Cargando…

A Novel α4/7-Conotoxin QuIA Selectively Inhibits α3β2 and α6/α3β4 Nicotinic Acetylcholine Receptor Subtypes with High Efficacy

α6β4 nAChR is expressed in the peripheral and central nervous systems and is associated with pain, addiction, and movement disorders. Natural α-conotoxins (α-CTxs) can effectively block different nAChR subtypes with higher efficacy and selectivity. However, the research on α6β4 nAChR is relatively p...

Descripción completa

Detalles Bibliográficos
Autores principales:	Wang, Liujun, Wu, Xixi, Zhu, Xiaopeng, Zhangsun, Dongting, Wu, Yong, Luo, Sulan
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2022
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8878501/ https://www.ncbi.nlm.nih.gov/pubmed/35200675 http://dx.doi.org/10.3390/md20020146

Ejemplares similares

Effect of Methionine Oxidation and Substitution of α-Conotoxin TxID on α3β4 Nicotinic Acetylcholine Receptor
por: Ren, Jie, et al.
Publicado: (2018)

Characterization of an α 4/7-Conotoxin LvIF from Conus lividus That Selectively Blocks α3β2 Nicotinic Acetylcholine Receptor
por: Guo, Man, et al.
Publicado: (2021)

Fluorescently Labeled α-Conotoxin TxID, a New Probe for α3β4 Neuronal Nicotinic Acetylcholine Receptors
por: Huang, Meiling, et al.
Publicado: (2022)

Influence of Disulfide Connectivity on Structure and Bioactivity of α-Conotoxin TxIA
por: Wu, Yong, et al.
Publicado: (2014)

Molecular Determinants of Species Specificity of α-Conotoxin TxIB towards Rat and Human α6/α3β4 Nicotinic Acetylcholine Receptors
por: Xie, Ting, et al.
Publicado: (2023)

α-Conotoxin TxIB: A Uniquely Selective Ligand for α6/α3β2β3 Nicotinic Acetylcholine Receptor Attenuates Nicotine-Induced Conditioned Place Preference in Mice
por: You, Shen, et al.
Publicado: (2019)

Recombinant Expression and Characterization of α-Conotoxin LvIA in Escherichia coli
por: Zhu, Xiaopeng, et al.
Publicado: (2016)

Identification of Crucial Residues in α-Conotoxin EI Inhibiting Muscle Nicotinic Acetylcholine Receptor
por: Ning, Jiong, et al.
Publicado: (2019)

Substitution of D-Arginine at Position 11 of α-RgIA Potently Inhibits α7 Nicotinic Acetylcholine Receptor
por: Wu, Yong, et al.
Publicado: (2023)

Alanine-Scanning Mutagenesis of α-Conotoxin GI Reveals the Residues Crucial for Activity at the Muscle Acetylcholine Receptor
por: Ning, Jiong, et al.
Publicado: (2018)

α-Conotoxin TxIB Inhibits Development of Morphine-Induced Conditioned Place Preference in Mice via Blocking α6β2* Nicotinic Acetylcholine Receptors
por: Li, Xiaodan, et al.
Publicado: (2021)

αO-Conotoxin GeXIVA Inhibits the Growth of Breast Cancer Cells via Interaction with α9 Nicotine Acetylcholine Receptors
por: Sun, Zhihua, et al.
Publicado: (2020)

Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB
por: Li, Xincan, et al.
Publicado: (2020)

DSPE-PEG Modification of α-Conotoxin TxID
por: Zhao, Weinan, et al.
Publicado: (2019)

The α9α10 Nicotinic Acetylcholine Receptor Antagonist αO-Conotoxin GeXIVA[1,2] Alleviates and Reverses Chemotherapy-Induced Neuropathic Pain
por: Wang, Huanbai, et al.
Publicado: (2019)

A Novel Inhibitor of α9α10 Nicotinic Acetylcholine Receptors from Conus vexillum Delineates a New Conotoxin Superfamily
por: Luo, Sulan, et al.
Publicado: (2013)

Degradation kinetics of α‐conotoxin TxID
por: Xu, Pan, et al.
Publicado: (2019)

d-Amino Acid Substitution of α-Conotoxin RgIA Identifies its Critical Residues and Improves the Enzymatic Stability
por: Ren, Jie, et al.
Publicado: (2019)

α-Conotoxin TxID and [S9K]TxID, α3β4 nAChR Antagonists, Attenuate Expression and Reinstatement of Nicotine-Induced Conditioned Place Preference in Mice
por: Li, Xiaodan, et al.
Publicado: (2020)

