C Freund

Summary

Affiliation: Harvard University
Country: USA

Publications

  1. ncbi The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences
    C Freund
    Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA
    Nat Struct Biol 6:656-60. 1999
  2. pmc Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation
    K Nishizawa
    Laboratory of Immunobiology, Dana Farber Cancer Institute, and Department of Medicine, Harvard Medical School, Boston, MA 02115, USA
    Proc Natl Acad Sci U S A 95:14897-902. 1998
  3. pmc SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55
    H Kang
    Dana Farber Cancer Institute and Departments of Medicine, Pathology and Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston MA 02115, USA
    EMBO J 19:2889-99. 2000
  4. ncbi Vsx1, a rapidly evolving paired-like homeobox gene expressed in cone bipolar cells
    R L Chow
    Program in Developmental Biology, The Research Institute, Hospital for Sick Children, 555 University Ave, Toronto, Ontario M5G 1X8, Canada
    Mech Dev 109:315-22. 2001
  5. doi Mutational analyses of c-FLIPR, the only murine short FLIP isoform, reveal requirements for DISC recruitment
    N Ueffing
    Institute of Molecular Medicine, University of Dusseldorf, Universitatsstrasse 1, Dusseldorf D 40225, Germany
    Cell Death Differ 15:773-82. 2008

Collaborators

  • C E Rudd
  • A Musacchio
  • N Ueffing
  • R L Chow
  • H Kang
  • R K├╝hne
  • E Keil
  • K Schulze-Osthoff
  • I Schmitz
  • G Wagner
  • K Nishizawa
  • B Snow
  • D Vidgen
  • J Looser
  • L Ploder
  • J Novak
  • R R McInnes
  • J S Duke-Cohan
  • J Li
  • E L Reinherz

Detail Information

Publications5

  1. ncbi The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences
    C Freund
    Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA
    Nat Struct Biol 6:656-60. 1999
    ..A hydrophobic surface patch is created by motif residues that are highly conserved among a variety of proteins from diverse eukaryotic species. Thus, the architecture of the GYF domain may be widely used in protein-protein associations...
  2. pmc Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation
    K Nishizawa
    Laboratory of Immunobiology, Dana Farber Cancer Institute, and Department of Medicine, Harvard Medical School, Boston, MA 02115, USA
    Proc Natl Acad Sci U S A 95:14897-902. 1998
    ..Hence, a proline-binding module distinct from SH3 and WW domains regulates protein-protein interactions...
  3. pmc SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55
    H Kang
    Dana Farber Cancer Institute and Departments of Medicine, Pathology and Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston MA 02115, USA
    EMBO J 19:2889-99. 2000
    ..Our findings extend the repertoire of SH3 domain binding motifs to include a tyrosine-based motif and demonstrate a regulatory role for this motif in receptor signaling...
  4. ncbi Vsx1, a rapidly evolving paired-like homeobox gene expressed in cone bipolar cells
    R L Chow
    Program in Developmental Biology, The Research Institute, Hospital for Sick Children, 555 University Ave, Toronto, Ontario M5G 1X8, Canada
    Mech Dev 109:315-22. 2001
    ....
  5. doi Mutational analyses of c-FLIPR, the only murine short FLIP isoform, reveal requirements for DISC recruitment
    N Ueffing
    Institute of Molecular Medicine, University of Dusseldorf, Universitatsstrasse 1, Dusseldorf D 40225, Germany
    Cell Death Differ 15:773-82. 2008
    ..Thus, despite the presence of similar tandem DEDs, viral and cellular FLIPs inhibit apoptosis by remarkably divergent mechanisms...