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A dual-beam optical tweezers measured the mechanics of alpha-actinin 2 and rabbit titin interaction at the single-molecule level. Depending on the direction of force application, the unbinding forces can more than triple. Multiple alpha-actinin/Z-repeat interactions cooperate to ensure long-term stable titin anchoring, while allowing the individual components to exchange dynamically.
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These results provide new insights into the regulation of SK2 channel trafficking by the cytoskeletal proteins FLNA and alpha-actinin2, involving distinct recycling pathways
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the interaction between GNE and alpha-actinin 1 and alpha-actinin 2 occur at different sites in the alpha-actinin molecules and that for alpha-actinin 2 the interaction site is located at the C-terminus of the protein.
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The full length mEos2 tagged protein expressed in adult cardiomyocytes shows that both mutations additionally affect Z-disc localization and dynamic behaviour
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study strengthens the hypothesis that ACTN2 influences caries risk.
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The novel heterozygous missense sequence variant ACTN2 cosegregated with a complex cardiomyopathic trait, characterized by the interplay of midapical, nonobstructive HCM, early onset of AF and AV block, as well as regional LV noncompaction.
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Clinical evaluation of an Australian family revealed diverse cardiac pathologies in four affected members and genetic testing of the exome identified a pathogenic ACTN2 heterozygous variant (Ala119Thr) that co-segregated with disease.
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Study reports a complete high-resolution structure of the 200 kDa alpha-actinin-2 dimer from striated muscle and explore its functional implications on the biochemical and cellular level.
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This study generated the genomic sequences of K88-positive and F18-positive porcine enteroteoxigenic E. coli (ETEC) strains and examined the phylogenetic distribution of clinical porcine ETEC strains and their plasmid-associated genetic content.
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Findigs show that the F-actin-binding protein alpha-actinin-2 targets CaMKIIalpha to F-actin in cells by binding to the CaMKII regulatory domain.
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data provide functional evidence that the primary sequences of alpha-actinin-2 and alpha-actinin-3 evolved differences to optimize their functions
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This is the first genome-wide linkage analysis that shows mutations in ACTN2 cause HCM
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BPAG1-b was detectable in vitro and in vivo as a high molecular mass protein in striated and heart muscle cells, co-localizing with alpha-actinin-2 and partially with the cytolinker plectin as well as with the intermediate filament protein desmin.
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Spectrin-like repeats from dystrophin and alpha-actinin-2 are not functionally interchangeable.
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Association of Ca2+-activated K+ channel with alpha-actinin2 localizes channel to entry of external Ca(2+) source, which regulates channel function.
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actinin-2 participate in sequestering parafibromin in the cytoplasmic compartment.
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ACTN2 expression is affected by the content of alpha-actinin-3.
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demonstrate that proper membrane localization of a small-conductance Ca(2+)-activated K(+) channel (SK2 or K(Ca)2.2) is dependent on its interacting protein, alpha-actinin2, a major F-actin crosslinking protein.
