{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hassoun R"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["4465"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9024677"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(8)"],"pubmed_abstract":["Human wild type (wt) cardiac α-actin and its mutants p.A295S or p.R312H and p.E361G correlated with hypertrophic or dilated cardiomyopathy, respectively, were expressed by using the <i>baculovirus/Sf21</i> insect cell system. The c-actin variants inhibited DNase I, indicating maintenance of their native state. Electron microscopy showed the formation of normal appearing actin filaments though they showed mutant specific differences in length and straightness correlating with their polymerization rates. TRITC-phalloidin staining showed that p.A295S and p.R312H exhibited reduced and the p.E361G mutant increased lengths of their formed filaments. Decoration of c-actins with cardiac tropomyosin (cTm) and troponin (cTn) conveyed Ca<sup>2+</sup>-sensitivity of the myosin-S1 ATPase stimulation, w"],"journal":["International journal of molecular sciences"],"pubmed_title":["Functional Characterization of Cardiac Actin Mutants Causing Hypertrophic (p.A295S) and Dilated Cardiomyopathy (p.R312H and p.E361G)."],"pmcid":["PMC9024677"],"funding_grant_id":["Ma 807/19-1"],"pubmed_authors":["Mannherz HG","Fujita-Becker S","Jaquet K","Geyer M","Mugge A","Schmitt S","Hamdani N","Hassoun R","Erdmann C","Schroder RR","Borbor M"],"additional_accession":[]},"is_claimable":false,"name":"Functional Characterization of Cardiac Actin Mutants Causing Hypertrophic (p.A295S) and Dilated Cardiomyopathy (p.R312H and p.E361G).","description":"Human wild type (wt) cardiac α-actin and its mutants p.A295S or p.R312H and p.E361G correlated with hypertrophic or dilated cardiomyopathy, respectively, were expressed by using the <i>baculovirus/Sf21</i> insect cell system. The c-actin variants inhibited DNase I, indicating maintenance of their native state. Electron microscopy showed the formation of normal appearing actin filaments though they showed mutant specific differences in length and straightness correlating with their polymerization rates. TRITC-phalloidin staining showed that p.A295S and p.R312H exhibited reduced and the p.E361G mutant increased lengths of their formed filaments. Decoration of c-actins with cardiac tropomyosin (cTm) and troponin (cTn) conveyed Ca<sup>2+</sup>-sensitivity of the myosin-S1 ATPase stimulation, w","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2025-04-18T13:54:36.168Z","creation":"2025-04-06T23:45:09.363Z"},"accession":"S-EPMC9024677","cross_references":{"pubmed":["35457283"],"doi":["10.3390/ijms23084465"]}}