Author

S. Klinke

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· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

L. H. Otero· 4 shared F. A. Goldbaum· 3 shared L. A. Defelipe· 2 shared A. J. Cagnoni· 1 shared A. Tijman· 1 shared C. Huck-Iriart· 1 shared C. Löw· 1 shared D. Monti· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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4 shared papersBiochemistry

L. H. Otero

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

A fijivirus major viroplasm protein shows RNA-stimulated ATPase activity by adopting pentameric and hexameric assemblies of dimers

G. Llauger, R. Melero, D. Monti, G. Sycz, C. Huck-Iriart, M. L. Cerutti, S. Klinke, E. Mikkelsen, A. Tijman, R. Arranz, V. Alfonso, S. M. Arellano, F. A. Goldbaum, Y. G. J. Sterckx, J.-M. Carazo, , L. H. Otero

This study identifies the structural and functional roles of the C-arm in the fijivirus P9-1 protein, revealing its role in viroplasm assembly and RNA-stimulated ATPase activity.

bioRxiv · Apr 16, 2022Biochemistry

Deamidation drives molecular aging of the SARS-CoV-2 spike receptor-binding motif

R. Lorenzo, L. A. Defelipe, L. Aliperti, S. Niebling, T. F. Custodio, C. Löw, J. J. Schwarz, K. Remans, P. O. Craig, L. H. Otero, S. Klinke, M. Garcia-Alai, I. E. Sanchez, L. G. Alonso

This study identifies deamidation hotspots in the SARS-CoV-2 spike receptor-binding motif, showing how this post-translational modification affects viral infectivity and immune response over time.

bioRxiv · May 20, 2021Biochemistry

Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level

L. H. Otero, S. Foscaldi, G. T. Antelo, S. Sirigu, S. Klinke, L. A. Defelipe, M. Sanchez-Lamas, G. Battocchio, L. M. G. Chavas, F. A. Goldbaum, M. A. Mroginski, J. Rinaldi, H. R. Bonomi

The paper presents atomic-level crystal structures of a full-length bacterial phytochrome in Pr and Pfr states, revealing the signaling mechanism involving chromophore isomerization and structural transitions.

bioRxiv · Feb 16, 2021Biophysics

Crystal structures of peanut lectin in the presence of synthetic β-N- and β-S-galactosidesdisclose evidences for the recognition of different glycomimetic ligands

A. J. Cagnoni, E. D. Primo, S. Klinke, M. E. Cano, W. Giordano, K. V. Marino, J. Kovensky, F. A. Goldbaum, M. L. Uhrig, L. H. Otero

This study reports crystal structures of peanut lectin bound to synthetic β-N- and β-S-galactosides, revealing molecular interactions and binding affinities for these novel ligands.

bioRxiv · Jun 20, 2020Biochemistry