P. F. Boesman, 163. Notes on the vocalizations of Rusty Pitohui (Pitohui ferrugineus), Ornithological Notes, 2016.

P. Bourée, Morsures de serpents, Médecine et Santé Tropicales, vol.24, issue.3, pp.255-256, 2014.

J. F. Paschoal, J. Yamaguchi, J. R. Miranda, G. Carretero, R. L. Melo et al., Insights into cardiovascular effects of proline-rich oligopeptide (Bj-PRO-10c) revealed by structure?activity analyses: dissociation of antihypertensive and bradycardic effects, Amino Acids, vol.46, issue.2, pp.401-413, 2013.

E. G. Dehaut, Les venins des Batraciens et les Batraciens venimeux; étude de zoologie médicale., VENINS, Les venins en recherche biologique et médicale -Encyclopaedia Universalis, 1910.

D. Sur,

. Cea and . Toxines, récepteurs et canaux ioniques

P. Joliot, Recherche fondamentale et recherche appliquée, Les conférences du Collège de France, 2011.

J. Chippaux, Toxicologie des venins, Venins de serpent et envenimations, pp.87-133

D. Sur, Eau disponible pour l'utilisation, 2017.

A. Depil-duval, Envenimations vipérines

. Santé-&-médecine-présenté-À, , vol.18, 2019.

D. Sur, Graphique 2.1. Revenu disponible ajusté net des ménages par habitant

. La-fonction-venimeuse, . Christine, . Jean-philippe, and . Max, Extrait [Internet]. calameo.com. [cité 30 juill, 2019.

B. G. Fry, K. Roelants, D. E. Champagne, H. Scheib, J. D. Tyndall et al., The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms, Annual Review of Genomics and Human Genetics, vol.10, issue.1, pp.483-511, 2009.

T. Besson, Étude de la régulation pharmacologique des canaux ioniques ASIC par des toxines animales, vol.12

D. Sur,

J. Chippaux, Place de l?immunothérapie dans le traitement actuel des envenimations ophidiennes, Bulletin de l'Académie Nationale de Médecine, vol.197, issue.4-5, pp.993-1008, 2013.

, Reorganizing the protein space at the Universal Protein Resource (UniProt), Nucleic Acids Research, vol.40, issue.D1, pp.D71-D75, 2011.

P. P. Aubry, Envenimations par les animaux terrestres, p.12

S. Larréché, Conduite à tenir devant une morsure de serpent

C. Dionne, Nos araignées moeurs et description /, 1910.

M. Manuels, . Le, and . Public,

D. Sur,

Y. Letourneux, J. Molgo, . Biodiversity, . The, . Conus-;-a-rich et al., , p.26

M. M. Yves and M. A. Karim, Ingénieurs Professeurs agrégés certifiés (IPAC) : Mme CONAN Muriel, Professeur d'anglais Mme CALAGUE, Professeur d'éducation physique

, Réctions allergiques aux aldéhydes: Glutaraldeéhyde et formaldéhyde études de cas observés au chu de reims, Acta Endoscopica, vol.30, issue.3, pp.XXV-XXV, 2000.

R. F. Foelix, Biology of Spiders, Insect Systematics & Evolution, vol.14, issue.1, p.16, 1983.

C. Nezha, A. Soulaymani, A. Mokhtari, and R. Bencheikh, Les envenimations scorpioniques à l'hôpital provincial de Beni Mellal, vol.69, pp.33-39, 2009.

L. Rouschmeyer, Clé de détermination simplifiée des Scorpions, p.15

F. A. Cordeiro, F. G. Amorim, F. A. Anjolette, and E. C. Arantes, Arachnids of medical importance in Brazil: main active compounds present in scorpion and spider venoms and tick saliva, Journal of Venomous Animals and Toxins including Tropical Diseases, vol.21, issue.1, 2015.

. Netgen, Envenimations marines; deuxième partie: Invertébrés, The Journal of Emergency Medicine, vol.10, issue.1, p.125, 1992.

