Ligand design for human acetylcholinesterase and nicotinic acetylcholine receptors, extending beyond the conventional and canonical-Reference-Cited by-同舟云学术

Ligand design for human acetylcholinesterase and nicotinic acetylcholine receptors, extending beyond the conventional and canonical

Published:2021-03-12 Issue:6 Volume:158 Page:1217-1222
ISSN:0022-3042
Container-title:Journal of Neurochemistry
language:en
Short-container-title:J. Neurochem.

Author:

Taylor Palmer¹^ORCID,Shyong Yan‐Jye¹,Samskey Nathan¹,Ho Kwok‐Yiu¹,Radic' Zoran¹,Fenical William²,Sharpless K. Barry³,Kovarik Zrinka⁴,Camacho‐Hernandez Gisela‐Andrea¹

Affiliation:

1. Department of Pharmacology Skaggs School of Pharmacy & Pharmaceutical Sciences University of California CA USA

2. Scripps Institution of Oceanography University of California CA USA

3. Skaggs Institute for Chemical Biology The Scripps Research Institute San Diego CA USA

4. Institute for Medical Research and Occupational Health Zagreb Croatia

Publisher

Wiley

Subject

Cellular and Molecular Neuroscience,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/jnc.15335

Reference26 articles.

1. An Analog of Lophotoxin Reacts Covalently with Tyr190 in the α-Subunit of the Nicotinic Acetylcholine Receptor

2. Selectivity Optimization of Substituted 1,2,3-Triazoles as α7 Nicotinic Acetylcholine Receptor Agonists

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

4. Synthesis, Pharmacological Characterization, and Structure–Activity Relationships of Noncanonical Selective Agonists for α7 nAChRs

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