Discovery, Synthesis, and Structure–Activity Relationships of Conotoxins

Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide

Merrifield, R. B. (1963) · Journal of the American Chemical Society · doi:10.1021/ja00897a025 · Cited by 7,647

Principles that Govern the Folding of Protein Chains

Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096

Protein folding and misfolding

Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791

Synthesis of Proteins by Native Chemical Ligation

Dawson, P. E., Muir, T. W., Clark-Lewis, I., & Kent, S. B. H. (1994) · Science · doi:10.1126/science.7973629 · Cited by 4,131

Protein folding in the cell

Gething, M.-J., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,123

Molecular chaperones in cellular protein folding

Hartl, F. U. (1996) · Nature · doi:10.1038/381571a0 · Cited by 3,568

Solid phase peptide synthesis utilizing 9‐fluorenylmethoxycarbonyl amino acids

FIELDS, G. B., & NOBLE, R. L. (1990) · International Journal of Peptide and Protein Research · doi:10.1111/j.1399-3011.1990.tb00939.x · Cited by 2,493

Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors

Brejc, K., van Dijk, W. J., Klaassen, R. V., Schuurmans, M., van der Oost, J., Smit, A. B., & Sixma, T. K. (2001) · Nature · doi:10.1038/35077011 · Cited by 1,759

Refined Structure of the Nicotinic Acetylcholine Receptor at 4Å Resolution

Unwin, N. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.031 · Cited by 1,659

Nicotine addiction

Benowitz, N. L. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0809890 · Cited by 1,508

Synthetic therapeutic peptides: science and market

Vlieghe, P., Lisowski, V., Martinez, J., & Khrestchatisky, M. (2010) · Drug Discovery Today · doi:10.1016/j.drudis.2009.10.009 · Cited by 1,476

Structure and gating mechanism of the acetylcholine receptor pore

Miyazawa, A., Fujiyoshi, Y., & Unwin, N. (2003) · Nature · doi:10.1038/nature01748 · Cited by 1,270

In situ neutralization in Boc‐chemistry solid phase peptide synthesis: Rapid, high yield assembly of difficult sequences

SCHNölzer, M., ALEWOOD, P., JONES, A., ALEWOOD, D., & KENT, S. B. H. (1992) · International Journal of Peptide and Protein Research · doi:10.1111/j.1399-3011.1992.tb00291.x · Cited by 1,049

Total chemical synthesis of proteins

Kent, S. B. H. (2009) · Chem. Soc. Rev. · doi:10.1039/b700141j · Cited by 922

Conus Venoms: A Rich Source of Novel Ion Channel-Targeted Peptides

TERLAU, H., & OLIVERA, B. M. (2004) · Physiological Reviews · doi:10.1152/physrev.00020.2003 · Cited by 897

Amino Acid-Protecting Groups

Isidro-Llobet, A., Álvarez, M., & Albericio, F. (2009) · Chemical Reviews · doi:10.1021/cr800323s · Cited by 850

SELENOCYSTEINE

Stadtman, T. C. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.000503 · Cited by 829

Nicotinic Receptors at the Amino Acid Level

Corringer, P.-J., Novère, N. L., & Changeux, J.-P. (2000) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.40.1.431 · Cited by 820

CALCIUM CHANNEL DIVERSITY AND NEUROTRANSMITTER RELEASE: The ω-Conotoxins and ω-Agatoxins

Olivera, B. M., Miljanich, G. P., Ramachandran, J., & Adams, M. E. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.004135 · Cited by 734

Selenocysteine: the 21st amino acid

Böck, A., Forchhammer, K., Heider, J., Leinfelder, W., Sawers, G., Veprek, B., & Zinoni, F. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb00722.x · Cited by 686

X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation

Bocquet, N., Nury, H., Baaden, M., Le Poupon, C., Changeux, J.-P., Delarue, M., & Corringer, P.-J. (2009) · Nature · doi:10.1038/nature07462 · Cited by 674

X-ray structure of a prokaryotic pentameric ligand-gated ion channel

Hilf, R. J. C., & Dutzler, R. (2008) · Nature · doi:10.1038/nature06717 · Cited by 665

Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations

Hansen, S. B., Sulzenbacher, G., Huxford, T., Marchot, P., Taylor, P., & Bourne, Y. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600828 · Cited by 641

PATAI'S Chemistry of Functional Groups

(2010) · Patai's chemistry of functional groups · doi:10.1002/series1078 · Cited by 621

Ziconotide: Neuronal Calcium Channel Blocker for Treating Severe Chronic Pain

Miljanich, G. P. (2004) · Current Medicinal Chemistry · doi:10.2174/0929867043363884 · Cited by 607

A glia-derived acetylcholine-binding protein that modulates synaptic transmission

Smit, A. B., Syed, N. I., Schaap, D., van Minnen, J., Klumperman, J., Kits, K. S., Lodder, H., van der Schors, R. C., van Elk, R., Sorgedrager, B., et al. (2001) · Nature · doi:10.1038/35077000 · Cited by 563

Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

Zhong, L., Arnér, E. S. J., & Holmgren, A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100114897 · Cited by 527

Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel

Hilf, R. J. C., & Dutzler, R. (2009) · Nature · doi:10.1038/nature07461 · Cited by 526

Methods and Protocols of Modern Solid Phase Peptide Synthesis

Amblard, M., Fehrentz, J.-A., Martinez, J., & Subra, G. (2006) · Molecular Biotechnology · doi:10.1385/mb:33:3:239 · Cited by 497

A New α-Conotoxin Which Targets α3β2 Nicotinic Acetylcholine Receptors

Cartier, G. E., Yoshikami, D., Gray, W. R., Luo, S., Olivera, B. M., & McIntosh, J. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.13.7522 · Cited by 489

Crystal structure of a voltage-gated sodium channel in two potentially inactivated states

Payandeh, J., Gamal El-Din, T. M., Scheuer, T., Zheng, N., & Catterall, W. A. (2012) · Nature · doi:10.1038/nature11077 · Cited by 483

Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel

Zhang, X., Ren, W., DeCaen, P., Yan, C., Tao, X., Tang, L., Wang, J., Hasegawa, K., Kumasaka, T., He, J., et al. (2012) · Nature · doi:10.1038/nature11054 · Cited by 466

Aphid Thermal Tolerance Is Governed by a Point Mutation in Bacterial Symbionts

Dunbar, H. E., Wilson, A. C. C., Ferguson, N. R., & Moran, N. A. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050096 · Cited by 458

Nucleophilic reactivity constants toward methyl iodide and trans-dichlorodi(pyridine)platinum(II)

Pearson, R. G., Sobel, H. R., & Songstad, J. (1968) · Journal of the American Chemical Society · doi:10.1021/ja01004a021 · Cited by 455

Conus Venom Peptide Pharmacology

Lewis, R. J., Dutertre, S., Vetter, I., & Christie, M. J. (2012) · Pharmacological Reviews · doi:10.1124/pr.111.005322 · Cited by 424

Purification and sequence of a presynaptic peptide toxin from Conus geographus venom

Olivera, B. M., McIntosh, J. M., Curz, L. J., Luque, F. A., & Gray, W. R. (1984) · Biochemistry · doi:10.1021/bi00317a001 · Cited by 419

The structural aspects of limited proteolysis of native proteins

Hubbard, S. J. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(97)00175-1 · Cited by 406

Conus geographus toxins that discriminate between neuronal and muscle sodium channels.

