| http://purl.uniprot.org/citations/26976709 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26976709 | http://www.w3.org/2000/01/rdf-schema#comment | "Higher affinity for TnI explains how troponin C (TnC) carrying a causative hypertrophic cardiomyopathy mutation, TnC(A8V), sensitizes muscle cells to Ca(2+). Muscle fibers reconstituted with TnC(A8V) require ∼2.3-fold less [Ca(2+)] to achieve 50% maximum-tension compared to fibers reconstituted with wild-type TnC (TnC(WT)). Binding measurements rule out a significant change in N-terminus Ca(2+)-affinity of isolated TnC(A8V), and TnC(A8V) binds the switch-peptide of troponin-I (TnI(sp)) ∼1.6-fold more strongly than TnC(WT); thus we model the TnC-TnI(sp) interaction as competing with the TnI-actin interaction. Tension data are well-fit by a model constrained to conditions in which the affinity of TnC(A8V) for TnI(sp) is 1.5-1.7-fold higher than that of TnC(WT) at all [Ca(2+)]. Mean ATPase rates of reconstituted cardiac myofibrils is greater for TnC(A8V) than TnC(WT) at all [Ca(2+)], with statistically significant differences in the means at higher [Ca(2+)]. To probe TnC-TnI interaction in low Ca(2+), displacement of bis-ANS from TnI was monitored as a function of TnC. Whereas Ca(2+)-TnC(WT) displaces significantly more bis-ANS than Mg(2+)-TnC(WT), Ca(2+)-TnC(A8V) displaces probe equivalently to Mg(2+)-TnC(A8V) and Ca(2+)-TnC(WT), consistent with stronger Ca(2+)-independent TnC(A8V)-TnI(sp). A Matlab program for computing theoretical activation is reported. Our work suggests that contractility is constantly above normal in hearts made hypertrophic by TnC(A8V)."xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.abb.2016.03.011"xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/author | "Zot H.G."xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/author | "Pinto J.R."xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/author | "Landim-Vieira M."xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/author | "Hasbun J.E."xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/author | "Michell C.A."xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/name | "Arch Biochem Biophys"xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/pages | "97-104"xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/title | "Enhanced troponin I binding explains the functional changes produced by the hypertrophic cardiomyopathy mutation A8V of cardiac troponin C."xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://purl.uniprot.org/core/volume | "601"xsd:string |
| http://purl.uniprot.org/citations/26976709 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26976709 |
| http://purl.uniprot.org/citations/26976709 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26976709 |
| http://purl.uniprot.org/uniprot/#_P63316-mappedCitation-26976709 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26976709 |
| http://purl.uniprot.org/uniprot/#_Q6FH91-mappedCitation-26976709 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26976709 |
| http://purl.uniprot.org/uniprot/P63316 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/26976709 |
| http://purl.uniprot.org/uniprot/Q6FH91 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/26976709 |