B J Mayer

Summary

Affiliation: Harvard University
Country: USA

Publications

  1. ncbi request reprint Protein-protein interactions in signaling cascades
    B J Mayer
    Howard Hughes Medical Institute, Children s Hospital, Boston, MA, USA
    Mol Biotechnol 13:201-13. 1999
  2. ncbi request reprint Signal transduction: clamping down on Src activity
    B J Mayer
    Howard Hughes Medical Institute, Children s Hospital, Department of Microbiology and Molecular Genetics, Harvard Medical School, 320 Longwood Avenue, Boston, Massachusetts 02115, USA
    Curr Biol 7:R295-8. 1997
  3. ncbi request reprint Endocytosis: EH domains lend a hand
    B J Mayer
    Howard Hughes Medical Institute, Children s Hospital, Department of Microbiology, Harvard Medical School, 300 Longwood Avenue, Boston, Massachusetts, 02115, USA
    Curr Biol 9:R70-3. 1999
  4. ncbi request reprint Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor
    T Miyoshi-Akiyama
    Laboratory of Molecular Medicine, Children s Hospital and Department of Microbiology and Molecular Genetics, Harvard Medical School, 300 Longwood Avenue, Boston, Massachusetts, MA 02115, USA
    Oncogene 20:4058-69. 2001
  5. pmc Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins
    M Tanaka
    Howard Hughes Medical Institute, Children s Hospital, Boston, Massachusetts 02115, USA
    Mol Cell Biol 15:6829-37. 1995
  6. ncbi request reprint Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
    R Rohatgi
    Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA
    J Biol Chem 276:26448-52. 2001
  7. pmc Profiling the global tyrosine phosphorylation state by Src homology 2 domain binding
    P Nollau
    Laboratory of Molecular Medicine, Children's Hospital, Boston, MA 02115, USA
    Proc Natl Acad Sci U S A 98:13531-6. 2001
  8. ncbi request reprint Abl family kinases and Cbl cooperate with the Nck adaptor to modulate Xenopus development
    C E Adler
    Laboratory of Molecular Medicine, Children s Hospital and Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA
    J Biol Chem 275:36472-8. 2000
  9. ncbi request reprint Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    M Lei
    Laboratory of Molecular Medicine, Children s Hospital, Boston, Massachusetts 02115, USA
    Cell 102:387-97. 2000
  10. ncbi request reprint Cdc42 is required for PIP(2)-induced actin polymerization and early development but not for cell viability
    F Chen
    Departments of Genetics, The Center for Blood Research, Harvard Medical School, Boston, MA 02115, USA
    Curr Biol 10:758-65. 2000

Detail Information

Publications12

  1. ncbi request reprint Protein-protein interactions in signaling cascades
    B J Mayer
    Howard Hughes Medical Institute, Children s Hospital, Boston, MA, USA
    Mol Biotechnol 13:201-13. 1999
    ..In this overview a variety of protein interaction modules are discussed, and issues relating to binding specificity and the significance of a particular interaction are considered...
  2. ncbi request reprint Signal transduction: clamping down on Src activity
    B J Mayer
    Howard Hughes Medical Institute, Children s Hospital, Department of Microbiology and Molecular Genetics, Harvard Medical School, 320 Longwood Avenue, Boston, Massachusetts 02115, USA
    Curr Biol 7:R295-8. 1997
    ....
  3. ncbi request reprint Endocytosis: EH domains lend a hand
    B J Mayer
    Howard Hughes Medical Institute, Children s Hospital, Department of Microbiology, Harvard Medical School, 300 Longwood Avenue, Boston, Massachusetts, 02115, USA
    Curr Biol 9:R70-3. 1999
    ..The three-dimensional structure of an EH domain has recently been solved, and is likely to presage significant advances in understanding molecular mechanisms of endocytosis...
  4. ncbi request reprint Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor
    T Miyoshi-Akiyama
    Laboratory of Molecular Medicine, Children s Hospital and Department of Microbiology and Molecular Genetics, Harvard Medical School, 300 Longwood Avenue, Boston, Massachusetts, MA 02115, USA
    Oncogene 20:4058-69. 2001
    ..Studies with Nck mutants suggested that the Nck SH2 domain is responsible for inhibiting the activity of Abl toward both Cbl and Nck itself, most likely by competing with the Abl SH2 for tyrosine-phosphorylated binding sites...
  5. pmc Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins
    M Tanaka
    Howard Hughes Medical Institute, Children s Hospital, Boston, Massachusetts 02115, USA
    Mol Cell Biol 15:6829-37. 1995
    ..Dominant-negative adaptors provide a novel means to identify binding interactions important in vivo for signaling in response to a variety of stimuli...
  6. ncbi request reprint Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
    R Rohatgi
    Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA
    J Biol Chem 276:26448-52. 2001
    ..These results suggest the existence of an Nck-dependent, Cdc42-independent mechanism to induce actin polymerization at tyrosine-phosphorylated Nck binding sites...
  7. pmc Profiling the global tyrosine phosphorylation state by Src homology 2 domain binding
    P Nollau
    Laboratory of Molecular Medicine, Children's Hospital, Boston, MA 02115, USA
    Proc Natl Acad Sci U S A 98:13531-6. 2001
    ..The general strategy we describe here is not limited to Src homology 2 domains and could be used to profile the binding sites for any class of protein interaction domain...
  8. ncbi request reprint Abl family kinases and Cbl cooperate with the Nck adaptor to modulate Xenopus development
    C E Adler
    Laboratory of Molecular Medicine, Children s Hospital and Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA
    J Biol Chem 275:36472-8. 2000
    ..These results suggest a role for both Cbl and Abl family kinases in patterning the Xenopus embryo...
  9. ncbi request reprint Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    M Lei
    Laboratory of Molecular Medicine, Children s Hospital, Boston, Massachusetts 02115, USA
    Cell 102:387-97. 2000
    ..GTPase binding will refold part of the IS domain and unfold the rest. A related switch has been seen in the Wiskott-Aldrich syndrome protein (WASP)...
  10. ncbi request reprint Cdc42 is required for PIP(2)-induced actin polymerization and early development but not for cell viability
    F Chen
    Departments of Genetics, The Center for Blood Research, Harvard Medical School, Boston, MA 02115, USA
    Curr Biol 10:758-65. 2000
    ..Also, whereas genetic analyses have shown that Cdc42 is essential for cell viability in yeast, its potential roles in the growth and development of mammalian cells have not been directly assessed...
  11. ncbi request reprint Concentration-dependent positive and negative regulation of a MAP kinase by a MAP kinase kinase
    M W Kieran
    Division of Hematology Oncology, Howard Hughes Medical Institute, Children s Hospital, Boston, MA 02115, USA
    Oncogene 18:6647-57. 1999
    ..These results reveal a potential mechanism for regulating stress-activated kinases, adding to a growing body of evidence suggesting that MAP kinases are controlled by relatively stable interactions with their activators...
  12. pmc NS5A, a nonstructural protein of hepatitis C virus, binds growth factor receptor-bound protein 2 adaptor protein in a Src homology 3 domain/ligand-dependent manner and perturbs mitogenic signaling
    S L Tan
    Department of Microbiology, School of Medicine, University of Washington, Seattle, WA 98195, USA
    Proc Natl Acad Sci U S A 96:5533-8. 1999
    ..Therefore, NS5A may function to perturb Grb2-mediated signaling pathways by selectively targeting the adaptor. These findings highlight a viral interceptor of cellular signaling with potential implications for HCV pathogenesis...