{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mateos B"],"funding":["Austrian Science Fund FWF","Christian Doppler Laboratory for High-Content Structural Biology and Biotechnology","Bundesministerium f?r Digitalisierung und Wirtschaftsstandort","Narodowe Centrum Nauki","Christian Doppler Forschungsgesellschaft","?sterreichische Nationalstiftung f?r Forschung, Technologie und Entwicklung"],"pagination":["1347-1355"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8154273"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["60(17)"],"pubmed_abstract":["Protein phosphorylation is an abundant post-translational modification (PTM) and an essential modulator of protein functionality in living cells. Intrinsically disordered proteins (IDPs) are particular targets of PTM protein kinases due to their involvement in fundamental protein interaction networks. Despite their dynamic nature, IDPs are far from having random-coil conformations but exhibit significant structural heterogeneity. Changes in the molecular environment, most prominently in the form of PTM via phosphorylation, can modulate these structural features. Therefore, how phosphorylation events can alter conformational ensembles of IDPs and their interactions with binding partners is of great interest. Here we study the effects of hyperphosphorylation on the IDP osteopontin (OPN), an "],"journal":["Biochemistry"],"pubmed_title":["Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition."],"pmcid":["PMC8154273"],"funding_grant_id":["P28937-B21","M2651","W1258","2015/18/A/ST4/00270","M 2651","P 28937"],"pubmed_authors":["Holzinger J","Kozminski W","Mateos B","Platzer G","Konrat R","Sealey-Cardona M","Anrather D","Conrad-Billroth C","Zerko S"],"additional_accession":[]},"is_claimable":false,"name":"Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition.","description":"Protein phosphorylation is an abundant post-translational modification (PTM) and an essential modulator of protein functionality in living cells. Intrinsically disordered proteins (IDPs) are particular targets of PTM protein kinases due to their involvement in fundamental protein interaction networks. Despite their dynamic nature, IDPs are far from having random-coil conformations but exhibit significant structural heterogeneity. Changes in the molecular environment, most prominently in the form of PTM via phosphorylation, can modulate these structural features. Therefore, how phosphorylation events can alter conformational ensembles of IDPs and their interactions with binding partners is of great interest. Here we study the effects of hyperphosphorylation on the IDP osteopontin (OPN), an ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 May","modification":"2026-05-08T15:06:40.75Z","creation":"2022-02-10T12:22:09.013Z"},"accession":"S-EPMC8154273","cross_references":{"pubmed":["33876640"],"doi":["10.1021/acs.biochem.1c00050"]}}