Differential Expression of Nicotine Acetylcholine Receptors Associates with Human Breast Cancer and Mediates Antitumor Activity of αO-Conotoxin GeXIVA
por: Sun, Zhihua, et al.
Publicado: (2020)

Structural mechanisms for α-conotoxin activity at the human α3β4 nicotinic acetylcholine receptor
por: Abraham, Nikita, et al.
Publicado: (2017)

From crystal structure of α-conotoxin GIC in complex with Ac-AChBP to molecular determinants of its high selectivity for α3β2 nAChR
por: Lin, Bo, et al.
Publicado: (2016)

Cysteine [2,4] Disulfide Bond as a New Modifiable Site of α-Conotoxin TxIB
por: Zhang, Baojian, et al.
Publicado: (2021)

Loop2 Size Modification Reveals Significant Impacts on the Potency of α-Conotoxin TxID
por: Dong, Jianying, et al.
Publicado: (2023)

Optimal Cleavage and Oxidative Folding of α-Conotoxin TxIB as a Therapeutic Candidate Peptide
por: Wu, Xiaosa, et al.
Publicado: (2013)

α-Conotoxin TxIB Improved Behavioral Abnormality and Changed Gene Expression in Zebrafish (Danio rerio) Induced by Alcohol Withdrawal
por: Mao, Kailin, et al.
Publicado: (2022)

Mechanism of interactions between α-conotoxin RegIIA and carbohydrates at the human α3β4 nicotinic acetylcholine receptor
por: Zheng, Meiling, et al.
Publicado: (2021)

Inflammation Regulation via an Agonist and Antagonists of α7 Nicotinic Acetylcholine Receptors in RAW264.7 Macrophages
por: Tan, Yao, et al.
Publicado: (2022)

Discovery of a Potent and Selective α3β4 Nicotinic Acetylcholine Receptor Antagonist from an α-Conotoxin Synthetic Combinatorial Library
por: Chang, Yi-Pin, et al.
Publicado: (2014)

Interactions of the α3β2 Nicotinic Acetylcholine Receptor Interfaces with α-Conotoxin LsIA and its Carboxylated C-terminus Analogue: Molecular Dynamics Simulations
por: Wen, Jierong, et al.
Publicado: (2020)

Novel αO-conotoxin GeXIVA[1,2] Nonaddictive Analgesic with Pharmacokinetic Modelling-Based Mechanistic Assessment
por: Zhu, Xiaoyu, et al.
Publicado: (2022)

Single-channel properties of α3β4, α3β4α5 and α3β4β2 nicotinic acetylcholine receptors in mice lacking specific nicotinic acetylcholine receptor subunits
por: Ciuraszkiewicz, Anna, et al.
Publicado: (2013)

The α5 Nicotinic Acetylcholine Receptor Subunit Differentially Modulates α4β2(*) and α3β4(*) Receptors
por: Scholze, Petra, et al.
Publicado: (2020)

Effects of C-Terminal Carboxylation on α-Conotoxin LsIA Interactions with Human α7 Nicotinic Acetylcholine Receptor: Molecular Simulation Studies
por: Wen, Jierong, et al.
Publicado: (2019)

Synthesis of the Most Potent Isomer of μ-Conotoxin KIIIA Using Different Strategies
por: Jian, Xunxun, et al.
Publicado: (2023)

Unique Pharmacological Properties of α-Conotoxin OmIA at α7 nAChRs
por: Ho, Thao N.T., et al.
Publicado: (2021)

Discovery Methodology of Novel Conotoxins from Conus Species
por: Fu, Ying, et al.
Publicado: (2018)

Identification of a Negative Allosteric Site on Human α4β2 and α3β4 Neuronal Nicotinic Acetylcholine Receptors
por: Pavlovicz, Ryan E., et al.
Publicado: (2011)

The crystal structure of Ac-AChBP in complex with α-conotoxin LvIA reveals the mechanism of its selectivity towards different nAChR subtypes
por: Xu, Manyu, et al.
Publicado: (2017)

Mutagenesis of α-Conotoxins for Enhancing Activity and Selectivity for Nicotinic Acetylcholine Receptors
por: Turner, Matthew W., et al.
Publicado: (2019)

Cannot write session to /tmp/vufind_sessions/sess_mcjnbk8o3krdnn41mgga285t9m