{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["13(1)"],"submitter":["Dixit H"],"pubmed_abstract":["Background
Tau is a disordered Microtubule Associated Protein (MAP) which prefers to bind and stabilize microtubules. Phosphorylation of tau in particular enhances tautubulin interaction which otherwise detaches from tubulin during hyperphosphorylation. The reason behind their destabilization, detachment and the role of β subunit (from microtubule) and the projection domain (Tau) in microtubule stability remains elusive till date. Thus, a complete 3D structural investigation of tau protein is much needed to address these queries as the existing crystal structures are in fragments and quite limited.Methods
In this study, the modelled human tau protein was subjected to phosphorylation and hyperphosphorylation which were later considered for docking with micro-tubules (βα subu"],"journal":["Avicenna journal of medical biotechnology"],"pagination":["24-34"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7903436"],"repository":["biostudies-literature"],"pubmed_title":["Role of Phosphorylation and Hyperphosphorylation of Tau in Its Interaction with βα Dimeric Tubulin Studied from a Bioinformatics Perspective."],"pmcid":["PMC7903436"],"pubmed_authors":["Kumar C S","Gadewal N","Chaudhary R","Dixit H","Thaker D","Dasgupta D"],"additional_accession":[]},"is_claimable":false,"name":"Role of Phosphorylation and Hyperphosphorylation of Tau in Its Interaction with βα Dimeric Tubulin Studied from a Bioinformatics Perspective.","description":"Background
Tau is a disordered Microtubule Associated Protein (MAP) which prefers to bind and stabilize microtubules. Phosphorylation of tau in particular enhances tautubulin interaction which otherwise detaches from tubulin during hyperphosphorylation. The reason behind their destabilization, detachment and the role of β subunit (from microtubule) and the projection domain (Tau) in microtubule stability remains elusive till date. Thus, a complete 3D structural investigation of tau protein is much needed to address these queries as the existing crystal structures are in fragments and quite limited.Methods
In this study, the modelled human tau protein was subjected to phosphorylation and hyperphosphorylation which were later considered for docking with micro-tubules (βα subu","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jan-Mar","modification":"2025-05-18T11:26:15.351Z","creation":"2021-03-08T08:09:36Z"},"accession":"S-EPMC7903436","cross_references":{"pubmed":["33680370"],"doi":["10.18502/ajmb.v13i1.4579"]}}