Relevant bibliographies by topics / Sarcomeric protein stoichiometry

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Academic literature on the topic 'Sarcomeric protein stoichiometry'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "Sarcomeric protein stoichiometry"

1

Flashman, Emily, Hugh Watkins, and Charles Redwood. "Localization of the binding site of the C-terminal domain of cardiac myosin-binding protein-C on the myosin rod." Biochemical Journal 401, no. 1 (2006): 97–102. http://dx.doi.org/10.1042/bj20060500.

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cMyBP-C [cardiac (MyBP-C) myosin-binding protein-C)] is a sarcomeric protein involved both in thick filament structure and in the regulation of contractility. It is composed of eight IgI-like and three fibronectin-3-like domains (termed C0–C10). Mutations in the gene encoding cMyBP-C are a principal cause of HCM (hypertrophic cardiomyopathy). cMyBP-C binds to the LMM (light meromyosin) portion of the myosin rod via its C-terminal domain, C10. We investigated this interaction in detail to determine whether HCM mutations in β myosin heavy chain located within the LMM portion alter the binding of
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2

Sussman, Mark A. "Analysis of Myofibrillar Organization and Degeneration by Fluorescence Confocal Microscopy." Proceedings, annual meeting, Electron Microscopy Society of America 54 (August 11, 1996): 18–19. http://dx.doi.org/10.1017/s0424820100162557.

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Myofibrillar degeneration is an important pathological process in progressive cardiomyopathy leading to heart failure. Loss of myofibrils in vivo has been observed in both adaptive cardiac responses (i.e. hypertrophy) as well as in chemotherapeutic use of antitumor drugs with cardiotoxic side effects (i.e. doxorubicin). The molecular mechanism(s) of myofibrillar degeneration are poorly understood in comparison with the sequence of events involved in myofibrillar assembly and organization. Maintenance of myofibril integrity is dependent upon a variety of factors, including contractile protein s
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3

Warmke, J., M. Yamakawa, J. Molloy, S. Falkenthal, and D. Maughan. "Myosin light chain-2 mutation affects flight, wing beat frequency, and indirect flight muscle contraction kinetics in Drosophila." Journal of Cell Biology 119, no. 6 (1992): 1523–39. http://dx.doi.org/10.1083/jcb.119.6.1523.

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We have used a combination of classical genetic, molecular genetic, histological, biochemical, and biophysical techniques to identify and characterize a null mutation of the myosin light chain-2 (MLC-2) locus of Drosophila melanogaster. Mlc2E38 is a null mutation of the MLC-2 gene resulting from a nonsense mutation at the tenth codon position. Mlc2E38 confers dominant flightless behavior that is associated with reduced wing beat frequency. Mlc2E38 heterozygotes exhibit a 50% reduction of MLC-2 mRNA concentration in adult thoracic musculature, which results in a commensurate reduction of MLC-2
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4

Agarwal, Radhika, Joao A. Paulo, Christopher N. Toepfer, et al. "Filamin C Cardiomyopathy Variants Cause Protein and Lysosome Accumulation." Circulation Research 129, no. 7 (2021): 751–66. http://dx.doi.org/10.1161/circresaha.120.317076.

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Rationale: Dominant heterozygous variants in filamin C ( FLNC ) cause diverse cardiomyopathies, although the underlying molecular mechanisms remain poorly understood. Objective: We aimed to define the molecular mechanisms by which FLNC variants altered human cardiomyocyte gene and protein expression, sarcomere structure, and contractile performance. Methods and Results: Using CRISPR/Cas9, we introduced FLNC variants into human induced pluripotent stem cell–derived cardiomyocytes (hiPSC-CMs). We compared isogenic hiPSC-CMs with normal (wild-type), ablated expression ( FLNC −/− ), or haploinsuff
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5

MARCO-FERRERES, Raquel, Juan J. ARREDONDO, Benito FRAILE, and Margarita CERVERA. "Overexpression of troponin T in Drosophila muscles causes a decrease in the levels of thin-filament proteins." Biochemical Journal 386, no. 1 (2005): 145–52. http://dx.doi.org/10.1042/bj20041240.

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Formation of the contractile apparatus in muscle cells requires co-ordinated activation of several genes and the proper assembly of their products. To investigate the role of TnT (troponin T) in the mechanisms that control and co-ordinate thin-filament formation, we generated transgenic Drosophila lines that overexpress TnT in their indirect flight muscles. All flies that overexpress TnT were unable to fly, and the loss of thin filaments themselves was coupled with ultrastructural perturbations of the sarcomere. In contrast, thick filaments remained largely unaffected. Biochemical analysis of
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6

Marín, María-Cruz, José-Rodrigo Rodríguez, and Alberto Ferrús. "Transcription of Drosophila Troponin I Gene Is Regulated by Two Conserved, Functionally Identical, Synergistic Elements." Molecular Biology of the Cell 15, no. 3 (2004): 1185–96. http://dx.doi.org/10.1091/mbc.e03-09-0663.

