Results 51 to 60 of about 2,250 (207)

Semienzymatic cyclization of disulfide-rich peptides using sortase A [PDF]

, 2014
Background: Sortase A (SrtA) is a transpeptidase capable of catalyzing the formation of amide bonds. Results: SrtA was used to backbone-cyclize disulfide-rich peptides, including kalata B1, -conotoxin Vc1.1, and SFTI-1.
Aboye, Antos, Antos, Barry, Bartels, Bolscher, Brünger, Cascales, Cemazar, Chan, Chen, Chia Chia Tan, Ching-I Anderson Wang, Christina I. Schroeder, Clark, Clark, Clark, Colgrave, Conibear, Contreras, Craik, Craik, Daly, Daly, David J. Craik, Davis, Dawson, Dominguez, Ganz, Gould, Gran, Greenwood, Griesinger, Gruber, Gunasekera, Gustafson, Güntert, Henriques, Huang, Huang, Hwang, Jason P. Mulvenna, Jennings, Jennings, Ji, K. Johan Rosengren, Kaas, Kawakami, Kimura, Koradi, Lai Y. Chan, Levary, Lindholm, Ling, Linge, Long, Luckett, Marraffini, Mazmanian, Moffatt, Muir, Mulvenna, Nederveen, Parthasarathy, Pattabiraman, Plan, Popp, Popp, Popp, Rosengren, Shen, Simonsen, Soohyun Kwon, Svangård, Tam, Tavassoli, Terlau, Thongyoo, Thongyoo, Ton-That, Trabi, Vranken, Wang, Wishart, Wishart, Witte, Wong, Wong, Wu, Wüthrich, Xinying Jia, Yen-Hua Huang   +91 more
core   +1 more source

Natural Compounds Interacting with Nicotinic Acetylcholine Receptors: From Low-Molecular Weight Ones to Peptides and Proteins

Toxins, 2015
Nicotinic acetylcholine receptors (nAChRs) fulfill a variety of functions making identification and analysis of nAChR subtypes a challenging task. Traditional instruments for nAChR research are d-tubocurarine, snake venom protein α-bungarotoxin (α-Bgt ...
Denis Kudryavtsev, Irina Shelukhina, Catherine Vulfius, Tatyana Makarieva, Valentin Stonik, Maxim Zhmak, Igor Ivanov, Igor Kasheverov, Yuri Utkin, Victor Tsetlin   +9 more
doaj   +1 more source

Conotoxins: structure, therapeutic potential and pharmacological applications. [PDF]

, 2016
Cone snails, also known as marine gastropods, from Conus genus produce in their venom a diverse range of small pharmacologically active structured peptides called conotoxins.
Kamal, M., Kamal, M., Karim, S., Karim, S., Mir, R., Mir, R., Mirza, Z., Mirza, Z., Wilson, C., Wilson, C.   +9 more
core   +2 more sources

From Crystal Structures of RgIA4 in Complex with Ac-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR

Marine Drugs, 2021
α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR.
Si Pan, Yingxu Fan, Xiaopeng Zhu, Yi Xue, Sulan Luo, Xinquan Wang   +5 more
doaj   +1 more source

Molecular basis for a pore block of Tentonin 3 expressed in HEK293 cells by a conopeptide, NMB‐1

British Journal of Pharmacology, Volume 183, Issue 9, Page 1845-1859, May 2026.
Background and Purpose Tentonin 3 (TTN3/TMEM150C) is a mechanosensitive ion channel that plays critical roles in mechanotransduction processes. TTN3 forms a tetramer with a predicted rectangular shape and a central pore. A conotoxin ρ‐TIA and its synthetic analog, noxious mechanosensation blocker 1 (NMB‐1), were initially developed to inhibit slowly ...
Sujin Lim, Junhyuk Woo, Sungmin Pak, Joonho Paik, Gyu‐Sang Hong, Ji Hun Wi, Sanghee Lee, Cristina Fenollar‐Ferrer, Kyungreem Han, Young Kee Shin, Uhtaek Oh   +10 more
wiley   +1 more source

RgIA4 Potently Blocks Mouse α9α10 nAChRs and Provides Long Lasting Protection against Oxaliplatin-Induced Cold Allodynia

Frontiers in Cellular Neuroscience, 2017
Transcripts for α9 and α10 nicotinic acetylcholine receptor (nAChR) subunits are found in diverse tissues. The function of α9α10 nAChRs is best known in mechanosensory cochlear hair cells, but elsewhere their roles are less well-understood.
Sean B. Christensen, Arik J. Hone, Isabelle Roux, Julie Kniazeff, Jean-Philippe Pin, Grégory Upert, Denis Servent, Elisabeth Glowatzki, Elisabeth Glowatzki, J. Michael McIntosh, J. Michael McIntosh, J. Michael McIntosh   +11 more
doaj   +1 more source

Y-aminobutyric acid type B (GABAB) receptor expression is needed for inhibition of N-type (Cav2.2) calcium channels by analgesic a-conotoxins [PDF]

, 2012
Background: A class of analgesic a-conotoxins potently inhibits N-type calcium channels. Results: The activity of a-conotoxins Vc1.1 and RgIA was reduced following knockdown of GABAB receptor expression in sensory neurons and can be reconstituted in ...
Adams, DJ, Berecki, G, Cuny, H, de Faoite, A, Huynh, T, Yasuda, T   +5 more
core  

Neurochemistry [PDF]

, 2021
Neurochemistry is a flourishing academic field that contributes to our understanding of molecular, cellular and medical neurobiology. As a scientific discipline, neurochemistry studies the role of chemicals that build the nervous system, it explores the ...

core   +1 more source

GABAB receptor‐mediated modulation of sensory neuron excitability: Roles of CaV2.2, G‐protein‐coupled inwardly rectifying potassium (GIRK) channels, and hyperpolarisation‐activated cyclic nucleotide‐gated (HCN) channels in human and mouse nociception

Experimental Physiology, Volume 111, Issue 4, Page 2026-2043, 1 April 2026.
Abstract Chronic visceral pain is a key symptom of irritable bowel syndrome. Modulation of voltage‐gated calcium and potassium channels by G protein‐coupled receptors plays a key role in dampening nociceptive transmission. Both baclofen and the analgesic peptide α‐conotoxin Vc1.1 activate GABAB receptors (GABABR), resulting in inhibition of CaV2.2 and ...
Mariana Brizuela, Anuja R. Bony, Sonia Garcia‐Caraballo, David J. Adams, Stuart M. Brierley   +4 more
wiley   +1 more source

Three-Dimensional Structure of Conotoxin tx3a: A m-1 Branch Peptide of the M-Superfamily [PDF]

, 2008
The M-superfamily, one of eight major conotoxin superfamilies found in the venom of the cone snail, contains a Cys framework with disulfide-linked loops labeled 1, 2, and 3 (- CC1C2C3CC-). M-superfamily conotoxins can be divided into the m-1, -2, -3 and -
McDougal, Owen M., Ormond, Andrew J., Poulter, C. Dale, Turner, Matthew W.   +3 more
core   +1 more source