ABCC1 p.Cys7Ala
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PMID: 12235150
[PubMed]
Yang Y et al: "Structural and functional consequences of mutating cysteine residues in the amino terminus of human multidrug resistance-associated protein 1."
No.
Sentence
Comment
49
Engineering Human MRP1 Constructs-Mutations of Cys7 and Cys32 to Ala were generated using the TransformerTM site-directed mutagenesis kit (Clontech, Palo Alto, CA).
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ABCC1 p.Cys7Ala 12235150:49:47
status: NEW
PMID: 12731862
[PubMed]
Leslie EM et al: "Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1)."
No.
Sentence
Comment
222
Yang et al. (26) recently reported that when Cys7 and Cys32 in the extracellular NH2 terminus of MRP1 were replaced with Ala, the Cys7Ala but not the Cys32Ala mutant showed significant structural and functional changes.
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ABCC1 p.Cys7Ala 12731862:222:130
status: NEW224 However, in contrast to our findings with the seven Cys mutants examined here, LTC4 transport by Cys7Ala-MRP1 was reduced by more than 90%, providing indirect evidence that the structure of MRP1 was more disrupted in this mutant.
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ABCC1 p.Cys7Ala 12731862:224:97
status: NEW225 On the other hand, the apparent changes in Cys7Ala-MRP1 conformation resulted in little or no impairment of plasma membrane localization unlike several of the Cys-substituted mutants investigated here (26).
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ABCC1 p.Cys7Ala 12731862:225:43
status: NEW
PMID: 12948592
[PubMed]
Ito K et al: "Mutation of proline residues in the NH(2)-terminal region of the multidrug resistance protein, MRP1 (ABCC1): effects on protein expression, membrane localization, and transport function."
No.
Sentence
Comment
222
Consistent with this idea are the recent findings of Yang et al. [36] which showed that replacement of Cys7 with Ala caused an almost complete loss of LTC4 transport activity and a change in conformation of the NH2 terminus although expression levels and plasma membrane localization of this mutant MRP1 were not diminished compared to wild-type MRP1.
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ABCC1 p.Cys7Ala 12948592:222:103
status: NEW221 Consistent with this idea are the recent findings of Yang et al. [36] which showed that replacement of Cys7 with Ala caused an almost complete loss of LTC4 transport activity and a change in conformation of the NH2 terminus although expression levels and plasma membrane localization of this mutant MRP1 were not diminished compared to wild-type MRP1.
X
ABCC1 p.Cys7Ala 12948592:221:103
status: NEW