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The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein*
TLDR
It is shown that NTAIL is able to bind its physiological partner, the phosphoprotein, and that it undergoes such an unstructured-to-structured transition upon binding to the C-terminal moiety of theosphoprotein.
K+ channel types targeted by synthetic OSK1, a toxin from Orthochirus scrobiculosus scorpion venom.
TLDR
Data suggest that OSK1 or [K16,D20]-OSK1 could serve as leads for the design and production of new immunosuppressive drugs.
Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton‐gated cation channels
TLDR
Psalmotoxin 1 (PcTx1), the first potent and specific blocker of the ASIC1a proton‐sensing channel, has been successfully expressed in the Drosophila melanogaster S2 cell recombinant expression system used here for the first time to produce a spider toxin.
Thermal unfolding of a llama antibody fragment: a two-state reversible process.
TLDR
The essentially complete (1)H and (15)N NMR backbone resonance assignments of a llama V(HH) antibody fragment, and an extensive analysis of the structure at higher temperatures are reported.
The Location of the Ligand-binding Site of Carbohydrate-binding Modules That Have Evolved from a Common Sequence Is Not Conserved*
TLDR
Structural data define a superfamily of CBMs, comprising CBM4, CBM6, and CBM22, and demonstrate that, although CBMs have evolved from a relatively small number of ancestors, the structural elements involved in ligand recognition have been assembled at different locations on the ancestral scaffold.
Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton‐gated channels
TLDR
A putative channel interaction surface is suggested for APETx2, encompassing its N terminus together with the type I‐β turn connecting β‐strands III and IV, which could play a role in the specificity observed for these different ion channel effectors.
Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: A new fold for an HERG toxin
TLDR
The structure of APETx1 is compared to those of the two other known effectors of the Ether‐a‐gogo potassium channel, CnErg1 and BeKm‐1, and the topological disposition of key functional residues proposed by analysis of the electrostatic anisotropy is analyzed.
Chemical synthesis and characterization of maurotoxin, a short scorpion toxin with four disulfide bridges that acts on K+ channels.
TLDR
The physicochemical and pharmacological properties of synthetic maurotoxin were indistinguishable from those of natural mau Rotoxin, which suggests that natural mAUrotoxin adopts the same half-cystine pairing pattern.
Generating a High Affinity Scorpion Toxin Receptor in KcsA-Kv1.3 Chimeric Potassium Channels*
TLDR
A structural model for the complex between KcsA-Kv1.3 chimeras and kaliotoxin is developed to aid future pharmacological studies of K+ channels and shows that a subregion of the S5-S6 linker may be an important determinant of the pharmacological profile of K- channels.
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