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http://purl.uniprot.org/citations/33307294http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33307294http://www.w3.org/2000/01/rdf-schema#comment"Tropomyosin (Tpm) is an actin-binding protein that plays a crucial role in the regulation of muscle contraction. Numerous point mutations in the TPM3 gene encoding Tpm of slow skeletal muscles (Tpm 3.12 or γ-Tpm) are associated with the genesis of various congenital myopathies. Two of these mutations, R91P and R245G, are associated with congenital fiber-type disproportion (CFTD) characterized by hypotonia and generalized muscle weakness. We applied various methods to investigate how these mutations affect the structural and functional properties of γγ-Tpm homodimers. The results show that both these mutations lead to strong structural changes in the γγ-Tpm molecule and significantly impaired its functional properties. These changes in the Tpm properties caused by R91P and R245G mutations give insight into the molecular mechanism of the CFTD development and the weakness of slow skeletal muscles observed in this inherited disease."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2020.11.103"xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Levitsky D.I."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Kleymenov S.Y."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Tsaturyan A.K."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Kopylova G.V."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Matyushenko A.M."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Shchepkin D.V."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Berg V.Y."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Gonchar A.D."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Kochurova A.M."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/author"Koubasova N.A."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/pages"8-13"xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/title"Effects of myopathy-causing mutations R91P and R245G in the TPM3 gene on structural and functional properties of slow skeletal muscle tropomyosin."xsd:string
http://purl.uniprot.org/citations/33307294http://purl.uniprot.org/core/volume"534"xsd:string
http://purl.uniprot.org/citations/33307294http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33307294
http://purl.uniprot.org/citations/33307294http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33307294
http://purl.uniprot.org/uniprot/#_A0A087WWU8-mappedCitation-33307294http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33307294
http://purl.uniprot.org/uniprot/#_A0A2R2Y2Q3-mappedCitation-33307294http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33307294
http://purl.uniprot.org/uniprot/#_A0A0S2Z4G4-mappedCitation-33307294http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33307294
http://purl.uniprot.org/uniprot/#_A0A0S2Z4G8-mappedCitation-33307294http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33307294
http://purl.uniprot.org/uniprot/#_A0A0S2Z4I4-mappedCitation-33307294http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33307294