Research Topics
Genomes and Genes | E S TrombettaSummaryAffiliation: Yale University Country: USA Publications
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Publications
Quality control and protein folding in the secretory pathwayE 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...
Glycoprotein reglucosylationE 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....
The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesisE 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...
Cell biology of antigen processing in vitro and in vivoE 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...
Quaternary and domain structure of glycoprotein processing glucosidase IIE 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...
Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulumE 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...
Lectins as chaperones in glycoprotein foldingE S Trombetta
Department of Cell Biology, Yale Medical School, New Haven, CT 06520 8002, USA
Curr Opin Struct Biol 8:587-92. 1998....
Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulumE 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...
Activation of lysosomal function during dendritic cell maturationE 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...
Abnormal acidification of melanoma cells induces tyrosinase retention in the early secretory pathwayRuth Halaban
Department of Dermatology, Yale University School of Medicine, New Haven, Connecticut 06520, USA
J Biol Chem 277:14821-8. 2002....
Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunitE 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...
CHMP5 is essential for late endosome function and down-regulation of receptor signaling during mouse embryogenesisJae 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...
Expression profiling reveals novel pathways in the transformation of melanocytes to melanomasKeith 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...
Cross-talk between the endocytic pathway and the endoplasmic reticulum in cross-presentation by MHC class I moleculesNgozi 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...
