<HashMap><database>biostudies-literature</database><scores/><additional><submitter>D'Alessio C</submitter><funding>NIDDK NIH HHS</funding><pagination>31-48</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4411176</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>16(1)</volume><pubmed_abstract>N-glycosylation in the endoplasmic reticulum (ER) consists of the transfer of a preassembled glycan conserved among species (Glc3Man9GlcNAc2) from a lipid donor to a consensus sequence within a nascent protein that is entering the ER. The protein-linked glycans are then processed by glycosidases and glycosyltransferases in the ER producing specific structures that serve as signalling molecules for the fate of the folding glycoprotein: to stay in the ER during the folding process, to be retrotranslocated to the cytosol for proteasomal degradation if irreversibly misfolded, or to pursue transit through the secretory pathway as a mature glycoprotein. In the ER, each glycan signalling structure is recognized by a specific lectin. A domain similar to that of the mannose 6-phosphate receptors (M</pubmed_abstract><journal>Current protein &amp; peptide science</journal><pubmed_title>Glucosidase II and MRH-domain containing proteins in the secretory pathway.</pubmed_title><pmcid>PMC4411176</pmcid><funding_grant_id>R01 DK042667</funding_grant_id><funding_grant_id>R01DK042667</funding_grant_id><pubmed_authors>D'Alessio C</pubmed_authors><pubmed_authors>Dahms NM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Glucosidase II and MRH-domain containing proteins in the secretory pathway.</name><description>N-glycosylation in the endoplasmic reticulum (ER) consists of the transfer of a preassembled glycan conserved among species (Glc3Man9GlcNAc2) from a lipid donor to a consensus sequence within a nascent protein that is entering the ER. The protein-linked glycans are then processed by glycosidases and glycosyltransferases in the ER producing specific structures that serve as signalling molecules for the fate of the folding glycoprotein: to stay in the ER during the folding process, to be retrotranslocated to the cytosol for proteasomal degradation if irreversibly misfolded, or to pursue transit through the secretory pathway as a mature glycoprotein. In the ER, each glycan signalling structure is recognized by a specific lectin. A domain similar to that of the mannose 6-phosphate receptors (M</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015</publication><modification>2025-04-04T11:05:12.293Z</modification><creation>2019-06-06T14:18:32Z</creation></dates><accession>S-EPMC4411176</accession><cross_references><pubmed>25692846</pubmed><doi>10.2174/1389203716666150213160438</doi></cross_references></HashMap>