{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14"],"submitter":["Bozzi M"],"pubmed_abstract":["<h4>Background</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.<h4>Results</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,"],"journal":["BMC biochemistry"],"pagination":["15"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3704865"],"repository":["biostudies-literature"],"pubmed_title":["Probing the stability of the \"naked\" mucin-like domain of human α-dystroglycan."],"pmcid":["PMC3704865"],"pubmed_authors":["Desiderio C","Di Stasio E","Martelli C","Brancaccio A","Giardina B","Sciandra F","Scaglione GL","Bozzi M"],"additional_accession":[]},"is_claimable":false,"name":"Probing the stability of the \"naked\" mucin-like domain of human α-dystroglycan.","description":"<h4>Background</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.<h4>Results</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,","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Jul","modification":"2025-04-26T14:09:35.779Z","creation":"2019-03-27T01:12:39Z"},"accession":"S-EPMC3704865","cross_references":{"pubmed":["23815856"],"doi":["10.1186/1471-2091-14-15"]}}