Generation of Candidate Ligands for Nicotinic Acetylcholine Receptors via in situ Click Chemistry with a Soluble Acetylcholine Binding Protein Template (Q27677865)

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Language	Label	Description	Also known as
English	Generation of Candidate Ligands for Nicotinic Acetylcholine Receptors via in situ Click Chemistry with a Soluble Acetylcholine Binding Protein Template	scientific article

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scholarly article

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Generation of Candidate Ligands for Nicotinic Acetylcholine Receptors via in situ Click Chemistry with a Soluble Acetylcholine Binding Protein Template (English)

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1 reference

based on heuristic

inferred from title

click chemistry

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based on heuristic

inferred from title

Karl Barry Sharpless

10

object named as

K Barry Sharpless

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Valery V. Fokin

12

object named as

Valery V Fokin

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Joseph R Fotsing

3

object named as

Joseph R Fotsing

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4

object named as

Timo Weide

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author name string

Neil P Grimster

1

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Bernhard Stump

2

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Todd T Talley

5

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John G Yamauchi

6

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Ákos Nemecz

7

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Choel Kim

8

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Kwok-Yiu Ho

9

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Palmer Taylor

11

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language of work or name

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publication date

18 April 2012

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Journal of the American Chemical Society

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134

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15

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6732-40

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Creating an 7 Nicotinic Acetylcholine Recognition Domain from the Acetylcholine-binding Protein: CRYSTALLOGRAPHIC AND LIGAND SELECTIVITY ANALYSES

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Conformational Remodeling of Femtomolar Inhibitor−Acetylcholinesterase Complexes in the Crystalline State

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Structural determinants in phycotoxins and AChBP conferring high affinity binding and nicotinic AChR antagonism

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Structural determinants for interaction of partial agonists with acetylcholine binding protein and neuronal α7 nicotinic acetylcholine receptor

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Nicotine binding to brain receptors requires a strong cation-pi interaction

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Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation

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Refinement of macromolecular structures by the maximum-likelihood method

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Likelihood-enhanced fast rotation functions

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Spectroscopic analysis of benzylidene anabaseine complexes with acetylcholine binding proteins as models for ligand-nicotinic receptor interactions

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Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors.

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Processing of X-ray diffraction data collected in oscillation mode

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Identifiers

10.1021/JA3001858

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