Cruz, L. J., Gray, W. R., Olivera, B. M., Zeikus, R. D., Kerr, L., Yoshikami, D., & Moczydlowski, E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39364-x · Cited by 399

Selenocysteine in proteins—properties and biotechnological use

Johansson, L., Gafvelin, G., & Arnér, E. S. J. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.05.010 · Cited by 352

Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analogs

Huber, R. E., & Criddle, R. S. (1967) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(67)90136-1 · Cited by 342

Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene ( Trsp )

Bösl, M. R., Takaku, K., Oshima, M., Nishimura, S., & Taketo, M. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.11.5531 · Cited by 337

Molecular genetics of ecological diversification: Duplication and rapid evolution of toxin genes of the venomous gastropod Conus

Duda, T. F., & Palumbi, S. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6820 · Cited by 328

The Engineering of an Orally Active Conotoxin for the Treatment of Neuropathic Pain

Clark, R. J., Jensen, J., Nevin, S. T., Callaghan, B. P., Adams, D. J., & Craik, D. J. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201000620 · Cited by 313

Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an α-conotoxin PnIA variant

Celie, P. H. N., Kasheverov, I. E., Mordvintsev, D. Y., Hogg, R. C., van Nierop, P., van Elk, R., van Rossum-Fikkert, S. E., Zhmak, M. N., Bertrand, D., Tsetlin, V., et al. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb951 · Cited by 310

Conus Peptides: Biodiversity-based Discovery and Exogenomics

Olivera, B. M. (2006) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84029-2 · Cited by 302

Biosynthesis of Selenocysteine on Its tRNA in Eukaryotes

Xu, X.-M., Carlson, B. A., Mix, H., Zhang, Y., Saira, K., Glass, R. S., Berry, M. J., Gladyshev, V. N., & Hatfield, D. L. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0050004 · Cited by 299

Conus Peptides Targeted to Specific Nicotinic Acetylcholine Receptor Subtypes

McIntosh, J. M., Santos, A. D., & Olivera, B. M. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.59 · Cited by 295

Selenocysteine in Native Chemical Ligation and Expressed Protein Ligation

Hondal, R. J., Nilsson, B. L., & Raines, R. T. (2001) · Journal of the American Chemical Society · doi:10.1021/ja005885t · Cited by 278

Mixture-Based Synthetic Combinatorial Libraries

Houghten, R. A., Pinilla, C., Appel, J. R., Blondelle, S. E., Dooley, C. T., Eichler, J., Nefzi, A., & Ostresh, J. M. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm990174v · Cited by 256

Conotoxins and the posttranslational modification of secreted gene products

Buczek, O., Bulaj, G., & Olivera, B. M. (2005) · Cellular and Molecular Life Sciences CMLS · doi:10.1007/s00018-005-5283-0 · Cited by 247

Engineering stable peptide toxins by means of backbone cyclization: Stabilization of the α-conotoxin MII

Clark, R. J., Fischer, H., Dempster, L., Daly, N. L., Rosengren, K. J., Nevin, S. T., Meunier, F. A., Adams, D. J., & Craik, D. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504613102 · Cited by 234

Molecular mechanism for analgesia involving specific antagonism of α9α10 nicotinic acetylcholine receptors

Vincler, M., Wittenauer, S., Parker, R., Ellison, M., Olivera, B. M., & McIntosh, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608715103 · Cited by 227

Two new classes of conopeptides inhibit the α1-adrenoceptor and noradrenaline transporter

Sharpe, I. A., Gehrmann, J., Loughnan, M. L., Thomas, L., Adams, D. A., Atkins, A., Palant, E., Craik, D. J., Adams, D. J., Alewood, P. F., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-902 · Cited by 220

Invertebrate vasopressin/oxytocin homologs. Characterization of peptides from Conus geographus and Conus straitus venoms.

Cruz, L. J., de Santos, V, Zafaralla, G. C., Ramilo, C. A., Zeikus, R., Gray, W. R., & Olivera, B. M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47661-2 · Cited by 219

Deep Venomics Reveals the Mechanism for Expanded Peptide Diversity in Cone Snail Venom

Dutertre, S., Jin, A., Kaas, Q., Jones, A., Alewood, P. F., & Lewis, R. J. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.021469 · Cited by 216

Mechanisms for Evolving Hypervariability: The Case of Conopeptides

Conticello, S. G., Gilad, Y., Avidan, N., Ben-Asher, E., Levy, Z., & Fainzilber, M. (2001) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a003786 · Cited by 213

Gamma-carboxyglutamate in a neuroactive toxin.

McIntosh, J. M., Olivera, B. M., Cruz, L. J., & Gray, W. R. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42601-9 · Cited by 201

Conus Venom Peptides: Reflections from the Biology of Clades and Species

Olivera, B. M. (2002) · Annual Review of Ecology and Systematics · doi:10.1146/annurev.ecolsys.33.010802.150424 · Cited by 199

Contulakin-G, an O-Glycosylated Invertebrate Neurotensin

Craig, A. G., Norberg, T., Griffin, D., Hoeger, C., Akhtar, M., Schmidt, K., Low, W., Dykert, J., Richelson, E., Navarro, V., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.13752 · Cited by 196

Structural determinants of selective α-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP

Ulens, C., Hogg, R. C., Celie, P. H., Bertrand, D., Tsetlin, V., Smit, A. B., & Sixma, T. K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507889103 · Cited by 193

Analogs of α-Conotoxin MII Are Selective for α6-Containing Nicotinic Acetylcholine Receptors

McIntosh, J. M., Azam, L., Staheli, S., Dowell, C., Lindstrom, J. M., Kuryatov, A., Garrett, J. E., Marks, M. J., & Whiteaker, P. (2004) · Molecular Pharmacology · doi:10.1124/mol.65.4.944 · Cited by 193

α6β2* and α4β2* Nicotinic Acetylcholine Receptors As Drug Targets for Parkinson’s Disease

