Alessandro Vannini
- Head of Structural Biology Research Centre, Biologia Strutturale
- Research Group Leader, Vannini Group
Alessandro Vannini è un biochimico. Dirige il Centro di Biologia Strutturale dopo quasi otto anni passati nel Regno Unito in qualità di Principal Investigator e Deputy Head of Division all’Institute of Cancer Research di Londra.
Il suo laboratorio si occupa di studiare in dettaglio i meccanismi molecolari di complessi proteici che vengono assemblati intorno a siti di legame per la RNA Polymerase III e che giocano un ruolo fondamentale nella regolazione dell’espressione genica e nella organizzazione strutturale del genoma eucariotico. Questi meccanismi sono spesso deregolati in patalogie umane, quali il cancro e malattie neurodegenerative congenite.
Email: alessandro.vannini[at]fht.org
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Pubblicazioni
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10/2010 - Nucleic Acids Res
The archaeo-eukaryotic primase of plasmid pRN1 requires a helix bundle domain for faithful primer synthesis
The plasmid pRN1 encodes for a multifunctional replication protein with primase, DNA polymerase and helicase activity. The minimal region required for primase activity encompasses amino-acid residues 40-370. While the N-terminal part of that minimal region (residues 47-247) folds into the prim/pol domain and bears the active site, the structure and function of the C-terminal part […]
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05/2008 - Analytical Chemistry
Multiplexed proteomics mapping of yeast RNA polymerase II and III allows near-complete sequence coverage and reveals several novel phosphorylation sites
The multisubunit RNA polymerases (Pols) II and III synthesize mainly eukaryotic mRNAs and tRNAs, respectively. Pol II and Pol III are protein complexes consisting of 12 and 17 subunits. Here we analyzed both yeast Pol II and Pol III by multiplexed mass spectrometric analysis using various proteases and both collision induced and electron transfer dissociation. […]
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01/2008 - Annu Rev Biophys
Structure of eukaryotic RNA polymerases
The eukaryotic RNA polymerases Pol I, Pol II, and Pol III are the central multiprotein machines that synthesize ribosomal, messenger, and transfer RNA, respectively. Here we provide a catalog of available structural information for these three enzymes. Most structural data have been accumulated for Pol II and its functional complexes. These studies have provided insights […]
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10/2007 - Structure
Structural biology of RNA polymerase III: mass spectrometry elucidates subcomplex architecture
RNA polymerases (Pol) II and III synthesize eukaryotic mRNAs and tRNAs, respectively. The crystal structure of the 12 subunit Pol II is known, but only limited structural information is available for the 17 subunit Pol III. Using mass spectrometry (MS), we correlated masses of Pol II complexes with the Pol II structure. Analysis of Pol […]
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09/2007 - EMBO Rep
Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex
Histone deacetylases (HDACs)-an enzyme family that deacetylates histones and non-histone proteins-are implicated in human diseases such as cancer, and the first-generation of HDAC inhibitors are now in clinical trials. Here, we report the 2.0 A resolution crystal structure of a catalytically inactive HDAC8 active-site mutant, Tyr306Phe, bound to an acetylated peptidic substrate. The structure clarifies […]
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