Alessandro Vannini
- Head of Structural Biology Research Centre, Structural biology
- Research Group Leader, Vannini Group
Alessandro Vannini is a biochemist. He heads the Centre for Structural Biology after almost 8 years as a Principal Investigator and Deputy Head of Division at the Institute of Cancer Research in London.
His laboratory focuses on structural and functional analisys of large macromolecular complexes assembling around RNA Pol III loci and that play a role in gene expression and structural organization of the eukaryotic genome. These mechanisms are often deregulated in human diseases, such as cancer and congenital neurodegenerative diseases.
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Publications
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10/2004 - Proc Natl Acad Sci U S A
Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor
Histone deacetylases (HDACs) are a family of enzymes involved in the regulation of gene expression, DNA repair, and stress response. These processes often are altered in tumors, and HDAC inhibitors have had pronounced antitumor activity with promising results in clinical trials. Here, we report the crystal structure of human HDAC8 in complex with a hydroxamic […]
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06/2004 - J Biol Chem
Crystal structure of the quorum-sensing protein TraM and its interaction with the transcriptional regulator TraR
Transfer of the tumor-inducing plasmid in Agrobacterium tumefaciens is controlled by a quorum-sensing system whose main components are the transcriptional regulator TraR and its autoinducer. This system allows bacteria to synchronize infection of the host plant when a “quorum” of cells has been reached. TraM is an A. tumefaciens protein involved in the regulation of […]
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02/2004 - Biochemistry
Mechanism of activation of human heparanase investigated by protein engineering
The aim of this study was to investigate the mechanism of activation of human heparanase, a key player in heparan sulfate degradation, thought to be involved in normal and pathologic cell migration processes. Active heparanase arises as a product of a series of proteolytic processing events. Upon removal of the signal peptide, the resulting, poorly […]
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01/2004 - Acta Crystallogr D Biol Crystallogr
Crystallization and preliminary X-ray diffraction studies of the quorum-sensing regulator TraM from Agrobacterium tumefaciens
TraM is a 11.4 kDa protein involved in the control of the conjugal transfer of Agrobacterium tumefaciens Ti plasmids by quorum-sensing. TraM was overexpressed and purified from Escherichia coli. This protein binds to the transcriptional regulator TraR, abolishing its function. Size-exclusion chromatography and dynamic light scattering show that the recombinant protein has an apparent molecular […]
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10/2002 - Analytical Chemistry
Determination of the stoichiometry of noncovalent complexes using reverse-phase high-performance liquid chromatography coupled with electrospray ion trap mass spectrometry
An electrospray mass spectrometry-based methodology has been developed to have a fast and sensitive method for protein-cofactor stoichiometry determination. As model systems, we used two proteins which require the presence of cofactors for activity: TraR, a member of the LuxR family of quorum-sensing transcriptional regulators, which requires an acyl-homoserine lactone molecule called Agrobacterium autoinducer (AAI) […]
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