articleTop 1% cited
FAK–Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
Nature Cell Biology · 2004 · Vol. 6(2) · pp. 154–161
Donna J. Webb✉(University of Virginia)Karen Donais(University of Virginia)Leanna Whitmore(University of Virginia)Sheila Μ. Thomas(Center for Cancer Research)Christopher E. Turner(SUNY Upstate Medical University)J. Thomas Parsons(University of Virginia)Alan F. Horwitz(University of Virginia)
Cell Adhesion Molecules ResearchCellular Mechanics and InteractionsWnt/β-catenin signaling in development and cancerPaxillinFocal adhesionCell biologyProto-oncogene tyrosine-protein kinase SrcCell adhesionMyosin light-chain kinaseKinaseAdhesionPTK2Cell adhesion molecule
MeSH terms
AnimalsCell AdhesionCell MovementCytoskeletal ProteinsFibroblastsMyosin-Light-Chain KinasePhosphoproteinsProtein-Tyrosine KinasesProteinsRecombinant Fusion ProteinsSignal Transductionsrc-Family KinasesMitogen-Activated Protein KinasesAdaptor Proteins, Vesicular TransportRetinoblastoma-Like Protein p130
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References
Autophosphorylation of the Focal Adhesion Kinase, ppl25<sup>FAK</sup>, Directs SH2-Dependent Binding of pp60<i><sup>src</sup></i>
Molecular and Cellular Biology · 1994 · 1,144 citations
Rho GTPases and cell migration
Journal of Cell Science · 2001 · 1,193 citations
Molecular complexity and dynamics of cell-matrix adhesions
Journal of Cell Science · 2001 · 1,094 citations
Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src.
Molecular and Cellular Biology · 1994 · 868 citations
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