. Revue-médicale-suisse, Regroupement en informatique médicale de laboratoire en Suisse, Revue Francophone des Laboratoires, vol.2013, issue.457, p.15, 2013.

D. Sur, Figure 4?figure supplement 1. Pearson correlation of gene expression from RNA-seq data of primary human RMS.

Y. Letourneux and A. Alliot, Les mollusques du genre Conus et les applications thérapeutiques de leurs venins, 2004.

G. Conotoxin and . Superfamilies,

B. Gao, C. Peng, J. Yang, Y. Yi, J. Zhang et al., Cone Snails: A Big Store of Conotoxins for Novel Drug Discovery, Toxins, vol.9, issue.12, p.397, 2017.

G. F. King, M. C. Gentz, P. Escoubas, and G. M. Nicholson, A rational nomenclature for naming peptide toxins from spiders and other venomous animals, Toxicon, vol.52, issue.2, pp.264-276, 2008.

. Douleur, Inserm -La science pour la santé

D. Sur,

Y. Frullani, Ventes de médicaments en France : stabilité en 2011, Actualités Pharmaceutiques, vol.51, issue.521, p.6, 2012.

J. Sol, P. Bases-anatomiques, and . Et-psychologiques, , p.27

E. Lingueglia, Douleur et canaux ioniques : une mise à jour importante mais pas encore majeure, Douleur et Analgésie, vol.29, issue.4, pp.187-188, 2016.

H. Kweon and B. Suh, Acid-sensing ion channels (ASICs): therapeutic targets for neurological diseases and their regulation, BMB Reports, vol.46, issue.6, pp.295-304, 2013.

C. J. Kreple, Y. Lu, R. J. Taugher, A. L. Schwager-gutman, J. Du et al., Acid-sensing ion channels contribute to synaptic transmission and inhibit cocaine-evoked plasticity, Nature Neuroscience, vol.17, issue.8, pp.1083-1091, 2014.

. Asics and . Neuropeptides,

M. P. Price, H. Gong, M. G. Parsons, J. R. Kundert, L. R. Reznikov et al., Localization and behaviors in null mice suggest that ASIC1 and ASIC2 modulate responses to aversive stimuli, Genes, Brain and Behavior, vol.13, issue.2, pp.179-194, 2013.

J. Mamet, A. Baron, M. Lazdunski, and N. Voilley, ProInflammatory Mediators, Stimulators of Sensory Neuron Excitability via the Expression of Acid-Sensing Ion Channels, The Journal of Neuroscience, vol.22, issue.24, pp.10662-10670, 2002.
URL : https://hal.archives-ouvertes.fr/hal-02277311

S. Kellenberger, L. D. Rash, and L. Schild, Acid-sensing (proton-gated) ion channels (ASICs) (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database, IUPHAR/BPS Guide to Pharmacology CITE, vol.2019, issue.4, 2019.

D. Sur,

F. Bosmans and K. J. Swartz, Targeting voltage sensors in sodium channels with spider toxins, Trends in Pharmacological Sciences, vol.31, issue.4, pp.175-182, 2010.

D. Sur,

W. A. Catterall and W. A. Catterall, From Ionic Currents to Molecular Mechanisms, Neuron, vol.26, issue.1, pp.13-25, 2000.

S. Lolignier, C. Bonnet, C. Gaudioso, J. Noël, J. Ruel et al., The Nav1.9 Channel Is a Key Determinant of Cold Pain Sensation and Cold Allodynia, Cell Reports, vol.11, issue.7, pp.1067-1078, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01208540

E. Leipold, L. Liebmann, G. C. Korenke, T. Heinrich, S. Gießelmann et al., A de novo gain-of-function mutation in SCN11A causes loss of pain perception, Nature Genetics, vol.45, issue.11, pp.1399-1404, 2013.

T. R. Cummins and S. G. Waxman, Downregulation of Tetrodotoxin-Resistant Sodium Currents and Upregulation of a Rapidly Repriming Tetrodotoxin-Sensitive Sodium Current in Small Spinal Sensory Neurons after Nerve Injury, The Journal of Neuroscience, vol.17, issue.10, pp.3503-3514, 1997.