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The Drosophila wings-up A gene encodes Troponin I. Two regions, located upstream of the transcription initiation site (upstream regulatory element) and in the first intron (intron regulatory element), regulate gene expression in specific developmental and muscle type domains. Based on LacZ reporter expression in transgenic lines, upstream regulatory element and intron regulatory element yield identical expression patterns. Both elements are required for full expression levels in vivo as indicated by quantitative reverse transcription-polymerase chain reaction assays. Three myocyte enhancer fac
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7

Li, Amy, Shane R. Nelson, Sheema Rahmanseresht, et al. "Skeletal MyBP-C isoforms tune the molecular contractility of divergent skeletal muscle systems." Proceedings of the National Academy of Sciences 116, no. 43 (2019): 21882–92. http://dx.doi.org/10.1073/pnas.1910549116.

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Skeletal muscle myosin-binding protein C (MyBP-C) is a myosin thick filament-associated protein, localized through its C terminus to distinct regions (C-zones) of the sarcomere. MyBP-C modulates muscle contractility, presumably through its N terminus extending from the thick filament and interacting with either the myosin head region and/or the actin thin filament. Two isoforms of MyBP-C (fast- and slow-type) are expressed in a muscle type-specific manner. Are the expression, localization, and Ca2+-dependent modulatory capacities of these isoforms different in fast-twitch extensor digitorum lo
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8

Dumka, D., J. Talent, I. Akopova, G. Guzman, D. Szczesna-Cordary, and J. Borejdo. "E22K mutation of RLC that causes familial hypertrophic cardiomyopathy in heterozygous mouse myocardium: effect on cross-bridge kinetics." American Journal of Physiology-Heart and Circulatory Physiology 291, no. 5 (2006): H2098—H2106. http://dx.doi.org/10.1152/ajpheart.00396.2006.

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Familial hypertrophic cardiomyopathy is a disease characterized by left ventricular and/or septal hypertrophy and myofibrillar disarray. It is caused by mutations in sarcomeric proteins, including the ventricular isoform of myosin regulatory light chain (RLC). The E22K mutation is located in the RLC Ca2+-binding site. We have studied transgenic (Tg) mouse cardiac myofibrils during single-turnover contraction to examine the influence of E22K mutation on 1) dissociation time (τ1) of myosin heads from thin filaments, 2) rebinding time (τ2) of the cross bridges to actin, and 3) dissociation time (
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9

Helms, Adam S., Vi Tang, Jonathan Hernandez, et al. "Abstract 17079: MYBPC3 Truncation Mutations Cause Contractile Dysregulation in iPSC-Derived Cardiomyocytes." Circulation 138, Suppl_1 (2018). http://dx.doi.org/10.1161/circ.138.suppl_1.17079.

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The mechanism of MYBPC3 (encoding cardiac myosin binding protein C, MyBP-C) truncation mutations, the most common genetic cause of hypertrophic cardiomyopathy, has been incompletely resolved. We hypothesized that truncating MYBPC3 mutations cause myofibrillar protein assembly defects and/or contractile dysfunction. Methods and Results: Control iPSCs were CRISPR/Cas9-edited to create cell lines with homozygous (homCT) and heterozygous (hetCT) C-terminal MYBPC3 truncation mutations and heterozygous MYBPC3 promoter knock-out (hetPROM). HetCT was further edited to add an N-terminal flag tag (FhetC
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10

Zhang, Zhentao, Wenhui Zhang, and Young-Jae Nam. "Stoichiometric optimization of Gata4, Hand2, Mef2c, and Tbx5 expression for contractile cardiomyocyte reprogramming." Scientific Reports 9, no. 1 (2019). http://dx.doi.org/10.1038/s41598-019-51536-8.

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Abstract Reprogramming of fibroblasts to induced cardiomyocyte-like cells (iCMs) offers potential strategies for new cardiomyocyte generation. However, a major challenge of this approach remains its low efficiency for contractile iCMs. Here, we showed that controlled stoichiometric expression of Gata4 (G), Hand2 (H), Mef2c (M), and Tbx5 (T) significantly enhanced contractile cardiomyocyte reprogramming over previously defined stoichiometric expression of GMT or uncontrolled expression of GHMT. We generated quad-cistronic vectors expressing distinct relative protein levels of GHMT within the co
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