Quik, M., & Wonnacott, S. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.003269 · Cited by 192

A nicotinic acetylcholine receptor ligand of unique specificity, alpha-conotoxin ImI

McIntosh, J. M., Yoshikami, D., Mahe, E., Nielsen, D. B., Rivier, J. E., Gray, W. R., & Olivera, B. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89452-8 · Cited by 186

α-Selenoconotoxins, a New Class of Potent α7 Neuronal Nicotinic Receptor Antagonists

Armishaw, C. J., Daly, N. L., Nevin, S. T., Adams, D. J., Craik, D. J., & Alewood, P. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512419200 · Cited by 184

The Formation of Diselenide Bridges in Proteins by Incorporation of Selenocysteine Residues: Biosynthesis and Characterization of (Se)2-Thioredoxin

Mueller, S., Senn, H., Gsell, B., Vetter, W., Baron, C., & Boeck, A. (1994) · Biochemistry · doi:10.1021/bi00177a034 · Cited by 175

Remarkable inter- and intra-species complexity of conotoxins revealed by LC/MS

Davis, J., Jones, A., & Lewis, R. J. (2009) · Peptides · doi:10.1016/j.peptides.2009.03.019 · Cited by 173

α-RgIA: A Novel Conotoxin That Specifically and Potently Blocks the α9α10 nAChR,

Ellison, M., Haberlandt, C., Gomez-Casati, M. E., Watkins, M., Elgoyhen, A. B., McIntosh, J. M., & Olivera, B. M. (2006) · Biochemistry · doi:10.1021/bi0520129 · Cited by 171

Folding of small disulfide-rich proteins: clarifying the puzzle

Arolas, J. L., Aviles, F. X., Chang, J.-Y., & Ventura, S. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.03.005 · Cited by 170

Use of Venom Peptides to Probe Ion Channel Structure and Function

Dutertre, S., & Lewis, R. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.076596 · Cited by 167

Molecular dissection of subunit interfaces in the acetylcholine receptor: Identification of determinants of α-Conotoxin M1 selectivity

Sines, S. M., Kreienkamp, H.-J., Bren, N., Maeda, R., & Taylor, P. (1995) · Neuron · doi:10.1016/0896-6273(95)90077-2 · Cited by 166

Structure determination of the three disulfide bond isomers of α-conotoxin GI: a model for the role of disulfide bonds in structural stability 1 1Edited by P. E. Wright

Gehrmann, J., Alewood, P. F., & Craik, D. J. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1701 · Cited by 163

Functional genomics of the nicotinic acetylcholine receptor gene family of the nematode, Caenorhabditis elegans

Jones, A. K., & Sattelle, D. B. (2003) · BioEssays · doi:10.1002/bies.10377 · Cited by 161

Extensive and Continuous Duplication Facilitates Rapid Evolution and Diversification of Gene Families

Chang, D., & Duda, T. F. (2012) · Molecular Biology and Evolution · doi:10.1093/molbev/mss068 · Cited by 158

AChBP‐targeted α‐conotoxin correlates distinct binding orientations with nAChR subtype selectivity

Dutertre, S., Ulens, C., Büttner, R., Fish, A., van Elk, R., Kendel, Y., Hopping, G., Alewood, P. F., Schroeder, C. I., Nicke, A., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601785 · Cited by 158

Speciation of Cone Snails and Interspecific Hyperdivergence of Their Venom Peptides: Potential Evolutionary Significance of Intronsa

Olivera, B. M., Walker, C. S., Cartier, G. E., Hooper, D. K., SANTOS, A. D., Schoenfeld, R. A., SHETTY, R., Watkins, M., Bandyopadhyay, P. K., & Hillyard, D. R. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb08883.x · Cited by 152

Electrostatics in Protein Binding and Function

Sinha, N., & Smith‐Gill, S. J. (2002) · Current Protein and Peptide Science · doi:10.2174/1389203023380431 · Cited by 151

Selenopeptide chemistry

Muttenthaler, M., & Alewood, P. F. (2008) · Journal of Peptide Science · doi:10.1002/psc.1075 · Cited by 151

Alpha9 nicotinic acetylcholine receptors and the treatment of pain

McIntosh, J. M., Absalom, N. L., Chebib, M., Elgoyhen, A. B., & Vincler, M. A. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.05.020 · Cited by 148

Structural and Ligand Recognition Characteristics of an Acetylcholine-binding Protein from Aplysia californica

Hansen, S. B., Talley, T. T., Radić, Z., & Taylor, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402452200 · Cited by 147

Structure/Function Characterization of μ-Conotoxin KIIIA, an Analgesic, Nearly Irreversible Blocker of Mammalian Neuronal Sodium Channels

Zhang, M.-M., Green, B. R., Catlin, P., Fiedler, B., Azam, L., Chadwick, A. T., Terlau, H., McArthur, J. R., French, R. J., Gulyas, J., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704616200 · Cited by 146

The Redox Potential of Selenocystine in Unconstrained Cyclic Peptides

Besse, D., Siedler, F., Diercks, T., et al. (1997) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199708831 · Cited by 144

μ-Conotoxin PIIIA, a New Peptide for Discriminating among Tetrodotoxin-Sensitive Na Channel Subtypes

Shon, K.-J., Olivera, B. M., Watkins, M., Jacobsen, R. B., Gray, W. R., Floresca, C. Z., Cruz, L. J., Hillyard, D. R., Brink, A., Terlau, H., et al. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-12-04473.1998 · Cited by 143

Selenoether oxytocin analogues have analgesic properties in a mouse model of chronic abdominal pain

de Araujo, A. D., Mobli, M., Castro, J., Harrington, A. M., Vetter, I., Dekan, Z., Muttenthaler, M., Wan, J., Lewis, R. J., King, G. F., et al. (2014) · Nature Communications · doi:10.1038/ncomms4165 · Cited by 142

Conotoxins: natural product drug leads

Halai, R., & Craik, D. J. (2009) · Natural Product Reports · doi:10.1039/b819311h · Cited by 142

KNOTTIN: the knottin or inhibitor cystine knot scaffold in 2007

Gracy, J., Le‐Nguyen, D., Gelly, J., Kaas, Q., Heitz, A., & Chiche, L. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm939 · Cited by 141

Modulating Oxytocin Activity and Plasma Stability by Disulfide Bond Engineering

Muttenthaler, M., Andersson, Å., de Araujo, A. D., Dekan, Z., Lewis, R. J., & Alewood, P. F. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100989w · Cited by 140

Oxidative folding of cystine‐rich peptides vs regioselective cysteine pairing strategies

Moroder, L., Besse, D., Musiol, H., Rudolph‐Böhner, S., & Siedler, F. (1996) · Biopolymers · Cited by 136

