Nucleotide occlusion in the human cystic fibrosis transmembrane conductance regulator. Different patterns in the two nucleotide binding domains.
about
A spectrum of ABCC6 mutations is responsible for pseudoxanthoma elasticumThe ABC protein turned chloride channel whose failure causes cystic fibrosisCFTR gating II: Effects of nucleotide binding on the stability of open statesCFTR gating I: Characterization of the ATP-dependent gating of a phosphorylation-independent CFTR channel (DeltaR-CFTR).ATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1)Role of the N-terminal transmembrane domain in the endo-lysosomal targeting and function of the human ABCB6 protein.ATP and AMP mutually influence their interaction with the ATP-binding cassette (ABC) adenylate kinase cystic fibrosis transmembrane conductance regulator (CFTR) at separate binding sites.The DrrAB efflux system of Streptomyces peucetius is a multidrug transporter of broad substrate specificityNormal gating of CFTR requires ATP binding to both nucleotide-binding domains and hydrolysis at the second nucleotide-binding domain.The H-loop in the second nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator is required for efficient chloride channel closingADP inhibits function of the ABC transporter cystic fibrosis transmembrane conductance regulator via its adenylate kinase activity.Mutations in the linker domain of NBD2 of SUR inhibit transduction but not nucleotide bindingTrapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport.A single amino acid substitution in CFTR converts ATP to an inhibitory ligand.Cysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels.Molecular diagnosis of ATP-binding cassette transporter-related diseases.Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP).On the mechanism of MgATP-dependent gating of CFTR Cl- channelsProlonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating.Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.Characterization of the adenosinetriphosphatase and transport activities of purified cystic fibrosis transmembrane conductance regulator.CLC-0 and CFTR: chloride channels evolved from transporters.State-dependent modulation of CFTR gating by pyrophosphate.Regulation of CFTR Cl- channel gating by ATP binding and hydrolysis.Molecular modeling of the heterodimer of human CFTR's nucleotide-binding domains using a protein-protein docking approachVanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis.Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motifIn vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer.Attempts to characterize the NBD heterodimer of MRP1: transient complex formation involves Gly771 of the ABC signature sequence but does not enhance the intrinsic ATPase activity.Degenerate ABC composite site is stably glued together by trapped ATP.The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover.The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics.Tandem function of nucleotide binding domains confers competence to sulfonylurea receptor in gating ATP-sensitive K+ channels.A combined analysis of the cystic fibrosis transmembrane conductance regulator: implications for structure and disease models.
P2860
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P2860
Nucleotide occlusion in the human cystic fibrosis transmembrane conductance regulator. Different patterns in the two nucleotide binding domains.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Nucleotide occlusion in the hu ...... wo nucleotide binding domains.
@en
Nucleotide occlusion in the hu ...... wo nucleotide binding domains.
@nl
type
label
Nucleotide occlusion in the hu ...... wo nucleotide binding domains.
@en
Nucleotide occlusion in the hu ...... wo nucleotide binding domains.
@nl
prefLabel
Nucleotide occlusion in the hu ...... wo nucleotide binding domains.
@en
Nucleotide occlusion in the hu ...... wo nucleotide binding domains.
@nl
P2093
P2860
P356
P1476
Nucleotide occlusion in the hu ...... wo nucleotide binding domains.
@en
P2093
P2860
P304
12209-12212
P356
10.1074/JBC.274.18.12209
P407
P577
1999-04-01T00:00:00Z