E S Trombetta

Summary

Affiliation: Yale University
Country: USA

Publications

  1. ncbi request reprint Quality control and protein folding in the secretory pathway
    E Sergio Trombetta
    Department of Cell Biology, Yale University School of Medicine, PO Box 208002, New Haven, Connecticut 06520 8002, USA
    Annu Rev Cell Dev Biol 19:649-76. 2003
  2. ncbi request reprint Glycoprotein reglucosylation
    E Sergio Trombetta
    Department of Cell Biology, Yale University School of Medicine, P O Box 208002, New Haven, CT 06520 8002, USA
    Methods 35:328-37. 2005
  3. ncbi request reprint The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis
    E Sergio Trombetta
    Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, CT 06520, USA
    Glycobiology 13:77R-91R. 2003
  4. ncbi request reprint Cell biology of antigen processing in vitro and in vivo
    E Sergio Trombetta
    Department of Cell Biology and Section of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, Connecticut 06520 8002, USA
    Annu Rev Immunol 23:975-1028. 2005
  5. ncbi request reprint Quaternary and domain structure of glycoprotein processing glucosidase II
    E S Trombetta
    Department of Cell Biology, Yale University School of Medicine, P O Box 208002, New Haven, Connecticut 06520 8002, USA
    Biochemistry 40:10717-22. 2001
  6. pmc Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulum
    E S Trombetta
    Department of Cell Biology, Yale Medical School, PO Box 208002, New Haven, CT 06520 8002, USA
    EMBO J 18:3282-92. 1999
  7. ncbi request reprint Lectins as chaperones in glycoprotein folding
    E S Trombetta
    Department of Cell Biology, Yale Medical School, New Haven, CT 06520 8002, USA
    Curr Opin Struct Biol 8:587-92. 1998
  8. pmc Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum
    E S Trombetta
    Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520 8002, USA
    J Cell Biol 148:1123-29. 2000
  9. ncbi request reprint Activation of lysosomal function during dendritic cell maturation
    E Sergio Trombetta
    Department of Cell Biology and Department of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520 8002, USA
    Science 299:1400-3. 2003
  10. ncbi request reprint Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
    Lelia Delamarre
    Department of Cell Biology and Department of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520 8002, USA
    Science 307:1630-4. 2005