Kinetics and equilibria of thiol/disulfide interchange reactions of selected biological thiols and related molecules with oxidized glutathione

Keire, D. A., Strauss, E. J., Guo, W., Noszál, B., & Rabenstein, D. L. (1992) · The Journal of Organic Chemistry · doi:10.1021/jo00027a023 · Cited by 134

Characterization of the Conus bullatus genome and its venom-duct transcriptome

Hu, H., Bandyopadhyay, P. K., Olivera, B. M., & Yandell, M. D. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-60 · Cited by 133

The A-superfamily of Conotoxins

Santos, A. D., McIntosh, J. M., Hillyard, D. R., Cruz, L. J., & Olivera, B. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309654200 · Cited by 129

The T-superfamily of Conotoxins

Walker, C. S., Steel, D. J., Jacobsen, R. B., Lirazan, M. B., Cruz, L. J., Hooper, D. K., Shetty, R., DelaCruz, R. C., Nielsen, J. S., Zhou, L., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30664 · Cited by 128

Oxidative refolding chromatography: folding of the scorpion toxin Cn5

Altamirano, M. M., García, C. M., Possani, L. D., & Fersht, A. R. (1999) · Nature Biotechnology · doi:10.1038/6192 · Cited by 121

Solving the alpha-conotoxin folding problem: efficient selenium-directed on-resin generation of more potent and stable nicotinic acetylcholine receptor antagonists.

Muttenthaler, M., Nevin, S., Grishin, A., Ngo, S., Choy, P., Daly, N., Hu, S.-H., Armishaw, C., Wang, C., Lewis, R., et al. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910602h · Cited by 119

Determinants of Specificity for α-Conotoxin MII on α3β2 Neuronal Nicotinic Receptors

Harvey, S. C., McIntosh, J. M., Cartier, G. E., Maddox, F. N., & Luetje, C. W. (1997) · Molecular Pharmacology · doi:10.1124/mol.51.2.336 · Cited by 116

Novel Conotoxins from Conus striatus and Conus kinoshitai Selectively Block TTX-Resistant Sodium Channels

Bulaj, G. W., West, P. J., Garrett, J. E., Watkins, M., Zhang, M.-M., Norton, R. S., Smith, B. J., Yoshikami, D., & Olivera, B. M. (2005) · Biochemistry · doi:10.1021/bi0473408 · Cited by 116

A New Level of Conotoxin Diversity, a Non-native Disulfide Bond Connectivity in α-Conotoxin AuIB Reduces Structural Definition but Increases Biological Activity

Dutton, J. L., Bansal, P. S., Hogg, R. C., Adams, D. J., Alewood, P. F., & Craik, D. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208842200 · Cited by 114

Evolutionary Diversification of Multigene Families: Allelic Selection of Toxins in Predatory Cone Snails

Duda, T. F., & Palumbi, S. R. (2000) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a026412 · Cited by 113

Therapeutic Potential of Cone Snail Venom Peptides (Conopeptides)

Vetter, I., & Lewis, R. J. (2012) · Current Topics in Medicinal Chemistry · doi:10.2174/156802612802652457 · Cited by 113

Single-Residue Alteration in α-Conotoxin PnIA Switches Its nAChR Subtype Selectivity

Luo, S., Nguyen, T. A., Cartier, G. E., Olivera, B. M., Yoshikami, D., & McIntosh, J. M. (1999) · Biochemistry · doi:10.1021/bi991252j · Cited by 112

IUPHAR-DB: updated database content and new features

Sharman, J. L., Benson, H. E., Pawson, A. J., Lukito, V., Mpamhanga, C. P., Bombail, V., Davenport, A. P., Peters, J. A., Spedding, M., Harmar, A. J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks960 · Cited by 112

Accelerated chemical synthesis of peptides and small proteins

Miranda, L. P., & Alewood, P. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1181 · Cited by 111

α‐Conotoxins as tools for the elucidation of structure and function of neuronal nicotinic acetylcholine receptor subtypes

Nicke, A., Wonnacott, S., & Lewis, R. J. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04145.x · Cited by 109

α-RgIA, a Novel Conotoxin That Blocks the α9α10 nAChR: Structure and Identification of Key Receptor-Binding Residues

Ellison, M., Feng, Z., Park, A. J., Zhang, X., Olivera, B. M., McIntosh, J. M., & Norton, R. S. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.082 · Cited by 107

Chronic Nicotine Differentially Regulates α6- and β3-Containing Nicotinic Cholinergic Receptors in Rat Brain

Perry, D. C., Mao, D., Gold, A. B., McIntosh, J. M., Pezzullo, J. C., & Kellar, K. J. (2007) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.121228 · Cited by 106

New Mollusk-Specific .alpha.-Conotoxins Block Aplysia Neuronal Acetylcholine Receptors

Fainzilber, M., Hasson, A., Oren, R., Burlingame, A. L., Gordon, D., Spira, M. E., & Zlotkin, E. (1994) · Biochemistry · doi:10.1021/bi00198a018 · Cited by 106

Catalysis of Electron Transfer by Selenocysteine

Nauser, T., Dockheer, S. M., Kissner, R., & Koppenol, W. H. (2006) · Biochemistry · doi:10.1021/bi0602260 · Cited by 105

Nuclear magnetic resonance studies of the solution chemistry of metal complexes. 23. Complexation of methylmercury by selenohydryl-containing amino acids and related molecules

Arnold, A. P., Tan, K. S., & Rabenstein, D. L. (1986) · Inorganic Chemistry · doi:10.1021/ic00234a030 · Cited by 105

Cyclic MrIA: A Stable and Potent Cyclic Conotoxin with a Novel Topological Fold that Targets the Norepinephrine Transporter

Lovelace, E. S., Armishaw, C. J., Colgrave, M. L., Wahlstrom, M. E., Alewood, P. F., Daly, N. L., & Craik, D. J. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060299h · Cited by 100

Folding of Conotoxins: Formation of the Native Disulfide Bridges During Chemical Synthesis and Biosynthesis of Conus Peptides

Bulaj, G. W., & Olivera, B. M. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1856 · Cited by 98

Elucidation of the molecular envenomation strategy of the cone snail Conus geographus through transcriptome sequencing of its venom duct

Hu, H., Bandyopadhyay, P. K., Olivera, B. M., & Yandell, M. D. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-284 · Cited by 97

PISCIVOROUS GASTROPODS OF THE GENUS CONUS

Kohn, A. J. (1956) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.42.3.168 · Cited by 94

Polypeptide Chains Containing d -γ-Hydroxyvaline

Pisarewicz, K., Mora, D., Pflueger, F. C., Fields, G. B., & Marí, F. (2005) · Journal of the American Chemical Society · doi:10.1021/ja050088m · Cited by 94

