Author

G. Finocchio

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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Biophysics· 2 Biochemistry· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:structural biology· 3 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Approach:deep learning· 1

Frequent Co-Authors

C. Loew· 2 shared D. C. Swarts· 2 shared E. Pardon· 2 shared J. Steyaert· 2 shared M. Jinek· 2 shared M. Killer· 2 shared A. Potocnik· 1 shared A.-S. Humm· 1 shared

Activity by Year

2022-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiophysics

C. Loew

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

RNA-guided RNA silencing by an Asgard archaeal Argonaute

C. Bastiaanssen, P. B. Ugarte, K. Kim, Y. Feng, G. Finocchio, T. A. Anzelon, S. Kostlbacher, D. Tamarit, T. J. G. Ettema, M. Jinek, I. J. MacRae, C. Joo, D. C. Swarts, F. Wu

The paper identifies an Asgard archaeal Argonaute, HrAgo1, that performs RNA-guided RNA silencing, bridging the gap between prokaryotic and eukaryotic Argonaute mechanisms.

bioRxiv · Dec 14, 2023Microbiology

Target DNA-dependent activation mechanism of the prokaryotic immune system SPARTA

G. Finocchio, B. Koopal, A. Potocnik, C. Heijstek, M. Jinek, D. C. Swarts

This study reveals how SPARTA, a prokaryotic immune system, is activated by target DNA through structural changes that enable oligomerization and catalytic activity.

bioRxiv · Sep 23, 2023Biochemistry

Plasticity of the binding pocket in peptide transporters underpins promiscuous substrate recognition

V. Kotov, M. Killer, K. E. J. Jungnickel, J. Lei, G. Finocchio, J. Steinke, K. Bartels, J. Strauss, F. Dupeux, A.-S. Humm, I. Cornaciu, J. A. Marquez, E. Pardon, J. Steyaert, C. Loew

The paper investigates the substrate recognition mechanism of the bacterial POT DtpB using structural and biochemical analyses, revealing that compact hydrophobic peptides are optimal binders.

bioRxiv · Feb 14, 2023Biophysics

Cryo-EM structure of an atypical proton-coupled peptide transporter: Di- and tripeptide permease C

M. Killer, G. Finocchio, H. Mertens, D. I. Svergun, E. Pardon, J. Steyaert, C. Loew

This study determines the cryo-EM structure of DtpC, an atypical proton-coupled peptide transporter, revealing structural insights into its ligand selectivity.

bioRxiv · Apr 12, 2022Biophysics