NMR Structure and Action on Nicotinic Acetylcholine Receptors of Water-soluble Domain of Human LYNX1
about
Mechanisms of inhibition and potentiation of α4β2 nicotinic acetylcholine receptors by members of the Ly6 protein familyFunctional interaction between Lypd6 and nicotinic acetylcholine receptors.SLEEPLESS is a bifunctional regulator of excitability and cholinergic synaptic transmissionSecreted Isoform of Human Lynx1 (SLURP-2): Spatial Structure and Pharmacology of Interactions with Different Types of Acetylcholine ReceptorsWater-soluble LYNX1 residues important for interaction with muscle-type and/or neuronal nicotinic receptors.Positive modulation of a Cys-loop acetylcholine receptor by an auxiliary transmembrane subunit.Lynx1 shifts α4β2 nicotinic receptor subunit stoichiometry by affecting assembly in the endoplasmic reticulum.Enhancement in motor learning through genetic manipulation of the Lynx1 gene.Ly6h regulates trafficking of alpha7 nicotinic acetylcholine receptors and nicotine-induced potentiation of glutamatergic signaling.Neural systems governed by nicotinic acetylcholine receptors: emerging hypotheses.Structural Analysis and Deletion Mutagenesis Define Regions of QUIVER/SLEEPLESS that Are Responsible for Interactions with Shaker-Type Potassium Channels and Nicotinic Acetylcholine Receptors.Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1) Is a Selective Allosteric Antagonist of α7 Nicotinic Acetylcholine Receptor.From toxins targeting ligand gated ion channels to therapeutic molecules.Natural compounds interacting with nicotinic acetylcholine receptors: from low-molecular weight ones to peptides and proteins.Structural Insight into Specificity of Interactions between Nonconventional Three-finger Weak Toxin from Naja kaouthia (WTX) and Muscarinic Acetylcholine Receptors.GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and thereby prevent lipoprotein lipase binding.Human SLURP-1 and SLURP-2 Proteins Acting on Nicotinic Acetylcholine Receptors Reduce Proliferation of Human Colorectal Adenocarcinoma HT-29 Cells.Deletion of lynx1 reduces the function of α6* nicotinic receptors.Interaction of Synthetic Human SLURP-1 with the Nicotinic Acetylcholine Receptors.Expression of the Ly-6 family proteins Lynx1 and Ly6H in the rat brain is compartmentalized, cell-type specific, and developmentally regulated.Isoform-specific mechanisms of α3β4*-nicotinic acetylcholine receptor modulation by the prototoxin lynx1.Human secreted proteins SLURP-1 and SLURP-2 control the growth of epithelial cancer cells via interactions with nicotinic acetylcholine receptors.Lynx1 Prevents Long-Term Potentiation Blockade and Reduction of Neuromodulator Expression Caused by Aβ1-42 and JNK Activation
P2860
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P2860
NMR Structure and Action on Nicotinic Acetylcholine Receptors of Water-soluble Domain of Human LYNX1
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
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2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@ast
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@en
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@nl
type
label
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@ast
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@en
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@nl
prefLabel
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@ast
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@en
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@nl
P2093
P2860
P921
P3181
P356
P1476
NMR Structure and Action on Ni ...... -soluble Domain of Human LYNX1
@en
P2093
Alexander S Arseniev
Alexandra P Krivolapova
Daniel Bertrand
Dieter D'Hoedt
Dmitry A Dolgikh
Ekaterina N Lyukmanova
Helena Janickova
Igor E Kasheverov
Konstantin S Mineev
Mikhail A Shulepko
P2860
P304
P3181
P356
10.1074/JBC.M110.189100
P407
P577
2011-03-25T00:00:00Z