{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mulukala SKN"],"funding":["Indian Council of Medical Research"],"pagination":["100774"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7322680"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23"],"pubmed_abstract":["Podocytes are crucial cells of the glomerular filtration unit and plays a vital role at the interface of the blood-urine barrier. Podocyte slit-diaphragm is a modified tight junction that facilitates size and charge-dependent permselectivity. Several proteins including podocin, nephrin, CD2AP, and TRPC6 form a macromolecular assembly and constitute the slit-diaphragm. Podocin is an integral membrane protein attached to the inner membrane of the podocyte via a short transmembrane region (101-125). The cytosolic N- and C-terminus help podocin to attain a hook-like structure. Podocin shares 44% homology with stomatin family proteins and similar to the stomatin proteins, podocin was shown to associate into higher-order oligomers at the site of slit-diaphragm. However, the stoichiometry of the "],"journal":["Biochemistry and biophysics reports"],"pubmed_title":["Structural features and oligomeric nature of human podocin domain."],"pmcid":["PMC7322680"],"funding_grant_id":["ICMR 2019/905"],"pubmed_authors":["Vadrevu R","Mulukala SKN","Kumar K","Pasupulati AK","Irukuvajjula SS","Garai K","Venkatesu P"],"additional_accession":[]},"is_claimable":false,"name":"Structural features and oligomeric nature of human podocin domain.","description":"Podocytes are crucial cells of the glomerular filtration unit and plays a vital role at the interface of the blood-urine barrier. Podocyte slit-diaphragm is a modified tight junction that facilitates size and charge-dependent permselectivity. Several proteins including podocin, nephrin, CD2AP, and TRPC6 form a macromolecular assembly and constitute the slit-diaphragm. Podocin is an integral membrane protein attached to the inner membrane of the podocyte via a short transmembrane region (101-125). The cytosolic N- and C-terminus help podocin to attain a hook-like structure. Podocin shares 44% homology with stomatin family proteins and similar to the stomatin proteins, podocin was shown to associate into higher-order oligomers at the site of slit-diaphragm. However, the stoichiometry of the ","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Sep","modification":"2026-04-30T11:24:10.982Z","creation":"2020-07-05T07:06:06Z"},"accession":"S-EPMC7322680","cross_references":{"pubmed":["32617419"],"doi":["10.1016/j.bbrep.2020.100774"]}}