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Alessandro Vannini

Researcher at Institute of Cancer Research

Publications -  52
Citations -  3193

Alessandro Vannini is an academic researcher from Institute of Cancer Research. The author has contributed to research in topics: RNA polymerase II & RNA polymerase III. The author has an hindex of 20, co-authored 49 publications receiving 2732 citations. Previous affiliations of Alessandro Vannini include Sapienza University of Rome & Roma Tre University.

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Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor

TL;DR: The crystal structure of human HDAC8 in complex with a hydroxamic acid inhibitor is reported, indicating the importance of this HDAC subtype for tumor cell proliferation and a direct role of potassium in the fold stabilization ofHDAC8.
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Conservation between the RNA Polymerase I, II, and III Transcription Initiation Machineries

TL;DR: The similarities and differences between the three eukaryotic transcription machineries are outlined, including the conserved core initiation complex that stabilizes the open DNA promoter complex and directs initial RNA synthesis.
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The crystal structure of the quorum sensing protein TraR bound to its autoinducer and target DNA

TL;DR: The crystal structure of TraR, the transcriptional regulator involved in quorum sensing of Agrobacterium tumefaciens, is determined and reveals an asymmetric homodimer, with one monomer longer than the other.
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Structure of eukaryotic RNA polymerases.

TL;DR: A catalog of available structural information for Pol I, Pol II, and Pol III is provided, which showed that the active center region and core enzymes are similar to Pol II and that strong structural differences on the surfaces account for gene class-specific functions.
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Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex.

TL;DR: The structure clarifies the role of active‐ site residues in the deacetylation reaction and substrate recognition and shows the unexpected role of a conserved residue at the active‐site rim, Asp 101, in positioning the substrate by directly interacting with the peptidic backbone and imposing a constrained cis‐conformation.