The strong dimerization of the transmembrane domain of the fibroblast growth factor receptor (FGFR) is modulated by C-terminal juxtamembrane residues.
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Left-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine KinasesStructure of FGFR3 Transmembrane Domain Dimer: Implications for Signaling and Human PathologiesStructure elucidation of dimeric transmembrane domains of bitopic proteinsUnderstanding cytokine and growth factor receptor activation mechanisms.Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?Virion-associated viral fibroblast growth factor stimulates cell motilitySelf-association of models of transmembrane domains of ErbB receptors in a lipid bilayerPrimary and secondary dimer interfaces of the fibroblast growth factor receptor 3 transmembrane domain: characterization via multiscale molecular dynamics simulations.
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The strong dimerization of the transmembrane domain of the fibroblast growth factor receptor (FGFR) is modulated by C-terminal juxtamembrane residues.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on February 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The strong dimerization of the ...... rminal juxtamembrane residues.
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The strong dimerization of the ...... roblast growth factor receptor
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label
The strong dimerization of the ...... rminal juxtamembrane residues.
@en
The strong dimerization of the ...... roblast growth factor receptor
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prefLabel
The strong dimerization of the ...... rminal juxtamembrane residues.
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The strong dimerization of the ...... roblast growth factor receptor
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P2860
P356
P1433
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The strong dimerization of the ...... rminal juxtamembrane residues.
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P2093
Weng Chuan Peng
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P304
P356
10.1002/PRO.65
P50
P577
2009-02-01T00:00:00Z