Point mutations in dimerization motifs of the transmembrane domain stabilize active or inactive state of the EphA2 receptor tyrosine kinase.
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Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".Eph receptor and ephrin function in breast, gut, and skin epithelia.From Type I to Type II: Design, Synthesis, and Characterization of Potent Pyrazin-2-ones as DFG-Out Inhibitors of PDGFRβ.Dimerization of the EphA1 receptor tyrosine kinase transmembrane domain: Insights into the mechanism of receptor activation.A small peptide promotes EphA2 kinase-dependent signaling by stabilizing EphA2 dimers.A novel pH-dependent membrane peptide that binds to EphA2 and inhibits cell migration
P2860
Point mutations in dimerization motifs of the transmembrane domain stabilize active or inactive state of the EphA2 receptor tyrosine kinase.
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2014 nî lūn-bûn
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name
Point mutations in dimerizatio ...... phA2 receptor tyrosine kinase.
@en
Point mutations in dimerizatio ...... phA2 receptor tyrosine kinase.
@nl
type
label
Point mutations in dimerizatio ...... phA2 receptor tyrosine kinase.
@en
Point mutations in dimerizatio ...... phA2 receptor tyrosine kinase.
@nl
prefLabel
Point mutations in dimerizatio ...... phA2 receptor tyrosine kinase.
@en
Point mutations in dimerizatio ...... phA2 receptor tyrosine kinase.
@nl
P2093
P2860
P356
P1476
Point mutations in dimerizatio ...... EphA2 receptor tyrosine kinase
@en
P2093
Alexander S Arseniev
Alexey V Feofanov
Eduard V Bocharov
Maria V Astapova
Peter M Kolosov
P2860
P304
14955-14964
P356
10.1074/JBC.M114.558783
P407
P577
2014-04-14T00:00:00Z