F. Zhang, X. Xu, T. Li, and Z. Liu, Shellfish Toxins Targeting Voltage-Gated Sodium Channels, Marine Drugs, vol.11, issue.12, pp.4698-4723, 2013.

S. Y. Er, Biotechnological applications of spider venom peptides, Spider-Venom Peptides as Therapeutics

D. Sur,

N. Weiss and M. D. Waard, Les canaux calciques dépendants du voltage au c?ur de la douleur, médecine/sciences, vol.22, issue.4, pp.396-404, 2006.

J. Nargeot and P. Charnet, Diversité moléculaire des canaux calciques : du gène à la fonction, médecine/sciences, vol.10, issue.12, p.1293, 1994.

S. Hatakeyama, M. Wakamori, M. Ino, N. Miyamoto, E. Takahashi et al., Differential nociceptive responses in mice lacking the ?1B subunit of N-type Ca2+ channels, Neuroreport, vol.12, issue.11, pp.2423-2427, 2001.

J. Busseroles and J. Noël, La douleur sous le contrôle des canaux potassiques, Douleur et Analgésie, vol.29, issue.4, pp.204-211, 2016.

C. J. Bohlen, A. T. Chesler, R. Sharif-naeini, K. F. Medzihradszky, S. Zhou et al., A heteromeric Texas coral snake toxin targets acid-sensing ion channels to produce pain, Nature, vol.479, issue.7373, pp.410-414, 2011.

D. Sur,

G. Mourier, M. Salinas, P. Kessler, E. A. Stura, M. Leblanc et al., Mambalgin-1 Pain-relieving Peptide, Stepwise Solid-phase Synthesis, Crystal Structure, and Functional Domain for Acid-sensing Ion Channel 1a Inhibition, Journal of Biological Chemistry, vol.291, issue.6, pp.2616-2629, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02267121

H. Lan, K. Wu, Y. Zheng, M. Pan, Y. Huang et al., Total synthesis of mambalgin-1/2/3 by two-segment hydrazide-based native chemical ligation, Journal of Peptide Science, vol.22, issue.5, pp.320-326, 2016.

M. Salinas, T. Besson, Q. Delettre, S. Diochot, S. Boulakirba et al., Binding Site and Inhibitory Mechanism of the Mambalgin-2 Pain-relieving Peptide on Acid-sensing Ion Channel 1a, Journal of Biological Chemistry, vol.289, issue.19, pp.13363-13373, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02115810

A. Báez, E. Salceda, M. Fló, M. Graña, C. Fernández et al., ?-Dendrotoxin inhibits the ASIC current in dorsal root ganglion neurons from rat, Neuroscience Letters, vol.606, pp.42-47, 2015.

X. Wang, S. Wang, M. Zhang, F. Gao, C. Yin et al., ?-Dendrotoxin-sensitive Kv1 channels contribute to conduction failure of polymodal nociceptive C-fibers from rat coccygeal nerve, Journal of Neurophysiology, vol.115, issue.2, pp.947-957, 2016.

J. K. Klint, J. J. Smith, I. Vetter, D. B. Rupasinghe, S. Y. Er et al., Seven novel modulators of the analgesic target NaV1.7 uncovered using a high-throughput venom-based discovery approach, British Journal of Pharmacology, vol.172, issue.10, pp.2445-2458, 2015.

D. Triggle, Faculty Opinions recommendation of Selective spider toxins reveal a role for the Nav1.1 channel in mechanical pain., 2016.

D. Sur,

N. J. Saez, M. Mobli, M. Bieri, I. R. Chassagnon, A. K. Malde et al., A Dynamic Pharmacophore Drives the Interaction between Psalmotoxin-1 and the Putative Drug Target Acid-Sensing Ion Channel 1a, Molecular Pharmacology, vol.80, issue.5, pp.796-808, 2011.

N. Joeres, K. Augustinowski, A. Neuhof, M. Assmann, and S. Gründer, Functional and pharmacological characterization of two different ASIC1a/2a heteromers reveals their sensitivity to the spider toxin PcTx1, Scientific Reports, vol.6, issue.1, p.27647, 2016.