Mechanisms of conotoxin inhibition of N-type (Cav2.2) calcium channels

Adams, D. J., & Berecki, G. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.01.019 · Cited by 94

Safety and efficacy of intrathecal ziconotide in the management of severe chronic pain

Smith, H. H. (2009) · Therapeutics and Clinical Risk Management · doi:10.2147/tcrm.s4438 · Cited by 93

Molecular basis for the differential sensitivity of rat and human α9α10 nAChRs to α‐conotoxin RgIA

Azam, L., & McIntosh, J. M. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07867.x · Cited by 91

Diversity and evolution of conotoxins based on gene expression profiling of Conus litteratus

Pi, C., Liu, J., Peng, C., Liu, Y., Jiang, X., Zhao, Y., Tang, S., Wang, L., Dong, M., Chen, S., et al. (2006) · Genomics · doi:10.1016/j.ygeno.2006.06.014 · Cited by 89

χ-Conopeptide Pharmacophore Development: Toward a Novel Class of Norepinephrine Transporter Inhibitor (Xen2174) for Pain

Brust, A., Palant, E., Croker, D. E., Colless, B., Drinkwater, R. D., Patterson, B., Schroeder, C. I., Wilson, D. T. R., Nielsen, C. K., Smith, M. T., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9003413 · Cited by 87

Predominant Interactions between μ-Conotoxin Arg-13 and the Skeletal Muscle Na+Channel Localized by Mutant Cycle Analysis

Chang, N. S., French, R. J., Lipkind, G. M., Fozzard, H. A., & Dudley, S. C. (1998) · Biochemistry · doi:10.1021/bi9724927 · Cited by 87

High-resolution picture of a venom gland transcriptome: Case study with the marine snail Conus consors

Terrat, Y., Biass, D., Dutertre, S., Favreau, P., Remm, M., Stöcklin, R., Piquemal, D., & Ducancel, F. (2011) · Toxicon · doi:10.1016/j.toxicon.2011.10.001 · Cited by 86

Structures of μO-conotoxins from Conus marmoreus

Daly, N. L., Ekberg, J. A. K., Thomas, L., Adams, D. J., Lewis, R. J., & Craik, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313002200 · Cited by 84

Conopressin-T from Conus tulipa Reveals an Antagonist Switch in Vasopressin-like Peptides

Dutertre, S., Croker, D. E., Daly, N. L., Andersson, Å., Muttenthaler, M., Lumsden, N. G., Craik, D. J., Alewood, P. F., Guillon, G., & Lewis, R. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706477200 · Cited by 83

Structure and Activity of (2,8)-Dicarba-(3,12)-cystino α-ImI, an α-Conotoxin Containing a Nonreducible Cystine Analogue

MacRaild, C. A., Illesinghe, J., van Lierop, B. J., Townsend, A. L., Chebib, M., Livett, B. G., Robinson, A. J., & Norton, R. S. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm8011504 · Cited by 82

Efficient oxidative folding of conotoxins and the radiation of venomous cone snails

Bulaj, G. W., Buczek, O., Goodsell, I., Jimenéz, E. C., Kranski, J., Nielsen, J. S., Garrett, J. E., & Olivera, B. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2335845100 · Cited by 81

Structure and Sodium Channel Activity of an Excitatory I1-Superfamily Conotoxin,

Buczek, O., Wei, D., Babon, J. J., Yang, X., Fiedler, B., Chen, P., Yoshikami, D., Olivera, B. M., Bulaj, G. W., & Norton, R. S. (2007) · Biochemistry · doi:10.1021/bi700797f · Cited by 80

Blockade of Neuronal α7-nAChR by α-Conotoxin ImI Explained by Computational Scanning and Energy Calculations

Yu, R., Craik, D. J., & Kaas, Q. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002011 · Cited by 80

The contryphans, a d ‐trvptophan‐containing family of Conus peptides: interconversion between conformers

Jacobsen, R. B., Jimenéz, E. C., Grilley, M. M., Watkins, M., Hillyard, D. R., Cruz, L. J., & Olivera, B. M. (1998) · Journal of Peptide Research · doi:10.1111/j.1399-3011.1998.tb01213.x · Cited by 80

Transcriptomic Messiness in the Venom Duct of Conus miles Contributes to Conotoxin Diversity

Jin, A., Dutertre, S., Kaas, Q., Lavergne, V., Kubala, P., Lewis, R. J., & Alewood, P. F. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030353 · Cited by 80

Regulatory Role of the ?7nAChR in Cancer

Schuller, H. M. (2012) · Current Drug Targets · doi:10.2174/138945012800398883 · Cited by 79

Hydroxyl group of Tyr13 is essential for the activity of omega-conotoxin GVIA, a peptide toxin for N-type calcium channel.

Kim, J. I., Takahashi, M., Ogura, A., Kohno, T., Kudo, Y., & Sato, K. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51019-5 · Cited by 78

Structure of the Analgesic μ-Conotoxin KIIIA and Effects on the Structure and Function of Disulfide Deletion

Khoo, K. K., Feng, Z., Smith, B. J., Zhang, M., Yoshikami, D., Olivera, B. M., Bulaj, G. W., & Norton, R. S. (2009) · Biochemistry · doi:10.1021/bi801998a · Cited by 76

μ-Conotoxin SmIIIA, a Potent Inhibitor of Tetrodotoxin-Resistant Sodium Channels in Amphibian Sympathetic and Sensory Neurons

West, P. J., Bulaj, G. W., Garrett, J. E., et al. (2002) · Biochemistry · doi:10.1021/bi0265628 · Cited by 76

Cyclization of conotoxins to improve their biopharmaceutical properties

Clark, R. J., Akcan, M., Kaas, Q., Daly, N. L., & Craik, D. J. (2010) · Toxicon · doi:10.1016/j.toxicon.2010.12.003 · Cited by 74

Pairwise Interactions between Neuronal α7Acetylcholine Receptors and α-Conotoxin PnIB

Quiram, P. A., McIntosh, J. M., & Sine, S. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.7.4889 · Cited by 73

The First γ-Carboxyglutamic Acid-containing Contryphan

Hansson, K., Ma, X., Eliasson, L., Czerwiec, E., Furie, B., Furie, B. C., Rorsman, P., & Stenflo, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313825200 · Cited by 73

A Novel Conus Snail Polypeptide Causes Excitotoxicity by Blocking Desensitization of AMPA Receptors

Walker, C. S., Jensen, S., Ellison, M., Matta, J. A., Lee, W. Y., Imperial, J. S., Duclos, N., Brockie, P. J., Madsen, D. M., Isaac, J. T. R., et al. (2009) · Current Biology · doi:10.1016/j.cub.2009.05.017 · Cited by 73

