The A391E mutation enhances FGFR3 activation in the absence of ligand.
about
Multiple consequences of a single amino acid pathogenic RTK mutation: the A391E mutation in FGFR3Characterization of membrane protein interactions in plasma membrane derived vesicles with quantitative imaging Förster resonance energy transferEffect of the G375C and G346E achondroplasia mutations on FGFR3 activation.Pathogenic Cysteine Removal Mutations in FGFR Extracellular Domains Stabilize Receptor Dimers and Perturb the TM Dimer Structure.High-throughput selection of transmembrane sequences that enhance receptor tyrosine kinase activationCoupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET.p38 Inhibition ameliorates skin and skull abnormalities in Fgfr2 Beare-Stevenson mice.FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.Physical-chemical principles underlying RTK activation, and their implications for human disease.The safety dance: biophysics of membrane protein folding and misfolding in a cellular contextSpectrum of genomic alterations in FGFR3: current appraisal of the potential role of FGFR3 in advanced urothelial carcinoma.The physical basis of FGFR3 response to fgf1 and fgf2.A Decade of FGF Receptor Research in Bladder Cancer: Past, Present, and Future Challenges.Effect of the achondroplasia mutation on FGFR3 dimerization and FGFR3 structural response to fgf1 and fgf2: A quantitative FRET study in osmotically derived plasma membrane vesicles.Mechanism of FGF receptor dimerization and activation.Structural differences between thermophilic and mesophilic membrane proteins.The pathogenic A391E mutation in FGFR3 induces a structural change in the transmembrane domain dimer.FGFR3 biology and skeletal disease.
P2860
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P2860
The A391E mutation enhances FGFR3 activation in the absence of ligand.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
The A391E mutation enhances FGFR3 activation in the absence of ligand.
@en
The A391E mutation enhances FGFR3 activation in the absence of ligand.
@nl
type
label
The A391E mutation enhances FGFR3 activation in the absence of ligand.
@en
The A391E mutation enhances FGFR3 activation in the absence of ligand.
@nl
prefLabel
The A391E mutation enhances FGFR3 activation in the absence of ligand.
@en
The A391E mutation enhances FGFR3 activation in the absence of ligand.
@nl
P2093
P2860
P1476
The A391E mutation enhances FGFR3 activation in the absence of ligand.
@en
P2093
Catherine Degnin
Fenghao Chen
Melanie Laederich
William A Horton
P2860
P304
P356
10.1016/J.BBAMEM.2011.04.007
P577
2011-04-22T00:00:00Z