<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>14</volume><submitter>Bozzi M</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>α-Dystroglycan (α-DG) is heavily glycosylated within its central mucin-like domain. The glycosylation shell of α-dystroglycan is known to largely influence its functional properties toward extracellular ligands. The structural features of this α-dystroglycan domain have been poorly studied so far. For the first time, we have attempted a recombinant expression approach in E. coli cells, in order to analyze by biochemical and biophysical techniques this important domain of the α-dystroglycan core protein.&lt;h4>Results&lt;/h4>We expressed the recombinant mucin-like domain of human α-dystroglycan in E. coli cells, and purified it as a soluble peptide of 174 aa. A cleavage event, that progressively emerges under repeated cycles of freeze/thaw, occurs at the carboxy side of Arg461,</pubmed_abstract><journal>BMC biochemistry</journal><pagination>15</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3704865</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Probing the stability of the "naked" mucin-like domain of human α-dystroglycan.</pubmed_title><pmcid>PMC3704865</pmcid><pubmed_authors>Desiderio C</pubmed_authors><pubmed_authors>Di Stasio E</pubmed_authors><pubmed_authors>Martelli C</pubmed_authors><pubmed_authors>Brancaccio A</pubmed_authors><pubmed_authors>Giardina B</pubmed_authors><pubmed_authors>Sciandra F</pubmed_authors><pubmed_authors>Scaglione GL</pubmed_authors><pubmed_authors>Bozzi M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Probing the stability of the "naked" mucin-like domain of human α-dystroglycan.</name><description>&lt;h4>Background&lt;/h4>α-Dystroglycan (α-DG) is heavily glycosylated within its central mucin-like domain. The glycosylation shell of α-dystroglycan is known to largely influence its functional properties toward extracellular ligands. The structural features of this α-dystroglycan domain have been poorly studied so far. For the first time, we have attempted a recombinant expression approach in E. coli cells, in order to analyze by biochemical and biophysical techniques this important domain of the α-dystroglycan core protein.&lt;h4>Results&lt;/h4>We expressed the recombinant mucin-like domain of human α-dystroglycan in E. coli cells, and purified it as a soluble peptide of 174 aa. A cleavage event, that progressively emerges under repeated cycles of freeze/thaw, occurs at the carboxy side of Arg461,</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Jul</publication><modification>2025-04-26T14:09:35.779Z</modification><creation>2019-03-27T01:12:39Z</creation></dates><accession>S-EPMC3704865</accession><cross_references><pubmed>23815856</pubmed><doi>10.1186/1471-2091-14-15</doi></cross_references></HashMap>