• Publications
  • Influence
Crystal structures of the membrane-binding C2 domain of human coagulation factor V
A mechanism of calcium-independent, stereospecific binding of factors Va and VIIIa to phospholipid membranes is proposed, on the basis of immersion of hydrophobic residues at the apices of these loops in the apolar membrane core and specific interactions with phosphatidylserine head groups in the groove enclosed by these loops. Expand
Tick-derived Kunitz-type inhibitors as antihemostatic factors.
The unsurpassed versatility of tick-derived Kunitz inhibitors establishes them as valuable tools for biochemical investigations, but also as lead compounds for the development of novel antithrombotics. Expand
Nucleocytoplasmic Shuttling Activity of Ataxin-3
Data show that Atx3 is actively imported to and exported from the cell nucleus, and that its nuclear export activity is dependent on a motif located at its N-terminal region, which is significantly enhanced in a longer construct that is truncated after the two ubiquitin interaction motifs. Expand
Polyglutamine diseases: The special case of ataxin-3 and Machado–Joseph disease
A number of recent evidence support the idea that the toxic entities behind neuronal demise may be either the dysfunctional expanded atx3 or the soluble amyloid-like oligomers formed by self-assembly of the aggregation-prone mutated protein. Expand
Human β-tryptase is a ring-like tetramer with active sites facing a central pore
Human tryptase, a mast-cell-specific serine proteinase that may be involved in causing asthma and other allergic and inflammatory disorders, is unique in two respects: it is enzymatically active onlyExpand
Isolation, Cloning and Structural Characterisation of Boophilin, a Multifunctional Kunitz-Type Proteinase Inhibitor from the Cattle Tick
The crystal structure of the bovine α-thrombin·boophilin·trypsin complex, refined at 2.35 Å resolution reveals a non-canonical binding mode to the proteinase, and suggests a mechanism for prothrominase inhibition in vivo. Expand
DisProt 7.0: a major update of the database of disordered proteins
The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007 and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered. Expand
New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus
Comparisons with the hyperthermostable ferredoxin from Thermotoga maritima reveal that improved polar interactions within the common iron-sulfur cluster binding (βαβ)2 motif, and an optimized charge distribution at the protein surface constitute a common strategy for increasing the thermal stability of these ferredoxins. Expand
Towards a structural understanding of the fibrillization pathway in Machado-Joseph's disease: trapping early oligomers of non-expanded ataxin-3.
Non-expanded ataxin-3 oligomers are recognized by a specific antibody that targets a conformational epitope present in soluble cytotoxic species found in the fibrillization pathway of expanded polyglutamine proteins and other amyloid-forming proteins. Expand
Heterologous Expression of the Vanadium-containing Chloroperoxidase from Curvularia inaequalis inSaccharomyces cerevisiae and Site-directed Mutagenesis of the Active Site Residues His496, Lys353,
A general mechanism for haloperoxidase catalysis is proposed that also correlates the kinetic properties of the mutants with the charge and the hydrogen-bonding network in the vanadate-binding site. Expand