S. Jami, A. Erickson, S. Brierley, and I. Vetter, Pain-Causing Venom Peptides: Insights into Sensory Neuron Pharmacology, Toxins, vol.10, issue.1, p.15, 2017.

J. S. Wingerd, C. A. Mozar, C. A. Ussing, S. S. Murali, N. Y. Chin et al., The tarantula toxin ?/?-TRTX-Pre1a highlights the importance of the S1-S2 voltage-sensor region for sodium channel subtype selectivity, Scientific Reports, vol.7, issue.1, p.974, 2017.

F. C. Cardoso, Z. Dekan, K. J. Rosengren, A. Erickson, I. Vetter et al., Identification and Characterization of ProTx-III [?-TRTX-Tp1a], a New Voltage-Gated Sodium Channel Inhibitor from Venom of the Tarantula Thrixopelma pruriens, Molecular Pharmacology, vol.88, issue.2, pp.291-303, 2015.

Y. Liu, J. Tang, Y. Zhang, X. Xun, D. Tang et al., Synthesis and Analgesic Effects of ?-TRTX-Hhn1b on Models of Inflammatory and Neuropathic Pain, Toxins, vol.6, issue.8, pp.2363-2378, 2014.

D. Sur, Function and solution structure of huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider

D. Sur,

A. H. Rowe, Y. Xiao, M. P. Rowe, T. R. Cummins, and H. H. Zakon, Voltage-Gated Sodium Channel in Grasshopper Mice Defends Against Bark Scorpion Toxin, Science, vol.342, issue.6157, pp.441-446, 2013.

Y. Xu, X. Meng, X. Hou, J. Sun, X. Kong et al., A mutant of theButhus martensiiKarsch antitumor-analgesic peptide exhibits reduced inhibition to hNav1.4 and hNav1.5 channels while retaining analgesic activity, Journal of Biological Chemistry, vol.292, issue.44, pp.18270-18280, 2017.

P. S. Staats, T. Yearwood, S. G. Charapata, R. W. Presley, M. S. Wallace et al., Intrathecal Ziconotide in the Treatment of Refractory Pain in Patients With Cancer or AIDS, JAMA, vol.291, issue.1, p.63, 2004.

, Bréve : Disponible sur internet: lait humain? avec bactéries!, Option/Bio, vol.24, issue.498, p.4, 2013.

R. Ma, R. Mahadevappa, and H. F. Kwok, Venom-based peptide therapy: insights into anti-cancer mechanism, Oncotarget, vol.8, issue.59, pp.100908-100930, 2017.

Y. S. Bakhle and R. J. Flower, Sergio Henrique Ferreira (1934-2016), British Journal of Pharmacology, vol.174, issue.4, pp.341-342, 2017.

B. A. Murray and R. J. Fitzgerald, Angiotensin Converting Enzyme Inhibitory Peptides Derived from Food Proteins: Biochemistry, Bioactivity and Production, Current Pharmaceutical Design, vol.13, issue.8, pp.773-791, 2007.

, De la biologie des systèmes et de la génomique vers la santé et la médecine personnalisées, Annales de biologie clinique, vol.69, issue.2, pp.200-201, 2011.

D. Boeck and S. , L'advertissement et responce des estats de Haynault sur la requeste faicte pour la liberte? de la Religion, et l'exercise d'icelle (18 Juill.)

. Diabète,

D. Sur, ROA Fact Sheets, 2012, 2012.

. Netgen, Analogues du GLP-1 versus inhibiteurs du SGLT-2 pour les diabétiques de type 2 obèses

. Revue-médicale-suisse, Liste type de tableaux du CAD sur la Suisse, Examens de l'OCDE sur la coopération pour le développement : Suisse 2019, pp.105-112, 2019.

J. Lacherade, Les conséquences de l?hypoglycémie, Réanimation, vol.17, issue.5, pp.437-441, 2008.

R. K. Finol?urdaneta, M. S. Remedi, W. Raasch, S. Becker, R. B. Clark et al., Block of K v 1.7 potassium currents increases glucose?stimulated insulin secretion, EMBO Molecular Medicine, vol.4, issue.5, pp.424-434, 2012.

