Author

R. A. Scheltema

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· 12

Signature Assays, Organisms & Methods

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Approach:experimental assay· 11 Assay:proteomics· 7 Research Focus:protein folding & dynamics· 5 Research Focus:chromatin & epigenetic regulation· 3 Organism:human· 3 Research Focus:cell type annotation· 2 Research Focus:protein structure prediction· 2 Approach:statistical model· 2

Frequent Co-Authors

A. J. R. Heck· 6 shared B. Steigenberger· 4 shared P. Albanese· 4 shared A. Jankevics· 3 shared M. Lubeck· 2 shared R. J. Pieters· 2 shared A. B. Meijer· 1 shared A. Bar Barroeta· 1 shared

Activity by Year

2019-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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6 shared papersBiochemistry

A. J. R. Heck

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12 papers

Recent·Most cited

Fast and accurate disulfide bridge detection

S. Heissel, Y. He, A. Jankevics, Y. Shi, H. Molina, R. Viner, R. A. Scheltema

This paper presents a fast and accurate method for detecting disulfide bridges in proteins using mass spectrometry with optimized sample preparation and data analysis.

bioRxiv · Nov 22, 2023Biochemistry

Type III-B CRISPR-Cas signaling-based cascade of proteolytic cleavages

J. Steens, J. P. Bravo, C. R. P. Salazar, C. Yildiz, A. M. Amieiro, S. Kostlbacher, S. H. P. Prinsen, C. Patinios, A. Bardis, A. Barendrecht, R. A. Scheltema, T. J. G. Ettema, J. van der Oost, D. W. Taylor, R. Staals

This study characterizes a type III-B CRISPR-Cas system in Haliangium ochraceum, revealing a proteolytic cascade involving SAVED-CHAT and PCaspase that activates immune responses against RNA targets.

bioRxiv · Jun 23, 2023 · PreprintBiochemistry

Thrombin activation of the factor XI dimer is a multi-staged process for each subunit

A. Bar Barroeta, P. Albanese, A. Marquart, J. C. M. Meijers, R. A. Scheltema

This study investigates thrombin's multi-staged activation of FXI, identifying key binding sites and dynamics involved in the process.

bioRxiv · Feb 11, 2023Biochemistry

CAF-1 deposits newly synthesized histones during DNA replication using distinct mechanisms on the leading and lagging strands

C. Rouillon, B. V. Eckhardt, L. Kollenstart, F. Gruss, A. E. E. Verkennis, I. Rondeel, P. H. L. Krijger, G. Ricci, A. Biran, T. van Laar, C. M. Delvaux de Fenffe, G. Luppens, P. Albanese, R. A. Scheltema, W. de Laat, , F. Mattiroli

This study shows CAF-1 deposits histones on both DNA strands during replication but uses different mechanisms on leading and lagging strands.

bioRxiv · Oct 14, 2022Biochemistry

MRPS36 provides a missing link in the eukaryotic 2-oxoglutarate dehydrogenase complex for recruitment of E3 to the E2 core

J. f. Hevler, P. Albanese, A. Cabrera-Orefice, A. Potter, A. Jankevics, J. Misic, R. A. Scheltema, U. Brandt, S. Arnold, A. J. R. Heck

The paper identifies MRPS36 as an essential component of the eukaryotic 2-oxoglutarate dehydrogenase complex, replacing the bacterial PSBD and providing structural insights into its organization.

bioRxiv · Oct 8, 2022 · PreprintBiochemistry

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

Oxonium Ion-Guided Ion Mobility-Assisted Glycoproteomics on the timsTOF Pro

S. Mukherjee, A. Jankevics, F. Busch, M. Lubeck, Y. Zou, G. Kruppa, A. J. R. Heck, R. A. Scheltema, K. Reiding

This paper introduces a method using ion mobility on the timsTOF Pro to separate glycopeptides from non-modified peptides, improving glycoproteomics analysis of complex samples.

bioRxiv · Jul 4, 2022Biochemistry

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

Flexible regions in the molecular architecture of Human fibrin clots structurally resolved by XL-MS and integrative structural modeling

O. Klykov, C. v. d. Zwaan, A. J. R. Heck, A. B. Meijer, R. A. Scheltema

This study resolves the molecular architecture of human fibrin clots using XL-MS and integrative modeling, revealing structural details of key domains and their role in lateral aggregation and clot formation.

bioRxiv · Aug 19, 2019 · PreprintBiochemistry

PhoX - an IMAC-enrichable Crosslinking Reagent

B. A. Steigenberger, R. J. Pieters, A. J. R. Heck, R. A. Scheltema

The paper introduces PhoX, a crosslinking reagent that enhances detection of crosslinked peptides through IMAC enrichment, demonstrating improved efficiency and specificity in structural studies.

bioRxiv · Feb 21, 2019Biochemistry