J E Schnitzer

Summary

Affiliation: Harvard University
Country: USA

Publications

  1. ncbi Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    J E Schnitzer
    Department of Pathology, Harvard Medical School, Beth Israel Hospital, Boston, MA 02215, USA
    Science 274:239-42. 1996
  2. ncbi Caveolae from luminal plasmalemma of rat lung endothelium: microdomains enriched in caveolin, Ca(2+)-ATPase, and inositol trisphosphate receptor
    J E Schnitzer
    Department of Pathology, Harvard Medical School, Beth Israel Hospital, Boston, MA 02215
    Proc Natl Acad Sci U S A 92:1759-63. 1995
  3. ncbi NEM inhibits transcytosis, endocytosis, and capillary permeability: implication of caveolae fusion in endothelia
    J E Schnitzer
    Department of Pathology, Harvard Medical School, Beth Israel Hospital, Boston, Massachusetts 02215
    Am J Physiol 268:H48-55. 1995

Detail Information

Publications3

  1. ncbi Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    J E Schnitzer
    Department of Pathology, Harvard Medical School, Beth Israel Hospital, Boston, MA 02215, USA
    Science 274:239-42. 1996
    ..Thus, caveolae may bud to form discrete carrier vesicles that participate in membrane trafficking...
  2. ncbi Caveolae from luminal plasmalemma of rat lung endothelium: microdomains enriched in caveolin, Ca(2+)-ATPase, and inositol trisphosphate receptor
    J E Schnitzer
    Department of Pathology, Harvard Medical School, Beth Israel Hospital, Boston, MA 02215
    Proc Natl Acad Sci U S A 92:1759-63. 1995
    ..1. The purified caveolae appeared to represent specific microdomains of the cell surface with their own unique molecular topography...
  3. ncbi NEM inhibits transcytosis, endocytosis, and capillary permeability: implication of caveolae fusion in endothelia
    J E Schnitzer
    Department of Pathology, Harvard Medical School, Beth Israel Hospital, Boston, Massachusetts 02215
    Am J Physiol 268:H48-55. 1995
    ..Like other vesicular pathways, endothelial caveolae transport their select ligands utilizing a NEM-sensitive mechanism, apparently requiring vesicle-membrane fusion...