F K Chan

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. pmc The pre-ligand binding assembly domain: a potential target of inhibition of tumour necrosis factor receptor function
    F K Chan
    Building 10, Room 11N311, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 1892, USA
    Ann Rheum Dis 59:i50-3. 2000
  2. ncbi request reprint Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations
    R M Siegel
    Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 288:2354-7. 2000
  3. ncbi request reprint The multifaceted role of Fas signaling in immune cell homeostasis and autoimmunity
    R M Siegel
    Laboratory of Immunology, National Institutes of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 1892, USA
    Nat Immunol 1:469-74. 2000
  4. ncbi request reprint Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein
    F K Chan
    Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-1892, USA
    Cytometry 44:361-8. 2001
  5. ncbi request reprint A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling
    F K Chan
    Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 288:2351-4. 2000

Collaborators

  • D A Zacharias
  • R M Siegel
  • M J Lenardo
  • D Lynch
  • M Johnson
  • H J Chun
  • J K Frederiksen
  • R Y Tsien

Detail Information

Publications5

  1. pmc The pre-ligand binding assembly domain: a potential target of inhibition of tumour necrosis factor receptor function
    F K Chan
    Building 10, Room 11N311, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 1892, USA
    Ann Rheum Dis 59:i50-3. 2000
    ....
  2. ncbi request reprint Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations
    R M Siegel
    Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 288:2354-7. 2000
    ..These results show that formation of preassociated receptor complexes is necessary for Fas signaling and dominant interference in human disease...
  3. ncbi request reprint The multifaceted role of Fas signaling in immune cell homeostasis and autoimmunity
    R M Siegel
    Laboratory of Immunology, National Institutes of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 1892, USA
    Nat Immunol 1:469-74. 2000
    ..Proximal signaling by Fas and related receptors depends on subunit preassembly, which accounts for the dominant-negative effect of pathogenic receptor mutants and natural splice variants...
  4. ncbi request reprint Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein
    F K Chan
    Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-1892, USA
    Cytometry 44:361-8. 2001
    ..Moreover, flow cytometry allows quantitative analyses to be carried out on a cell-by-cell basis on large number of cells. Published 2001 Wiley-Liss, Inc...
  5. ncbi request reprint A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling
    F K Chan
    Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 288:2351-4. 2000
    ..Thus, TNFRs and related receptors appear to function as preformed complexes rather than as individual receptor subunits that oligomerize after ligand binding...