<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Baumges H</submitter><funding>Deutsche Forschungsgemeinschaft</funding><pagination>1355</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12427801</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14(17)</volume><pubmed_abstract>Fucose-containing glycoproteins and glycolipids broadly occur in humans as well as in many other species and are essential for a wide range of physiological processes, such as cell adhesion, fertilization, and tumor development. In humans, the cellular degradation of various fucosylated glycoconjugates depends on the &lt;i>FUCA1&lt;/i>-encoded lysosomal tissue α-L-fucosidase (FUCA1). The crucial role of FUCA1 is reflected by the severe lysosomal storage disease fucosidosis, which causes a massive accumulation of fucosylated glycans, glycolipids, and α(1,6)-fucosylated glycoasparagines. Therefore, it is reasonable to assume that FUCA1 is predominantly responsible for the degradation of fucosylated glycoconjugates, although a second, functionally uncharacterized α-L-fucosidase, the plasma α-L-fuco</pubmed_abstract><journal>Cells</journal><pubmed_title>Deciphering α-L-Fucosidase Activity Contribution in Human and Mouse: Tissue α-L-Fucosidase FUCA1 Meets Plasma α-L-Fucosidase FUCA2.</pubmed_title><pmcid>PMC12427801</pmcid><funding_grant_id>FOR2625 TP7</funding_grant_id><pubmed_authors>Lubke T</pubmed_authors><pubmed_authors>Lange H</pubmed_authors><pubmed_authors>Hausser JA</pubmed_authors><pubmed_authors>Markmann S</pubmed_authors><pubmed_authors>Braulke T</pubmed_authors><pubmed_authors>Jelinek S</pubmed_authors><pubmed_authors>Ilse MB</pubmed_authors><pubmed_authors>Baumges H</pubmed_authors><pubmed_authors>Capriotti E</pubmed_authors></additional><is_claimable>false</is_claimable><name>Deciphering α-L-Fucosidase Activity Contribution in Human and Mouse: Tissue α-L-Fucosidase FUCA1 Meets Plasma α-L-Fucosidase FUCA2.</name><description>Fucose-containing glycoproteins and glycolipids broadly occur in humans as well as in many other species and are essential for a wide range of physiological processes, such as cell adhesion, fertilization, and tumor development. In humans, the cellular degradation of various fucosylated glycoconjugates depends on the &lt;i>FUCA1&lt;/i>-encoded lysosomal tissue α-L-fucosidase (FUCA1). The crucial role of FUCA1 is reflected by the severe lysosomal storage disease fucosidosis, which causes a massive accumulation of fucosylated glycans, glycolipids, and α(1,6)-fucosylated glycoasparagines. Therefore, it is reasonable to assume that FUCA1 is predominantly responsible for the degradation of fucosylated glycoconjugates, although a second, functionally uncharacterized α-L-fucosidase, the plasma α-L-fuco</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Aug</publication><modification>2026-04-08T19:55:29.524Z</modification><creation>2026-04-08T14:35:10.568Z</creation></dates><accession>S-EPMC12427801</accession><cross_references><pubmed>40940767</pubmed><doi>10.3390/cells14171355</doi></cross_references></HashMap>