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Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic ret...

Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic ret...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6319373

Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum

About this item

Full title

Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum

Publisher

United States: The American Association for the Advancement of Science

Journal title

Science (American Association for the Advancement of Science), 2018-04, Vol.360 (6385), p.215-219

Language

English

Formats

Publication information

Publisher

United States: The American Association for the Advancement of Science

More information

Scope and Contents

Contents

Many secretory and membrane proteins are modified through the attachment of sugar chains by N-glycosylation. Such modification is required for correct protein folding, targeting, and functionality. In mammalian cells, N-glycosylation is catalyzed by the oligosaccharyltransferase (OST) complex via its STT3 subunit. OST forms a complex with the ribos...

Alternative Titles

Full title

Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6319373

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6319373

Other Identifiers

ISSN

0036-8075

E-ISSN

1095-9203

DOI

10.1126/science.aar7899

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