Proteomic Analysis Provides Insights on Venom Processing in Conus textile

Tayo, L. L., Lu, B., Cruz, L. J., & Yates, J. R. (2010) · Journal of Proteome Research · doi:10.1021/pr901032r · Cited by 72

Single Amino Acid Substitutions in α-Conotoxin PnIA Shift Selectivity for Subtypes of the Mammalian Neuronal Nicotinic Acetylcholine Receptor

Hogg, R. C., Miranda, L. P., Craik, D. J., Lewis, R. J., Alewood, P. F., & Adams, D. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.51.36559 · Cited by 72

α-Conotoxin AuIB Isomers Exhibit Distinct Inhibitory Mechanisms and Differential Sensitivity to Stoichiometry of α3β4 Nicotinic Acetylcholine Receptors

Grishin, A. A., Wang, C.-I. A., Muttenthaler, M., Alewood, P. F., Lewis, R. J., & Adams, D. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.111880 · Cited by 71

A novel µ‐conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors

Favreau, P., Benoit, É., Hocking, H. G., Carlier, L., hoedt, D. D., Leipold, E., Markgraf, R., Schlumberger, S., Córdova, M., Gaertner, H., et al. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.01837.x · Cited by 68

Evolution of Conus peptide toxins: Analysis of Conus californicus Reeve, 1844

Biggs, J. S., Watkins, M., Puillandre, N., Ownby, J.-P., López‐Vera, E., Christensen, S. B., Juárez‐Moreno, K., Bernáldez-Sarabia, J., Licea-Navarro, A. F., Corneli, P. S., et al. (2010) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2010.03.029 · Cited by 68

Pairwise Interactions between Neuronal α7Acetylcholine Receptors and α-Conotoxin ImI

Quiram, P. A., Jones, J. J., & Sine, S. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19517 · Cited by 68

Synthesis of single‐ and multiple‐stranded cystine‐rich peptides

Moroder, L., Musiol, H., Götz, M. G., & Renner, C. (2004) · Biopolymers · doi:10.1002/bip.20174 · Cited by 67

Identification and Functional Expression of a Family of Nicotinic Acetylcholine Receptor Subunits in the Central Nervous System of the Mollusc Lymnaea stagnalis

van Nierop, P., Bertrand, S., Munno, D. W., Gouwenberg, Y., van Minnen, J., Spafford, J. D., Syed, N. I., Bertrand, D., & Smit, A. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508571200 · Cited by 66

Determinants Involved in the Affinity of α-Conotoxins GI and SI for the Muscle Subtype of Nicotinic Acetylcholine Receptors

Groebe, D. R., Gray, W. R., & Abramson, S. N. (1997) · Biochemistry · doi:10.1021/bi970195w · Cited by 65

A new Conus peptide ligand for Ca channel subtypes

Monje, V. D., Haack, J. A., Naisbitt, S. R., Miljanich, G. P., Ramachandran, J., Nasdasdi, L., Olivera, B. M., Hillyard, D. R., & Gray, W. R. (1993) · Neuropharmacology · doi:10.1016/0028-3908(93)90008-q · Cited by 64

Effects of Cyclization on Stability, Structure, and Activity of α-Conotoxin RgIA at the α9α10 Nicotinic Acetylcholine Receptor and GABAB Receptor

Halai, R., Callaghan, B., Daly, N. L., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201060r · Cited by 64

Toxin insights into nicotinic acetylcholine receptors

Dutertre, S., & Lewis, R. J. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.03.027 · Cited by 64

Synthesis, Structure Elucidation, in Vitro Biological Activity, Toxicity, and Caco-2 Cell Permeability of Lipophilic Analogues of α-Conotoxin MII

Blanchfield, J. T., Dutton, J. L., Hogg, R. C., Gallagher, O. P., Craik, D. J., Jones, A., Adams, D. J., Lewis, R. J., Alewood, P. F., & Tóth, I. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm020426j · Cited by 63

β2 Subunit Contribution to 4/7 α-Conotoxin Binding to the Nicotinic Acetylcholine Receptor

Dutertre, S., Nicke, A., & Lewis, R. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504229200 · Cited by 63

Loss of α‐conotoxinMII‐ and A85380‐sensitive nicotinic receptors in Parkinson's disease striatum

Quik, M., Bordia, T., Forno, L. S., & McIntosh, J. M. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02177.x · Cited by 63

Isolation and Structure-Activity of μ-Conotoxin TIIIA, A Potent Inhibitor of Tetrodotoxin-Sensitive Voltage-Gated Sodium Channels

Lewis, R. J., Schroeder, C. I., Ekberg, J. A. K., Nielsen, K. J., Loughnan, M. L., Thomas, L., Adams, D. A., Drinkwater, R. D., Adams, D. J., & Alewood, P. F. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.028225 · Cited by 62

Co‐expression of NaVβ subunits alters the kinetics of inhibition of voltage‐gated sodium channels by pore‐blocking μ‐conotoxins

Zhang, M., Wilson, M. J., Azam, L., Gajewiak, J., Rivier, J., Bulaj, G. W., Olivera, B. M., & Yoshikami, D. (2012) · British Journal of Pharmacology · doi:10.1111/bph.12051 · Cited by 61

Site-Specific Effects of Diselenide Bridges on the Oxidative Folding of a Cystine Knot Peptide, ω-Selenoconotoxin GVIA

Gowd, K. H., Yarotskyy, V., Elmslie, K. S., Skalicky, J. J., Olivera, B. M., & Bulaj, G. W. (2010) · Biochemistry · doi:10.1021/bi902137c · Cited by 61

Chemical Syntheses and Biological Activities of Lactam Analogues of α-Conotoxin SI,,

Hargittai, B., Solé, N. A., Groebe, D. R., Abramson, S. N., & Bárány, G. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm990635c · Cited by 61

Role of Hydroxyprolines in the in Vitro Oxidative Folding and Biological Activity of Conotoxins

López‐Vera, E., Walewska, A., Skalicky, J. J., Olivera, B. M., & Bulaj, G. W. (2008) · Biochemistry · doi:10.1021/bi701934m · Cited by 59

The Effect of Backbone Cyclization on the Thermodynamics of β-Sheet Unfolding: Stability Optimization of the PIN WW Domain

Deechongkit, S., & Kelly, J. W. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0123608 · Cited by 58

Structurally Diverse μ‐Conotoxin PIIIA Isomers Block Sodium Channel Na V 1.4

Tietze, A. A., Tietze, D., Ohlenschläger, O., Leipold, E., Ullrich, F., Kühl, T., Mischo, A., Buntkowsky, G., Görlach, M., Heinemann, S. H., et al. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201107011 · Cited by 57

