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May 1, 1995Molecular and Cellular BiologyOpen Access

pp125 FAK -Dependent Tyrosine Phosphorylation of Paxillin Creates a High-Affinity Binding Site for Crk

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MSMichael D. SchallerWest Virginia UniversityJPJ. Thomas ParsonsFundación Juan March

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Schaller et al. (1995) studied this question.

synapsesocial.com/papers/6a6ffc615d37378ac1dd0abfhttps://doi.org/10.1128/mcb.15.5.2635
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak- binding region1994 · 314 citations
  2. 2Tyrosine phosphorylation of the focal adhesion kinase pp125FAK during development: relation to paxillin1993 · 138 citations
  3. 3Adaptor plasmids simplify the insertion of foreign DNA into helper-independent retroviral vectors1987 · 643 citations
  4. 4Integrins and other cell adhesion molecules1990 · 1,974 citations
  5. 5Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.1994 · 224 citations