Author

P. Fucini

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· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:bacteria (other)· 2 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Schedlbauer· 3 shared B. Ochoa-Lizarralde· 3 shared R. Capuni· 3 shared S. R. Connell· 3 shared T. Kaminishi· 3 shared E. de Astigarraga· 2 shared A. Fabbretti· 1 shared C. O. Gualerzi· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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3 shared papersBiochemistry

A. Schedlbauer

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Orthoformimycin inhibits translation elongation by displacing the A-site tRNA and preventing peptide bond formation

A. Schedlbauer, T. Kaminishi, A. Fabbretti, P. Milon, X. Han, B. Ochoa-Lizarralde, R. Capuni, C. O. Gualerzi, S. R. Connell, P. Fucini

This study investigates how orthoformimycin inhibits translation elongation by displacing the A-site tRNA and blocking peptide bond formation using X-ray crystallography and kinetic analysis.

bioRxiv · Nov 29, 2021 · PreprintBiochemistry

A conserved rRNA switch is central to decoding site maturation on the small ribosomal subunit

A. Schedlbauer, I. Iturrioz, B. Ochoa-Lizarralde, T. Diercks, J. P. Lopez-Alonso, J. L. Lavin, T. Kaminishi, R. Capuni, N. Dhimole, E. de Astigarraga, D. Gil-Carton, P. Fucini, S. R. Connell

The paper uses cryo-EM to study bacterial ribosome assembly factors and identifies a conserved rRNA switch involved in decoding site maturation.

bioRxiv · Oct 19, 2020Microbiology

The third-generation tetracycline, KBP-7072, exploits and reveals a new potential of the primary tetracycline binding pocket

T. Kaminishi, A. Schedlbauer, B. Ochoa-Lizarralde, E. de Astigarraga, R. Capuni, F. Yang, V. Benn, Q. Liu, X. Tan, M. Zhang, S. R. Connell, P. Fucini

This study determines the structure of KBP-7072 bound to the 30S ribosomal subunit, showing it inhibits protein synthesis by binding to the primary tetracycline site and interacting uniquely with the subunit.

bioRxiv · Dec 31, 2018 · PreprintBiochemistry