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E S Trombetta

Showing results (1-10 of 8) with videos related to

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The Journal of Cell Biology|March 22, 2000
Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulumE S Trombetta, A Helenius
Current Opinion in Structural Biology|November 18, 1998
Lectins as chaperones in glycoprotein foldingE S Trombetta, A Helenius
The EMBO Journal|June 16, 1999
Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulumE S Trombetta, A Helenius
Advances in Protein Chemistry|March 1, 2002
N-glycan processing and glycoprotein foldingE S Trombetta, A J Parodi
The Journal of Biological Chemistry|November 1, 1996
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, J F Simons, A Helenius
Biochemistry|August 29, 2001
Quaternary and domain structure of glycoprotein processing glucosidase IIE S Trombetta, K G Fleming, A Helenius
The Journal of Biological Chemistry|August 28, 1999
Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein foldingC D'Alessio, F Fernández, E S Trombetta, et al.
The EMBO Journal|December 16, 1996
N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulinA R Rodan, J F Simons, E S Trombetta, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
The Journal of Cell Biology|March 22, 2000
Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulumE S Trombetta, A Helenius
Current Opinion in Structural Biology|November 18, 1998
Lectins as chaperones in glycoprotein foldingE S Trombetta, A Helenius
The EMBO Journal|June 16, 1999
Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulumE S Trombetta, A Helenius
Advances in Protein Chemistry|March 1, 2002
N-glycan processing and glycoprotein foldingE S Trombetta, A J Parodi
The Journal of Biological Chemistry|November 1, 1996
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, J F Simons, A Helenius
Biochemistry|August 29, 2001
Quaternary and domain structure of glycoprotein processing glucosidase IIE S Trombetta, K G Fleming, A Helenius
The Journal of Biological Chemistry|August 28, 1999
Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein foldingC D'Alessio, F Fernández, E S Trombetta, et al.
The EMBO Journal|December 16, 1996
N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulinA R Rodan, J F Simons, E S Trombetta, et al.
Pageof 1