Locating a plausible binding site for an open-channel blocker, GlyH-101, in the pore of the cystic fibrosis transmembrane conductance regulator. (Q36412828)

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English	Locating a plausible binding site for an open-channel blocker, GlyH-101, in the pore of the cystic fibrosis transmembrane conductance regulator.	scientific article

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scholarly article

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12 February 2020

Locating a plausible binding site for an open-channel blocker, GlyH-101, in the pore of the cystic fibrosis transmembrane conductance regulator (English)

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12 February 2020

transmembrane protein

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cystic fibrosis

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Mark S.P. Sansom

6

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12 February 2020

author name string

Yohei Norimatsu

1

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12 February 2020

Anthony Ivetac

2

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12 February 2020

Christopher Alexander

3

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12 February 2020

Nicolette O'Donnell

4

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12 February 2020

Leah Frye

5

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12 February 2020

David C Dawson

7

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12 February 2020

publication date

24 August 2012

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12 February 2020

Molecular Pharmacology

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12 February 2020

82

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12 February 2020

1042-1055

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12 February 2020

6

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12 February 2020

Structure-based drug screening for G-protein-coupled receptors

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30 September 2017

Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore

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Alternating access to the transmembrane domain of the ATP-binding cassette protein cystic fibrosis transmembrane conductance regulator (ABCC7).

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In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer

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CFTR: Ligand exchange between a permeant anion ([Au(CN)2]-) and an engineered cysteine (T338C) blocks the pore

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Substituted-cysteine accessibility method

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Analysis of the binding of hydroxamic acid and carboxylic acid inhibitors to the stromelysin-1 (matrix metalloproteinase-3) catalytic domain by isothermal titration calorimetry

1 reference

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Identifiers

10.1124/MOL.112.080267

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12 February 2020

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12 February 2020

1 reference

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12 February 2020

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