, D. Mateju, S. Carra, S. Alberti, , F. Stengel

This study identifies HspB8's role in preventing FUS condensate hardening by interacting with its RNA-binding domain, suggesting a mechanism to prevent neurodegenerative disease-associated phase transitions.

bioRxiv · Apr 13, 2021Biochemistry