Identification of Equivalent Residues in the γ, δ, and ε Subunits of the Nicotinic Receptor That Contribute to α-Bungarotoxin Binding

Sine, S. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23521 · Cited by 55

Roles of Individual Disulfide Bonds in the Stability and Folding of an ω-Conotoxin

Price-Carter, M. L., Hull, M. S., & Goldenberg, D. P. (1998) · Biochemistry · doi:10.1021/bi9803978 · Cited by 54

Optimization of oxidative folding methods for cysteine‐rich peptides: a study of conotoxins containing three disulfide bridges

Steiner, A. M., & Bulaj, G. W. (2010) · Journal of Peptide Science · doi:10.1002/psc.1283 · Cited by 53

Decrease in α3*/α6* Nicotinic Receptors but Not Nicotine-Evoked Dopamine Release in Monkey Brain after Nigrostriatal Damage

McCallum, S. E., Parameswaran, N., Bordia, T., McIntosh, J. M., Grady, S. R., & Quik, M. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.012773 · Cited by 53

Conorfamide, a Conus venom peptide belonging to the RFamide family of neuropeptides

Maillo, M. A., Aguilar, M. B., López‐Vera, E., Craig, A. G., Bulaj, G. W., Olivera, B. M., & Heimer, E. P. (2002) · Toxicon · doi:10.1016/s0041-0101(01)00176-3 · Cited by 52

Interactions of Key Charged Residues Contributing to Selective Block of Neuronal Sodium Channels by μ-Conotoxin KIIIA

McArthur, J. R., Singh, G., McMaster, D., Winkfein, R. J., Tieleman, D. P., & French, R. J. (2011) · Molecular Pharmacology · doi:10.1124/mol.111.073460 · Cited by 52

Characterization of novel M‐superfamily conotoxins with new disulfide linkage

Han, Y., Wang, Q., Jiang, H., Liu, L., Xiao, C., Yuan, D., Shao, X., Dai, Q., Cheng, J., & Chi, C. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05493.x · Cited by 51

α‐Conotoxins EpI and AuIB switch subtype selectivity and activity in native versus recombinant nicotinic acetylcholine receptors

Nicke, A., Samochocki, M., Loughnan, M. L., Bansal, P. S., Maelicke, A., & Lewis, R. J. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01161-x · Cited by 51

Intrathecal Therapy: What Has Changed With the Introduction of Ziconotide

Kress, H. G., Simpson, K. H., Marchettini, P., Donck, A. V., & Varrassi, G. (2009) · Pain Practice · doi:10.1111/j.1533-2500.2009.00308.x · Cited by 50

Electrostatic Recognition and Induced Fit in the κ-PVIIA Toxin Binding to Shaker Potassium Channel

Huang, X., Dong, F., & Zhou, H. (2005) · Journal of the American Chemical Society · doi:10.1021/ja042641q · Cited by 50

Conotoxins of the O-superfamily affecting voltage-gated sodium channels

Heinemann, S. H., & Leipold, E. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6565-5 · Cited by 50

A novel conotoxin from Conus striatus, μ-SIIIA, selectively blocking rat tetrodotoxin-resistant sodium channels

Wang, C., Zhang, H., Jiang, H., Lu, W., Zhao, Z., & Chi, C. (2005) · Toxicon · doi:10.1016/j.toxicon.2005.10.008 · Cited by 49

Site‐Specific pKa Determination of Selenocysteine Residues in Selenovasopressin by Using 77Se NMR Spectroscopy

Mobli, M., Morgenstern, D., King, G. F., et al. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201104169 · Cited by 49

Novel α‐conotoxins fromConus spuriusand the α‐conotoxin EI share high‐affinity potentiation and low‐affinity inhibition of nicotinic acetylcholine receptors

López‐Vera, E., Aguilar, M. B., Schiavon, E., Marinzi, C., Ortíz, E., Cassulini, R. R., Batista, C. V. F., Possani, L. D., Heimer, E. P., Peri, F., et al. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05931.x · Cited by 47

Identifying Key Amino Acid Residues That Affect α-Conotoxin AuIB Inhibition of α3β4 Nicotinic Acetylcholine Receptors

Grishin, A. A., Cuny, H., Hung, A., Clark, R. J., Brust, A., Akondi, K. B., Alewood, P. F., Craik, D. J., & Adams, D. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.512582 · Cited by 47

Hyperhydroxylation: A New Strategy for Neuronal Targeting by Venomous Marine Molluscs

Franco, A., Pisarewicz, K., Möller, C., Mora, D., Fields, G. B., & Marí, F. (2006) · Progress in molecular and subcellular biology · doi:10.1007/978-3-540-30880-5_4 · Cited by 46

Analysis of expressed sequence tags from the venom ducts of Conus striatus: focusing on the expression profile of conotoxins

Pi, C., Liu, Y., Peng, C., Jiang, X., Liu, J., Xu, B. D., Yu, X., Yu, Y., Jiang, X., Wang, L., et al. (2005) · Biochimie · doi:10.1016/j.biochi.2005.08.001 · Cited by 46

Role of γ-Carboxyglutamic Acid in the Calcium-Induced Structural Transition of Conantokin G, a Conotoxin from the Marine Snail Conus geographus,

Rigby, A. C., Baleja, J., Li, L., et al. (1997) · Biochemistry · doi:10.1021/bi9718550 · Cited by 46

Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics

Jin, A., Brandstaetter, H., Nevin, S. T., Tan, C. C., Clark, R. J., Adams, D. J., Alewood, P. F., Craik, D. J., & Daly, N. L. (2007) · BMC Structural Biology · doi:10.1186/1472-6807-7-28 · Cited by 45

Specialisation of the Venom Gland Proteome in Predatory Cone Snails Reveals Functional Diversification of the Conotoxin Biosynthetic Pathway

Safavi-Hemami, H., Siero, W. A., Gorasia, D. G., Young, N. D., Macmillan, D. L., Williamson, N. A., & Purcell, A. W. (2011) · Journal of Proteome Research · doi:10.1021/pr1012976 · Cited by 45

Determination of α‐conotoxin binding modes on neuronal nicotinic acetylcholine receptors

Dutertre, S., Nicke, A., Tyndall, J. D. A., & Lewis, R. J. (2004) · Journal of Molecular Recognition · doi:10.1002/jmr.683 · Cited by 43

Modulation of Conotoxin Structure and Function Is Achieved through a Multienzyme Complex in the Venom Glands of Cone Snails

