Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity.
about
A region within a lumenal loop of Saccharomyces cerevisiae Ycf1p directs proteolytic processing and substrate specificity.Targeting xCT, a cystine-glutamate transporter induces apoptosis and tumor regression for KSHV/HIV-associated lymphomaRole of the NH2-terminal membrane spanning domain of multidrug resistance protein 1/ABCC1 in protein processing and traffickingMultidrug resistance protein 1 (MRP1, ABCC1), a "multitasking" ATP-binding cassette (ABC) transporter.xCT, not just an amino-acid transporter: a multi-functional regulator of microbial infection and associated diseasesThe MRP family of drug efflux pumps.Substrate recognition and transport by multidrug resistance protein 1 (ABCC1).Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.Functional analysis of nonsynonymous single nucleotide polymorphisms of multidrug resistance-associated protein 2 (ABCC2).Structure of a human multidrug transporter in an inward-facing conformation.Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1).Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transpArsenic transport by the human multidrug resistance protein 1 (MRP1/ABCC1). Evidence that a tri-glutathione conjugate is required.Nucleotides and transported substrates modulate different steps of the ATPase catalytic cycle of MRP1 multidrug transporter.Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity, and nucleotide interactions.Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to low affinity substrate binding staMultiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1.Identification of domains participating in the substrate specificity and subcellular localization of the multidrug resistance proteins MRP1 and MRP2.ATP and GSH dependence of MRP1-mediated outward translocation of phospholipid analogs in the human erythrocyte membrane.Single Nanoparticle Plasmonic Spectroscopy for Study of Charge-Dependent Efflux Function of Multidrug ABC Transporters of Single Live Bacillus subtilis Cells.
P2860
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P2860
Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity.
description
2002 nî lūn-bûn
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2002年の論文
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name
Charged amino acids in the six ...... minants of transport activity.
@en
Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1
@nl
type
label
Charged amino acids in the six ...... minants of transport activity.
@en
Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1
@nl
prefLabel
Charged amino acids in the six ...... minants of transport activity.
@en
Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1
@nl
P2860
P921
P356
P1476
Charged amino acids in the six ...... minants of transport activity.
@en
P2093
Anass Haimeur
Roger G Deeley
P2860
P304
41326-41333
P356
10.1074/JBC.M206228200
P407
P50
P577
2002-08-18T00:00:00Z