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http://purl.uniprot.org/citations/8002995http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8002995http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8002995http://www.w3.org/2000/01/rdf-schema#comment"Tropomodulin is a 40.6-kDa protein that binds to one end of the rod-like tropomyosin and inhibits its cooperativity and binding to actin. In myofibrils, tropomodulin has been localized at or near the free end of thin filaments. Using recombinant and chimeric molecules in a solid-phase binding assay, we demonstrate that it is the N-terminus of tropomyosin that interacts with tropomodulin. Among several tropomyosin isoforms tested, hTM5 encoded by the human gamma-tropomyosin gene has the highest affinity toward human erythrocyte tropomodulin. Tropomodulin may, therefore, regulate the length and/or organization of actin filaments by differential binding to tropomyosin isoforms. hTM5 exists in the human erythrocyte membrane skeleton. In non-muscle cells, tropomodulin may block the head-to-tail association of tropomyosins and their interaction with actin at the pointed end of actin filaments by preferentially binding to TM5 at its N-terminus."xsd:string
http://purl.uniprot.org/citations/8002995http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1994.1747"xsd:string
http://purl.uniprot.org/citations/8002995http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1994.1747"xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/author"Lin J.J.-C."xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/author"Lin J.J.-C."xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/author"Sung L.A."xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/author"Sung L.A."xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/pages"627-634"xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/pages"627-634"xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/title"Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the gamma-tropomyosin gene."xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/title"Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the gamma-tropomyosin gene."xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/volume"201"xsd:string
http://purl.uniprot.org/citations/8002995http://purl.uniprot.org/core/volume"201"xsd:string
http://purl.uniprot.org/citations/8002995http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8002995
http://purl.uniprot.org/citations/8002995http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8002995
http://purl.uniprot.org/citations/8002995http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8002995
http://purl.uniprot.org/citations/8002995http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8002995
http://purl.uniprot.org/uniprot/P06753http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8002995
http://purl.uniprot.org/uniprot/P28289http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8002995