The Walker B motif of the second nucleotide-binding domain (NBD2) of CFTR plays a key role in ATPase activity by the NBD1-NBD2 heterodimer. - Wikidata - awgldk - TriplyDB

The Walker B motif of the second nucleotide-binding domain (NBD2) of CFTR plays a key role in ATPase activity by the NBD1-NBD2 heterodimer.

The Walker B motif of the second nucleotide-binding domain (NBD2) of CFTR plays a key role in ATPase activity by the NBD1-NBD2 heterodimer.

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Requirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved Sequences CFTR and TNR-CFTR expression and function in the kidney.The H-loop in the second nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator is required for efficient chloride channel closing A single amino acid substitution in CFTR converts ATP to an inhibitory ligand.The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.ATP induces conformational changes in the carboxyl-terminal region of ClC-5 Neonatal Diabetes and Congenital Hyperinsulinism Caused by Mutations in ABCC8/SUR1 are Associated with Altered and Opposite Affinities for ATP and ADP Functional Relationship of ATP Hydrolysis, Presynaptic Filament Stability, and Homologous DNA Pairing Activity of the Human Meiotic Recombinase DMC1.Molecular modelling and molecular dynamics of CFTR.The CFTR ion channel: gating, regulation, and anion permeation Nonequilibrium gating of CFTR on an equilibrium theme.State-dependent modulation of CFTR gating by pyrophosphate.Gating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerisation.Conformational changes opening and closing the CFTR chloride channel: insights from cysteine scanning mutagenesis.Current insights into the role of PKA phosphorylation in CFTR channel activity and the pharmacological rescue of cystic fibrosis disease-causing mutants.Regulation of conductance by the number of fixed positive charges in the intracellular vestibule of the CFTR chloride channel pore.CFTR structure and function: is there a role in the kidney?The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor.Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.The NBDs that wouldn't die: A cautionary tale of the use of isolated nucleotide binding domains of ABC transporters.Conformational changes in a pore-lining helix coupled to cystic fibrosis transmembrane conductance regulator channel gating.A common mechanism for CFTR potentiators.Sites associated with Kalydeco binding on human Cystic Fibrosis Transmembrane Conductance Regulator revealed by Hydrogen/Deuterium Exchange.

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P2860

The Walker B motif of the second nucleotide-binding domain (NBD2) of CFTR plays a key role in ATPase activity by the NBD1-NBD2 heterodimer.

http://www.wikidata.org/entity/Q42072546

description

2007 nî lūn-bûn

@nan

2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

@zh-sg

2007年學術文章

@yue

2007年學術文章

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2007年學術文章

@zh-hant

name

The Walker B motif of the seco ...... by the NBD1-NBD2 heterodimer.

@en

The Walker B motif of the second nucleotide-binding domain

@nl

type

label

The Walker B motif of the seco ...... by the NBD1-NBD2 heterodimer.

@en

The Walker B motif of the second nucleotide-binding domain

@nl

prefLabel

The Walker B motif of the seco ...... by the NBD1-NBD2 heterodimer.

@en

The Walker B motif of the second nucleotide-binding domain

@nl

P1433

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P1433

Biochemical Journal

P1476

The Walker B motif of the seco ...... by the NBD1-NBD2 heterodimer.

@en

P2093

Christine E Bear

http://www.w3.org/2001/XMLSchema#string

Fiona L L Stratford

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Joanne C Cheung

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Ling-Jun Huan

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Mohabir Ramjeesingh

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P2860

H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB

Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters

The ABC protein turned chloride channel whose failure causes cystic fibrosis

Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily

The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism

Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator)

Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA

Structural biology. The xyz of ABC transporters

Cystic fibrosis

ATPase activity of the cystic fibrosis transmembrane conductance regulator

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581-586

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scholarly article

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10.1042/BJ20060968

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2

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401

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16989640

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1820796

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