Please use this identifier to cite or link to this item:
https://hdl.handle.net/11147/11824
Title: | NAChRDB: A web resource of structure-function annotations to unravel the allostery of nicotinic acetylcholine receptors | Authors: | Chareshneu, Aliaksei Pant, Purbaj Ramos, Ravi Jose Tristao Sehmal, David Gökbel, Tuğrul Ionescu, Crina-Maria Koca, Jaroslav |
Keywords: | Nicotinic acetylcholine receptors NAChRDB |
Publisher: | American Chemical Society | Abstract: | Nicotinic acetylcholine receptors (nAChRs) comprise a large and ancient family of allosteric ion channels mediating synaptic transmission. The vast knowledge about nAChRs has become difficult to navigate. NAChRDB is a web-accessible resource of curated residue-level functional annotations of neuromuscular nAChRs. Interactive three-dimensional (3D) visualization and sequence alignment give further context to this rich and growing collection of experimental observations and computational predictions. NAChRDB is freely available at https://crocodile.ncbr.muni.cz/Apps/NAChRDB/, with interactive tutorials and regular updates to the content and web interface. No installation or user registration is required. NAChRDB is accessible through any modern internet browser on desktops and mobile devices. By providing immediate and systematic access to practical knowledge gained through decades of research, NAChRDB represents a powerful educational tool and helps guide discovery by revealing gaps in current knowledge and aiding the interpretation of results of molecular and structural biology experiments or computational studies. | URI: | https://doi.org/10.1021/acsomega.1c00817 https://hdl.handle.net/11147/11824 |
ISSN: | 2470-1343 |
Appears in Collections: | Molecular Biology and Genetics / Moleküler Biyoloji ve Genetik PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection |
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acsomega.1c00817.pdf | 2.37 MB | Adobe PDF | View/Open |
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