Results 41 to 50 of about 1,314 (186)

Synthesis and evaluation of a novel analgesic conotoxin Lt7b that inhibits calcium currents and increases sodium currents

Journal of Cellular and Molecular Medicine, Volume 26, Issue 20, Page 5330-5334, October 2022., 2022
Abstract Conotoxins are promising neuropharmacological tools and drug candidates due to their high efficiency and specificity in targeting ion channels or neurotransmitter receptors. In this study, a novel O2‐superfamily conotoxin, Lt7b, was synthesized and its pharmacological functions were evaluated.
Yun Wu, Manyi Yang, Yubin Li, Wei Zhang, Maojun Zhou   +4 more
wiley   +1 more source

Discovery of KV1.3 ion channel inhibitors: Medicinal chemistry approaches and challenges

Medicinal Research Reviews, Volume 41, Issue 4, Page 2423-2473, July 2021., 2021
Abstract The KV1.3 voltage‐gated potassium ion channel is involved in many physiological processes both at the plasma membrane and in the mitochondria, chiefly in the immune and nervous systems. Therapeutic targeting KV1.3 with specific peptides and small molecule inhibitors shows great potential for treating cancers and autoimmune diseases, such as ...
Špela Gubič, Louise A. Hendrickx, Žan Toplak, Maša Sterle, Steve Peigneur, Tihomir Tomašič, Luis A. Pardo, Jan Tytgat, Anamarija Zega, Lucija P. Mašič   +9 more
wiley   +1 more source

ConoMode, a database for conopeptide binding modes

Database, 2020
Abstract ConoMode is a database for complex three-dimensional (3D) structures of conopeptides binding with their target proteins. Conopeptides, a large family of peptides from the venom of marine snails of the Conus genus, have exceptionally diverse sequences, and their high specificity to block ion channels makes them crucial as drug ...
Xiao Li, Hao Liu 0045, Chunxiao Gao, Yangyang Li, Dongning Jia, Yanbo Yang, Jinbo Yang, Zhiqiang Wei 0002, Tao Jiang 0057, Rilei Yu   +9 more
openaire   +2 more sources

The mitochondrial genome of the venomous cone snail conus consors [PDF]

, 2012
Cone snails are venomous predatory marine neogastropods that belong to the species-rich superfamily of the Conoidea. So far, the mitochondrial genomes of two cone snail species (Conus textile and Conus borgesi) have been described, and these feed on ...
Baden-Tillson, Holly, Brauer, Age, Heidler, Juliana, Kauferstein, Silke, Kurz, Alexander, Mebs, Dietrich, Remm, Maido, Stockwell, Tim, Stöcklin, Reto, Wittig, Ilka   +9 more
core   +7 more sources

Venomous secretions from marine snails of the Terebridae family target acetylcholine receptors [PDF]

, 2013
Venoms from cone snails (Conidae) have been extensively studied during the last decades, but those from other members of the suborder Toxoglossa, such as of Terebridae and Turridae superfamilies attracted less interest so far. Here, we report the effects
Kauferstein, Silke, Kendel, Yvonne, Kurz, Alexander, Mebs, Dietrich, Melaun, Christian, Nicke, Annette, Peigneur, Steve, Tytgat, Jan, Wunder, Cora   +8 more
core   +3 more sources

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

BMC Genomics, 2011
Background The venomous marine gastropods, cone snails (genus Conus), inject prey with a lethal cocktail of conopeptides, small cysteine-rich peptides, each with a high affinity for its molecular target, generally an ion channel, receptor or transporter.
Olivera Baldomero M, Bandyopadhyay Pradip K, Hu Hao, Yandell Mark   +3 more
doaj   +1 more source

Novel conopeptides of the I-superfamily occur in several clades of cone snails [PDF]

, 2004
The I-superfamily of conotoxins represents a new class of peptides in the venom of some Conus species. These toxins are characterized by four disulfide bridges and inhibit or modify ion channels of nerve cells.
Huys, I., Kauferstein, S., Kuch, U., Mebs, D., Melaun, C., Tytgat, J.   +5 more
core   +1 more source

Cupryphans, metal‐binding, redox‐active, redesigned conopeptides [PDF]

Protein Science, 2009
AbstractContryphans are bioactive peptides, isolated from the venom of marine snails of the genus Conus, which are characterized by the short length of the polypeptide chain and the high degree of unusual post‐translational modifications. The cyclization of the polypeptide chain through a single disulphide bond, the presence of two conserved Pro ...
BARBA, MARCO, A. P. SOBOLEV, C. ROMEO, SCHININA', Maria Eugenia, D. PIETRAFORTE, MANNINA, LUISA, G. MUSCI, F. POLTICELLI   +7 more
openaire   +6 more sources

Identification and Characterization of a Novel Family of Cysteine-Rich Peptides (MgCRP-I) from Mytilus galloprovincialis [PDF]

, 2015
We report the identification of a novel gene family (named MgCRP-I) encoding short secreted cysteine-rich peptides in the Mediterranean mussel Mytilus galloprovincialis.
Benincasa, Monica, Gerdol, Marco, Giulianini, Piero Giulio, Guarnaccia, Corrado, Lucaf\uf2, Marianna, Manfrin, Chiara, Moro, Gianluca De, Pallavicini, Alberto, Puillandre, Nicolas, Sava, Gianni, Torboli, Valentina, Venier, Paola, Zlatev, Ventislav   +12 more
core   +2 more sources

Engineered biosynthesis of cyclotides

New Zealand Journal of Botany, Volume 58, Issue 4, Page 358-377, December 2020., 2020
ABSTRACT A system based on cyanobacterial split inteins, SICLOPPs (Split Intein Circular Ligation of Proteins and Peptides), has been used to synthesise a small natively cyclic plant protein, kalata B1, and cyclised versions of the natively linear therapeutic peptides ziconotide and leconotide.
Thomas N. G. Handley, Hyon‐Xhi Tan, Malcolm T. Rutledge, Hans Henning Brewitz, Joel D. A. Tyndall, Torsten Kleffmann, Margi I. Butler, Russell T. M. Poulter, Sigurd M. Wilbanks   +8 more
wiley   +1 more source