<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kuribara T</submitter><funding>Japan Society for the Promotion of Science</funding><pagination>199</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8869290</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(2)</volume><pubmed_abstract>Glycoprotein folding plays a critical role in sorting glycoprotein secretion and degradation in the endoplasmic reticulum (ER). Furthermore, relationships between glycoprotein folding and several diseases, such as type 2 diabetes and various neurodegenerative disorders, are indicated. Patients' cells with type 2 diabetes, and various neurodegenerative disorders induce ER stress, against which the cells utilize the unfolded protein response for protection. However, in some cases, chronic and/or massive ER stress causes critical damage to cells, leading to the onset of ER stress-related diseases, which are categorized into misfolding diseases. Accumulation of misfolded proteins may be a cause of ER stress, in this respect, perturbation of oligomannose-type glycan processing in the ER may occ</pubmed_abstract><journal>Biology</journal><pubmed_title>Oligomannose-Type Glycan Processing in the Endoplasmic Reticulum and Its Importance in Misfolding Diseases.</pubmed_title><pmcid>PMC8869290</pmcid><funding_grant_id>JP16K01938</funding_grant_id><funding_grant_id>JP16H06290</funding_grant_id><pubmed_authors>Kuribara T</pubmed_authors><pubmed_authors>Totani K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Oligomannose-Type Glycan Processing in the Endoplasmic Reticulum and Its Importance in Misfolding Diseases.</name><description>Glycoprotein folding plays a critical role in sorting glycoprotein secretion and degradation in the endoplasmic reticulum (ER). Furthermore, relationships between glycoprotein folding and several diseases, such as type 2 diabetes and various neurodegenerative disorders, are indicated. Patients' cells with type 2 diabetes, and various neurodegenerative disorders induce ER stress, against which the cells utilize the unfolded protein response for protection. However, in some cases, chronic and/or massive ER stress causes critical damage to cells, leading to the onset of ER stress-related diseases, which are categorized into misfolding diseases. Accumulation of misfolded proteins may be a cause of ER stress, in this respect, perturbation of oligomannose-type glycan processing in the ER may occ</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Jan</publication><modification>2025-04-22T01:27:22.871Z</modification><creation>2025-04-05T19:57:21.737Z</creation></dates><accession>S-EPMC8869290</accession><cross_references><pubmed>35205066</pubmed><doi>10.3390/biology11020199</doi></cross_references></HashMap>