User profiles for Nicolas Gilles

Nicolas Gilles

reseacher CEA
Verified email at cea.fr
Cited by 3101

The differential preference of scorpion α-toxins for insect or mammalian sodium channels: implications for improved insect control

D Gordon, I Karbat, N Ilan, L Cohen, R Kahn, N Gilles… - Toxicon, 2007 - Elsevier
Receptor site-3 on voltage-gated sodium channels is targeted by a variety of structurally
distinct toxins from scorpions, sea anemones, and spiders whose typical action is the inhibition …

[HTML][HTML] Distinct primary structures of the major peptide toxins from the venom of the spider Macrothele gigas that bind to sites 3 and 4 in the sodium channel

G Corzo, N Gilles, H Satake, E Villegas, L Dai… - FEBS letters, 2003 - Elsevier
Six peptide toxins (Magi 1–6) were isolated from the Hexathelidae spider Macrothele gigas.
The amino acid sequences of Magi 1, 2, 5 and 6 have low similarities to the amino acid …

New method for characterizing highly disulfide-bridged peptides in complex mixtures: application to toxin identification from crude venoms

L Quinton, K Demeure, R Dobson, N Gilles… - Journal of proteome …, 2007 - ACS Publications
Animal venoms are highly complex mixtures that can contain many disulfide-bridged toxins.
This work presents an LC-MALDI approach allowing (1) a rapid classification of toxins …

[HTML][HTML] Common features in the functional surface of scorpion β-toxins and elements that confer specificity for insect and mammalian voltage-gated sodium channels

L Cohen, I Karbat, N Gilles, N Ilan, M Benveniste… - Journal of Biological …, 2005 - ASBMB
Scorpion β-toxins that affect the activation of mammalian voltage-gated sodium channels (Na
v s) have been studied extensively, but little is known about their functional surface and …

Peptidomic comparison and characterization of the major components of the venom of the giant ant Dinoponera quadriceps collected in four different areas of Brazil

…, E Jourdan, M Degueldre, G Upert, N Gilles… - Journal of …, 2013 - Elsevier
Despite the noxious effects inflicted by Dinoponera ant's envenomation, the information about
the biological properties and composition of their venom is still very limited. Ants from the …

[HTML][HTML] Molecular basis of the high insecticidal potency of scorpion α-toxins

I Karbat, F Frolow, O Froy, N Gilles, L Cohen… - Journal of Biological …, 2004 - ASBMB
Scorpion α-toxins are similar in their mode of action and three-dimensional structure but differ
considerably in affinity for various voltage-gated sodium channels (NaChs). To clarify the …

Isolation and pharmacological characterization of AdTx1, a natural peptide displaying specific insurmountable antagonism of the α1A‐adrenoceptor

…, A Ménez, S Palea, D Servent, N Gilles - British journal of …, 2010 - Wiley Online Library
Background and purpose: Venoms are a rich source of ligands for ion channels, but very little
is known about their capacity to modulate G‐protein coupled receptor (GPCR) activity. We …

Green mamba peptide targets type-2 vasopressin receptor against polycystic kidney disease

…, C Mendre, R Witzgall, N Gilles - Proceedings of the …, 2017 - National Acad Sciences
Polycystic kidney diseases (PKDs) are genetic disorders that can cause renal failure and
death in children and adults. Lowering cAMP in cystic tissues through the inhibition of the type-…

[HTML][HTML] High-throughput expression of animal venom toxins in Escherichia coli to generate a large library of oxidized disulphide-reticulated peptides for drug …

…, CIPD Guerreiro, L Quinton, E De Pauw, N Gilles… - Microbial cell …, 2017 - Springer
Background Animal venoms are complex molecular cocktails containing a wide range of
biologically active disulphide-reticulated peptides that target, with high selectivity and efficacy, a …

[HTML][HTML] Gene design, fusion technology and TEV cleavage conditions influence the purification of oxidized disulphide-rich venom peptides in Escherichia coli

…, LT Gama, LMA Ferreira, CIPI Guerreiro, N Gilles… - Microbial cell …, 2017 - Springer
Background Animal venoms are large, complex libraries of bioactive, disulphide-rich peptides.
These peptides, and their novel biological activities, are of increasing pharmacological …