Affiliation: Harvard University
- The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequencesC 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...
- Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activationK 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...
- SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55H 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...
- Vsx1, a rapidly evolving paired-like homeobox gene expressed in cone bipolar cellsR 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....
- Mutational analyses of c-FLIPR, the only murine short FLIP isoform, reveal requirements for DISC recruitmentN 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...