ABCC7 p.Asp835Ala
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PMID: 20952391
[PubMed]
Wang G et al: "State-dependent regulation of cystic fibrosis transmembrane conductance regulator (CFTR) gating by a high affinity Fe3+ bridge between the regulatory domain and cytoplasmic loop 3."
No.
Sentence
Comment
132
Fig. 4, B and E, indicate that only D836A dramatically prevented inhibition by Fe3ϩ , whereas E822A, E826A, D828A, E831A, and D835A did not.
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ABCC7 p.Asp835Ala 20952391:132:132
status: NEW
PMID: 23060444
[PubMed]
Wang G et al: "Regulation of Activation and Processing of the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) by a Complex Electrostatic Interaction between the Regulatory Domain and Cytoplasmic Loop 3."
No.
Sentence
Comment
11
First, not only D835A, D836A and E838A but also K946A reduced the PKA dependent CFTR activation.
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ABCC7 p.Asp835Ala 23060444:11:16
status: NEW60 Similar observations with D835A and E838A were summarized in Fig. 2D. The K1/2 for PKA activation reduced from 10 units/ml to 5 units/ml once K946 from the CL3, and D835, D836 and E838 from NEG2 were mutated to alanines (Fig.2D).
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ABCC7 p.Asp835Ala 23060444:60:26
status: NEW138 First, the PKA sensitivity of channel activation was significantly enhanced for K946A, D835A, D836A and E838A mutants (Fig.2).
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ABCC7 p.Asp835Ala 23060444:138:87
status: NEW9 First, not only D835A, D836A, and E838A but also K946A reduced the PKA-dependent CFTR activation.
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ABCC7 p.Asp835Ala 23060444:9:16
status: NEW63 Similar observations with D835A and E838A are summarized in Fig. 2D.
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ABCC7 p.Asp835Ala 23060444:63:26
status: NEW167 First, the PKA sensitivity of channel activation was significantly enhanced for K946A, D835A, D836A, and E838A mutants (Fig. 2).
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ABCC7 p.Asp835Ala 23060444:167:87
status: NEW