ABCC7 p.Ser222Ala
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PMID: 11888281
[PubMed]
Partridge AW et al: "Polar residues in membrane domains of proteins: molecular basis for helix-helix association in a mutant CFTR transmembrane segment."
No.
Sentence
Comment
82
For example, the point mutations Q220A, S222A, F224A, and F229A each resulted in species patterns with a more heavily populated dimer band versus the higher order oligomer bands.
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ABCC7 p.Ser222Ala 11888281:82:40
status: NEW
PMID: 15304546
[PubMed]
Sugita M et al: "Molecular dissection of the butyrate action revealed the involvement of mitogen-activated protein kinase in cystic fibrosis transmembrane conductance regulator biogenesis."
No.
Sentence
Comment
215
In the present study, LA- SDSE-MAPKK, in which Leu33 , Leu37 , Ser218 , and Ser222 were replaced by Ala, Ala, Asp, and Glu, respectively, was used as the constitutively active mutant (Fukuda et al., 1997).
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ABCC7 p.Ser222Ala 15304546:215:76
status: NEW234 We also checked the effect of cotransfection of the dominant-negative construct SASA-MAPKK, in which Ser218 and Ser222 were replaced by Ala (Gotoh et al., 1999); however, the cellular levels of active ERK/MAPKK were significantly reduced by CFTR transfection (Fig. 7A).
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ABCC7 p.Ser222Ala 15304546:234:112
status: NEW