Safavi-­Hemami, H., Gorasia, D. G., Steiner, A. M., Williamson, N. A., Karas, J. A., Gajewiak, J., Olivera, B. M., Bulaj, G. W., & Purcell, A. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.366781 · Cited by 42

Facile preparation of disulfide‐bridged peptides using the polymer‐supported oxidant CLEAR‐OXTM*

Darłak, K., Long, D. W., Czerwiński, A. A., Darlak, M., Valenzuela, F. J., Spatola, A. F., & Bárány, G. (2004) · Journal of Peptide Research · doi:10.1111/j.1399-3011.2004.00153.x · Cited by 41

NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids

Marx, U. C., Daly, N. L., & Craik, D. J. (2006) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.1821 · Cited by 41

Protein Folding Determinants: Structural Features Determining Alternative Disulfide Pairing in α- and χ/λ-Conotoxins,

Kang, T. S., Radić, Z., Talley, T. T., Jois, S. D. S., Taylor, P., & Kini, R. M. (2007) · Biochemistry · doi:10.1021/bi061969o · Cited by 40

Engineering of α‐conotoxin MII‐derived peptides with increased selectivity for native α6β2 ∗ nicotinic acetylcholine receptors

Pucci, L., Grazioso, G., Dallanoce, C., Rizzi, L., Micheli, C. D., Clementi, F., Bertrand, S., Bertrand, D., Longhi, R., Amici, M. D., et al. (2011) · The FASEB Journal · doi:10.1096/fj.10-179853 · Cited by 40

PADLOC: A Powerful Tool to Assign Disulfide Bond Connectivities in Peptides and Proteins by NMR Spectroscopy

Poppe, L., Hui, J. O., Ligutti, J., Murray, J. K., & Schnier, P. D. (2011) · Analytical Chemistry · doi:10.1021/ac203078x · Cited by 39

A Synthetic Combinatorial Strategy for Developing α-Conotoxin Analogs as Potent α7 Nicotinic Acetylcholine Receptor Antagonists

Armishaw, C. J., Singh, N. P., Medina‐Franco, J. L., Clark, R. J., Scott, K. C. M., Houghten, R. A., & Jensen, A. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071183 · Cited by 38

Conolysin-Mt: A Conus Peptide That Disrupts Cellular Membranes

Biggs, J. S., Rosenfeld, Y., Shai, Y., & Olivera, B. M. (2007) · Biochemistry · doi:10.1021/bi700775p · Cited by 37

Constrained De Novo Sequencing of Conotoxins

Bhatia, S. P., Kil, Y. J., Ueberheide, B. M., Chait, B. T., Tayo, L. L., Cruz, L. J., Lu, B., Yates, J. R., & Bern, M. W. (2012) · Journal of Proteome Research · doi:10.1021/pr300312h · Cited by 34

Role of disulfide bridges in the folding, structure and biological activity of ω-conotoxin GVIA

Flinn, J. P., Pallaghy, P. K., Lew, M. J., Murphy, R., Angus, J. A., & Norton, R. S. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00165-x · Cited by 34

Cryptic Species Differentiated in Conus ebraeus, a Widespread Tropical Marine Gastropod

Duda, T. F., Kohn, A. J., & Matheny, A. M. (2009) · Biological Bulletin · doi:10.1086/bblv217n3p292 · Cited by 34

Analogies and differences between ω-conotoxins MVIIC and MVIID: binding sites and functions in bovine chromaffin cells

Gandı́a, L., Lara, B., Imperial, J. S., Villarroya, M., Albillos, A., Maroto, R., Garcı́a, A. G., & Olivera, B. M. (1997) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s004240050483 · Cited by 33

Improving the Stability of α-Conotoxin AuIB Through N-to-C Cyclization: The Effect of Linker Length on Stability and Activity at Nicotinic Acetylcholine Receptors

Armishaw, C. J., Jensen, A. A., Balle, L. D., Scott, K. C. M., Sørensen, L., & Strømgaard, K. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3458 · Cited by 32

Enhanced microwave‐assisted method for on‐bead disulfide bond formation: Synthesis of α‐conotoxin MII

Galanis, A., Alberício, F., & Grøtli, M. (2008) · Biopolymers · doi:10.1002/bip.21116 · Cited by 31

Solution structure of an M‐1 conotoxin with a novel disulfide linkage

Du, W., Han, Y., Huang, F., Li, J., Chi, C., & Fang, W. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05795.x · Cited by 30

Recruitment of Glycosyl Hydrolase Proteins in a Cone Snail Venomous Arsenal: Further Insights into Biomolecular Features of Conus Venoms

Violette, A., Leonardi, A., Piquemal, D., Terrat, Y., Biass, D., Dutertre, S., Noguier, F., Ducancel, F., Stöcklin, R., Križaj, I., et al. (2012) · Marine Drugs · doi:10.3390/md10020258 · Cited by 30

Spinal actions of ω‐conotoxins, CVID , MVIIA and related peptides in a rat neuropathic pain model

Jayamanne, A., Jeong, H. J., Schroeder, C. I., Lewis, R. J., Christie, M. J., & Vaughan, C. W. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12251 · Cited by 30

A New Mechanism for Metal Ion-assisted Interchain Helix Assembly in a Naturally Occurring Peptide Mediated by Optimally Spaced γ-Carboxyglutamic Acid Residues

Dai, Q., Prorok, M., & Castellino, F. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.12.027 · Cited by 29

Glycosylation of Conotoxins

Gerwig, G. J., Hocking, H. G., Stöcklin, R., Kamerling, J. P., & Boelens, R. (2013) · Marine Drugs · doi:10.3390/md11030623 · Cited by 29

μ-Conotoxin KIIIA Derivatives with Divergent Affinities versus Efficacies in Blocking Voltage-Gated Sodium Channels

Zhang, M.-M., Han, T., Olivera, B. M., Bulaj, G. W., & Yoshikami, D. (2010) · Biochemistry · doi:10.1021/bi100207k · Cited by 29

Probing peptide libraries from Conus achatinus using mass spectrometry and cDNA sequencing: identification of δ and ω‐conotoxins

Gowd, K. H., Dewan, K. K., Iengar, P., Krishnan, K. S., & Balaram, P. (2008) · Journal of Mass Spectrometry · doi:10.1002/jms.1377 · Cited by 28

Efficient Binding of 4/7 α-Conotoxins to Nicotinic α4β2 Receptors Is Prevented by Arg185 and Pro195 in the α4 Subunit

Beissner, M., Dutertre, S., Schemm, R., Danker, T., Sporning, A., Grubmüller, H., & Nicke, A. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.078683 · Cited by 27

Chemistry and Enzymology of Disulfide Cross-Linking in Proteins

Fass, D., & Thorpe, C. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00123 · Cited by 321