X Espanel

Summary

Affiliation: Serono Pharmaceutical Research Institute
Country: Switzerland

Publications

  1. ncbi Yes-associated protein and p53-binding protein-2 interact through their WW and SH3 domains
    X Espanel
    Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York, New York 10029 6574, USA
    J Biol Chem 276:14514-23. 2001
  2. ncbi Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II
    A Chang
    Department of Biochemistry and Molecular Biology, New York University Mount Sinai School of Medicine, New York, New York 10029, USA
    J Biol Chem 275:20562-71. 2000
  3. ncbi The WW domain of dystrophin requires EF-hands region to interact with beta-dystroglycan
    S Rentschler
    Department of Biochemistry, Mount Sinai School of Medicine, New York, NY 10029, USA
    Biol Chem 380:431-42. 1999
  4. ncbi Pulling strings below the surface: hormone receptor signaling through inhibition of protein tyrosine phosphatases
    X Espanel
    Serono Pharmaceutical Research Institute, Geneva, Switzerland
    Endocrine 15:19-28. 2001

Collaborators

Detail Information

Publications4

  1. ncbi Yes-associated protein and p53-binding protein-2 interact through their WW and SH3 domains
    X Espanel
    Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York, New York 10029 6574, USA
    J Biol Chem 276:14514-23. 2001
    ..Since overexpression of an activated form of c-Yes resulted in tyrosine phosphorylation of p53BP-2, we propose that the p53BP-2 phosphorylation, possibly in the WW1 domain-binding motif, might negatively regulate the YAP.p53BP-2 complex...
  2. ncbi Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II
    A Chang
    Department of Biochemistry and Molecular Biology, New York University Mount Sinai School of Medicine, New York, New York 10029, USA
    J Biol Chem 275:20562-71. 2000
    ..In view of the recent data pertaining to phosphorylation-driven interactions between the RNA pol II CTD and the WW domain of Ess1/Pin1, we suggest that CTD dephosphorylation may be a prerequisite for targeted RNA pol II degradation...
  3. ncbi The WW domain of dystrophin requires EF-hands region to interact with beta-dystroglycan
    S Rentschler
    Department of Biochemistry, Mount Sinai School of Medicine, New York, NY 10029, USA
    Biol Chem 380:431-42. 1999
    ..Targeted mutagenesis of conserved WW domain residues reveals that the dystrophin/beta-dystroglycan interaction occurs primarily through the WW domain of dystrophin. Precise mapping of this interaction could aid in therapeutic design...
  4. ncbi Pulling strings below the surface: hormone receptor signaling through inhibition of protein tyrosine phosphatases
    X Espanel
    Serono Pharmaceutical Research Institute, Geneva, Switzerland
    Endocrine 15:19-28. 2001
    ..In the present review, we outline this new paradigm for therapeutic regulation of the insulin receptor and discuss evidence that hints at other specific receptor-PTP pairs...