Author

B. Steigenberger

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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Approach:experimental assay· 4 Research Focus:chromatin & epigenetic regulation· 2 Assay:structural biology· 2 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

R. A. Scheltema· 4 shared A. J. R. Heck· 2 shared A. Konijnenberg· 1 shared A. M. J. J. Bonvin· 1 shared A. M. Liaci· 1 shared C. Basquin· 1 shared E. Bijl· 1 shared E. Lorentzen· 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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4 shared papersBiochemistry

R. A. Scheltema

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Author profile →

4 papers

Recent·Most cited

Thriving in the heat - Lysine acetylation stabilizes the quaternary structure of a Mega-Dalton hyperthermoactive PEP-synthase

P. Albanese, W. Song, S. v. Keulen, J. Koendjbiharie, F. Koh, B. Steigenberger, T. Vincent, A. Konijnenberg, A. J. R. Heck, S. Kengen, A. M. J. J. Bonvin, F. Förster, R. A. Scheltema

The paper investigates how lysine acetylation stabilizes the structure of a hyperthermoactive PEP-synthase from Pyrococcus furious, revealing its role in maintaining function under extreme temperatures.

bioRxiv · Aug 11, 2022 · PreprintBiochemistry

Nse5/6 inhibits the Smc5/6 ATPase to facilitate DNA substrate selection.

M. Taschner, J. Basquin, B. Steigenberger, I. Schaefer, Y.-M. Soh, C. Basquin, E. Lorentzen, M. Raeschle, R. A. Scheltema, S. Gruber

The paper shows Nse5/6 inhibits Smc5/6 ATPase activity, modulating DNA substrate selection in yeast.

bioRxiv · Feb 9, 2021Biochemistry

Structure of the Human Signal Peptidase Complex Reveals the Determinants for Signal Peptide Cleavage

A. M. Liaci, B. Steigenberger, S. Tamara, P. C. Telles de Souza, M. Grollers-Mulderij, P. Ogrissek, S.-J. Marrink, R. A. Scheltema, F. Foerster

The paper determines the atomic structures of human signal peptidase complex paralogs and identifies how their architecture enables specific recognition and cleavage of signal peptides.

bioRxiv · Nov 11, 2020Biochemistry

Benefits of Collisional Cross Section Assisted Precursor Selection (caps-PASEF) for Cross-linking Mass Spectrometry

B. Steigenberger, H. W. P. van den Toorn, E. Bijl, J.-F. Greisch, O. Raether, M. Lubeck, R. J. Pieters, A. J. R. Heck, R. A. Scheltema

The paper demonstrates that ion mobility improves cross-linking mass spectrometry by separating mono-linked peptides from cross-linked peptide pairs, increasing detected cross-linked peptides by 50-70%.

bioRxiv · Apr 16, 2020Biochemistry