J. G. Menting, J. Gajewiak, C. A. Macraild, D. Chou, M. M. Disotuar et al., A minimized human insulin-receptor-binding motif revealed in a Conus geographus venom insulin, Nature Structural & Molecular Biology, vol.23, issue.10, pp.916-920, 2016.

D. Sur, ROA Fact Sheets, 2012, 2012.

J. Risset, Ce que c?est qu?un endroit de la Terre, Le Genre humain, vol.N?47, issue.1, p.33, 2008.

D. Sur,

C. R. Rubincam and P. Goukowsky, Essai sur les origines du mythe d'Alexandre. Tome 1: Les origines politiques, Phoenix, vol.35, issue.2, p.168, 1981.

T. Görögh, L. Bèress, E. S. Quabius, P. Ambrosch, and M. Hoffmann, Head and neck cancer cells and xenografts are very sensitive to palytoxin: decrease of c-jun n-terminale kinase-3 expression enhances palytoxin toxicity, Molecular Cancer, vol.12, issue.1, p.12, 2013.

T. Calon, S. Sinno-tellier, L. De-haro, and J. Bloch, Exposition à la palytoxine des personnes manipulant des coraux mous d?aquarium d?eau de mer : étude des cas rapportés au réseau des Centres antipoison de 2000 à 2017, Toxicologie Analytique et Clinique, vol.31, issue.1, pp.64-76, 2019.

W. P. Schilling, D. Snyder, W. G. Sinkins, and M. Estacion, Palytoxin-induced cell death cascade in bovine aortic endothelial cells, American Journal of Physiology-Cell Physiology, vol.291, issue.4, pp.C657-C667, 2006.

B. Li, P. Lyu, X. Xi, L. Ge, R. Mahadevappa et al., Triggering of cancer cell cycle arrest by a novel scorpion venom?derived peptide?Gonearrestide, Journal of Cellular and Molecular Medicine, vol.22, issue.9, pp.4460-4473, 2018.

S. D. Gupta, A. Gomes, A. Debnath, A. Saha, and A. Gomes, Apoptosis induction in human leukemic cells by a novel protein Bengalin, isolated from Indian black scorpion venom: Through mitochondrial pathway and inhibition of heat shock proteins, Chemico-Biological Interactions, vol.183, issue.2, pp.293-303, 2010.

C. Wang, T. Chen, N. Zhang, M. Yang, B. Li et al., Melittin, a Major Component of Bee Venom, Sensitizes Human Hepatocellular Carcinoma Cells to Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL)-induced Apoptosis by Activating CaMKII-TAK1-JNK/p38 and Inhibiting I?B? Kinase-NF?B, Journal of Biological Chemistry, vol.284, issue.6, pp.3804-3813, 2008.

G. Cohen, S. Burks, and J. Frank, Chlorotoxin?A Multimodal Imaging Platform for Targeting Glioma Tumors, Toxins, vol.10, issue.12, p.496, 2018.

N. Graf, T. E. Mokhtari, I. A. Papayannopoulos, and S. J. Lippard, Platinum(IV)-chlorotoxin (CTX) conjugates for targeting cancer cells, Journal of Inorganic Biochemistry, vol.110, pp.58-63, 2012.

L. , Addresse |dn[!] lord maire, &de la lieutenance de Londres. Presentée le vendredy 30. juill. V.S. (9. août N.S.) 1715

D. Sur, LAS VEGAS SANDS CORP., a Nevada corporation, Plaintiff, v. UKNOWN REGISTRANTS OF www.wn0000.com, www.wn1111.com, www.wn2222.com, www.wn3333.com, www.wn4444.com, www.wn5555.com, www.wn6666.com, www.wn7777.com, www.wn8888.com, www.wn9999.com, www.112211.com, www.4456888.com, www.4489888.com, www.001148.com, and www.2289888.com, Defendants., Gaming Law Review and Economics, vol.20, issue.10, pp.859-868, 2016.