(Q54155070)

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Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of alpha-helical peptide hydrogens in the nicotinic acetylcholine receptor.

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7493938%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of alpha-helical peptide hydrogens in the nicotinic acetylcholine receptor (English)

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7493938%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

1

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7493938%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

author name string

N Méthot

2

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7493938%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

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1 December 1995

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7493938%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

Journal of Biological Chemistry

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7493938%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

270

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19 October 2019

49

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19 October 2019

29129-29137

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7493938%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

Functional architecture of the nicotinic acetylcholine receptor: from electric organ to brain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

The permeation pathway of neurotransmitter-gated ion channels

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Structure of nicotinic acetylcholine receptors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Structural homology of Torpedo californica acetylcholine receptor subunits

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Nucleotide and deduced amino acid sequences of Torpedo californica acetylcholine receptor gamma subunit

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Acetylcholine receptor channel structure probed in cysteine-substitution mutants.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

FTIR analysis of nicotinic acetylcholine receptor secondary structure in reconstituted membranes.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Threonine in the selectivity filter of the acetylcholine receptor channel

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

An open-channel blocker interacts with adjacent turns of α-helices in the nicotinic acetylcholine receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Secondary structure of the nicotinic acetylcholine receptor: implications for structural models of a ligand-gated ion channel.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Incorporation of the nicotinic acetylcholine receptor into planar multilamellar films: characterization by fluorescence and Fourier transform infrared difference spectroscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Probing conformational changes in the nicotinic acetylcholine receptor by Fourier transform infrared difference spectroscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Hydrogen exchange

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

The hydrophobic heart of rhodopsin revealed by an infrared1H2H exchange study

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Conformation of acetylcholine receptor in the presence of agonists and antagonists

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Beta-structure in the membrane-spanning part of the nicotinic acetylcholine receptor (or how helical are transmembrane helices?).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: an FTIR study.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

Acetylcholine receptor channel imaged in the open state

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.49.29129

21 January 2018

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