Collaborators

Detail Information

Publications16

  1. ncbi request reprint Quality control and protein folding in the secretory pathway
    E Sergio Trombetta
    Department of Cell Biology, Yale University School of Medicine, PO Box 208002, New Haven, Connecticut 06520 8002, USA
    Annu Rev Cell Dev Biol 19:649-76. 2003
    ..In other cases, pathology arises from the downregulation of mutated but potentially functional proteins that are retained and degraded by the QC system...
  2. ncbi request reprint Glycoprotein reglucosylation
    E Sergio Trombetta
    Department of Cell Biology, Yale University School of Medicine, P O Box 208002, New Haven, CT 06520 8002, USA
    Methods 35:328-37. 2005
    ....
  3. ncbi request reprint The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis
    E Sergio Trombetta
    Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, CT 06520, USA
    Glycobiology 13:77R-91R. 2003
    ..Processing of N-linked oligosaccharides begins in the ER and participates in glycoprotein folding and assembly. The elucidation of N-glycan processing mechanisms in the ER is uncovering their role in glycoprotein biosynthesis...
  4. ncbi request reprint Cell biology of antigen processing in vitro and in vivo
    E Sergio Trombetta
    Department of Cell Biology and Section of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, Connecticut 06520 8002, USA
    Annu Rev Immunol 23:975-1028. 2005
    ..How dendritic cells handle antigens is likely to be as important a determinant of immunogenicity and tolerance as is the nature of the antigens themselves...
  5. ncbi request reprint Quaternary and domain structure of glycoprotein processing glucosidase II
    E S Trombetta
    Department of Cell Biology, Yale University School of Medicine, P O Box 208002, New Haven, Connecticut 06520 8002, USA
    Biochemistry 40:10717-22. 2001
    ..Through its C-terminal HDEL signal, the beta subunit may retain the complete alpha(1)beta(1) complex in the ER...
  6. pmc Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulum
    E S Trombetta
    Department of Cell Biology, Yale Medical School, PO Box 208002, New Haven, CT 06520 8002, USA
    EMBO J 18:3282-92. 1999
    ..By eliminating UDP, which is an inhibitory product of the UDP-Glc:glycoprotein glucosyltransferase, it is likely to promote reglucosylation reactions involved in glycoprotein folding and quality control in the ER...
  7. ncbi request reprint Lectins as chaperones in glycoprotein folding
    E S Trombetta
    Department of Cell Biology, Yale Medical School, New Haven, CT 06520 8002, USA
    Curr Opin Struct Biol 8:587-92. 1998
    ....
  8. pmc Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum
    E S Trombetta
    Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520 8002, USA
    J Cell Biol 148:1123-29. 2000
    ..The findings suggest that discrete populations of nonnative conformations are selectively reglucosylated to participate in the calnexin/calreticulin chaperone pathway...
  9. ncbi request reprint Activation of lysosomal function during dendritic cell maturation
    E Sergio Trombetta
    Department of Cell Biology and Department of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520 8002, USA
    Science 299:1400-3. 2003
    ..Lysosomal function in DCs thus appears to be specialized for the developmentally regulated processing of internalized antigens...
  10. ncbi request reprint Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
    Lelia Delamarre
    Department of Cell Biology and Department of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520 8002, USA
    Science 307:1630-4. 2005
    ..Limited lysosomal proteolysis also favored antigen presentation. These results help explain why DCs are able to efficiently accumulate, process, and disseminate antigens and microbes systemically for purposes of tolerance and immunity...
  11. ncbi request reprint Abnormal acidification of melanoma cells induces tyrosinase retention in the early secretory pathway
    Ruth Halaban
    Department of Dermatology, Yale University School of Medicine, New Haven, Connecticut 06520, USA
    J Biol Chem 277:14821-8. 2002
    ....
  12. pmc Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis
    Lelia Delamarre
    Department of Cell Biology and Section of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, CT 06520, USA
    J Exp Med 203:2049-55. 2006
    ..These findings suggest that stability to lysosomal proteolysis may be an important factor in determining immunogenicity, with potential implications for vaccine design...
  13. ncbi request reprint Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit
    E S Trombetta
    Department of Cell Biology, Yale University School of Medicine, P O Box 208002, New Haven, Connecticut 06520 8002, USA
    J Biol Chem 271:27509-16. 1996
    ..It encoded a soluble protein rich in glutamic and aspartic acid with a putative ER retention signal (HDEL) at the C terminus. This suggested that the beta subunit is responsible for the ER localization of the enzyme...
  14. pmc CHMP5 is essential for late endosome function and down-regulation of receptor signaling during mouse embryogenesis
    Jae Hyuck Shim
    Section of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, CT 06520, USA
    J Cell Biol 172:1045-56. 2006
    ..Therefore, CHMP5 regulates late endosome function downstream of MVB formation, and the loss of CHMP5 enhances signal transduction by inhibiting lysosomal degradation of activated receptors...
  15. ncbi request reprint Expression profiling reveals novel pathways in the transformation of melanocytes to melanomas
    Keith Hoek
    Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 15 York Street, New Haven, CT 06520 8059, USA
    Cancer Res 64:5270-82. 2004
    ..These results provide a comprehensive view of changes in advanced melanoma relative to normal melanocytes and reveal new targets that can be used in assessing prognosis, staging, and therapy of melanoma patients...
  16. ncbi request reprint Cross-talk between the endocytic pathway and the endoplasmic reticulum in cross-presentation by MHC class I molecules
    Ngozi Monu
    Cancer Institute, New York University School of Medicine, 522 First Avenue, New York, NY 10016, USA
    Curr Opin Immunol 19:66-72. 2007
    ..Understanding the molecular and cellular basis of cross-presentation will illuminate novel aspects of cell physiology and might lead to improved vaccine design...