Covalent modification of the nucleotide binding domains of cystic fibrosis transmembrane conductance regulator (Q42686651)

4 November 2017

title

Covalent modification of the nucleotide binding domains of cystic fibrosis transmembrane conductance regulator (English)

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4 November 2017

main subject

transmembrane protein

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cystic fibrosis

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author name string

J F Cotten

series ordinal

1

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4 November 2017

M J Welsh

series ordinal

2

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4 November 2017

language of work or name

English

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publication date

1 November 1998

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Journal of Biological Chemistry

4 November 2017

published in

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4 November 2017

volume

273

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4 November 2017

issue

48

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4 November 2017

page(s)

31873-31879

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The Cystic Fibrosis Transmembrane Conductance Regulator

4 November 2017

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Demonstration That CFTR Is a Chloride Channel by Alteration of Its Anion Selectivity

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Novel pore-lining residues in CFTR that govern permeation and open-channel block

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Nucleoside triphosphates are required to open the CFTR chloride channel.

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Regulation by ATP and ADP of CFTR chloride channels that contain mutant nucleotide-binding domains

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Coupling of CFTR Cl- channel gating to an ATP hydrolysis cycle

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Regulation of the gating of cystic fibrosis transmembrane conductance regulator C1 channels by phosphorylation and ATP hydrolysis

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The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity

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ATPase activity of the cystic fibrosis transmembrane conductance regulator

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Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity

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P-glycoprotein shows strong catalytic cooperativity between the two nucleotide sites.

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Sequence homologies between nucleotide binding regions of CFTR and G-proteins suggest structural and functional similarities

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Pyrophosphate stimulates wild-type and mutant cystic fibrosis transmembrane conductance regulator Cl- channels

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Two conformations of crystalline adenylate kinase

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Effect of ATP concentration on CFTR Cl- channels: a kinetic analysis of channel regulation

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Reactivity and pH dependence of thiol conjugation to N-ethylmaleimide: detection of a conformational change in chalcone isomerase.

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Altered drug-stimulated ATPase activity in mutants of the human multidrug resistance protein

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.48.31873

1 reference

4 November 2017

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