Artykuły w czasopismach: „Filamine C”

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Kopishinskaia, S. V., A. A. Lesnikova, D. I. Abramova i I. A. Velichko. "Filaminopathy type C". Medical alphabet, nr 33 (14.01.2021): 62–65. http://dx.doi.org/10.33667/2078-5631-2020-33-62-65.

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Filamin is an actin-binding protein that, by forming flexible molecular cross-links, stabilizes the three-dimensional F-actin networks and gives them the mechanical properties of a gel. It is represented by three isoforms: filamine A (FLNA), filamin B (FLNB), and filamin C (FLNC), derived from 3 homologous genes. Laminopathies caused by mutations in the FLNA, FLNB, and FLNC genes represent an extensive allelic series of diseases. The review discusses in detail the genotype-phenotypic correlation of all types of phylaminopathies. The neuromuscular and cardiac clinic of C-type phylaminopathy is described in detail. Three variants of C phylaminopathy known at the moment are analyzed.

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Mao, Zhenfeng, i Fumihiko Nakamura. "Structure and Function of Filamin C in the Muscle Z-Disc". International Journal of Molecular Sciences 21, nr 8 (13.04.2020): 2696. http://dx.doi.org/10.3390/ijms21082696.

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Filamin C (FLNC) is one of three filamin proteins (Filamin A (FLNA), Filamin B (FLNB), and FLNC) that cross-link actin filaments and interact with numerous binding partners. FLNC consists of a N-terminal actin-binding domain followed by 24 immunoglobulin-like repeats with two intervening calpain-sensitive hinges separating R15 and R16 (hinge 1) and R23 and R24 (hinge-2). The FLNC subunit is dimerized through R24 and calpain cleaves off the dimerization domain to regulate mobility of the FLNC subunit. FLNC is localized in the Z-disc due to the unique insertion of 82 amino acid residues in repeat 20 and necessary for normal Z-disc formation that connect sarcomeres. Since phosphorylation of FLNC by PKC diminishes the calpain sensitivity, assembly, and disassembly of the Z-disc may be regulated by phosphorylation of FLNC. Mutations of FLNC result in cardiomyopathy and muscle weakness. Although this review will focus on the current understanding of FLNC structure and functions in muscle, we will also discuss other filamins because they share high sequence similarity and are better characterized. We will also discuss a possible role of FLNC as a mechanosensor during muscle contraction.

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Kim, Hugh, Fumihiko Nakamura, Wilson Lee, Yulia Shifrin, Pamela Arora i Christopher A. McCulloch. "Filamin A is required for vimentin-mediated cell adhesion and spreading". American Journal of Physiology-Cell Physiology 298, nr 2 (luty 2010): C221—C236. http://dx.doi.org/10.1152/ajpcell.00323.2009.

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Cell adhesion and spreading are regulated by complex interactions involving the cytoskeleton and extracellular matrix proteins. We examined the interaction of the intermediate filament protein vimentin with the actin cross-linking protein filamin A in regulation of spreading in HEK-293 and 3T3 cells. Filamin A and vimentin-expressing cells were well spread on collagen and exhibited numerous cell extensions enriched with filamin A and vimentin. By contrast, cells treated with small interfering RNA (siRNA) to knock down filamin A or vimentin were poorly spread; both of these cell populations exhibited >50% reductions of cell adhesion, cell surface β1 integrin expression, and β1 integrin activation. Knockdown of filamin A reduced vimentin phosphorylation and blocked recruitment of vimentin to cell extensions, whereas knockdown of filamin and/or vimentin inhibited the formation of cell extensions. Reduced vimentin phosphorylation, cell spreading, and β1 integrin surface expression, and activation were phenocopied in cells treated with the protein kinase C inhibitor bisindolylmaleimide; cell spreading was also reduced by siRNA knockdown of protein kinase C-ε. By immunoprecipitation of cell lysates and by pull-down assays using purified proteins, we found an association between filamin A and vimentin. Filamin A also associated with protein kinase C-ε, which was enriched in cell extensions. These data indicate that filamin A associates with vimentin and to protein kinase C-ε, thereby enabling vimentin phosphorylation, which is important for β1 integrin activation and cell spreading on collagen.

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Corrado, Domenico, i Alessandro Zorzi. "Filamin C". JACC: Clinical Electrophysiology 4, nr 4 (kwiecień 2018): 515–17. http://dx.doi.org/10.1016/j.jacep.2018.01.004.

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Ruskamo, Salla, Robert Gilbert, Gregor Hofmann, Pengju Jiang, Iain D. Campbell, Jari Ylänne i Ulla Pentikäinen. "The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended". Biochemical Journal 446, nr 2 (14.08.2012): 261–69. http://dx.doi.org/10.1042/bj20120361.

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Filamins are large proteins that cross-link actin filaments and connect to other cellular components. The C-terminal rod 2 region of FLNa (filamin A) mediates dimerization and interacts with several transmembrane receptors and intracellular signalling adaptors. SAXS (small-angle X-ray scattering) experiments were used to make a model of a six immunoglobulin-like domain fragment of the FLNa rod 2 (domains 16–21). This fragment had a surprising three-branched structural arrangement, where each branch was made of a tightly packed two-domain pair. Peptides derived from transmembrane receptors and intracellular signalling proteins induced a more open structure of the six domain fragment. Mutagenesis studies suggested that these changes are caused by peptides binding to the CD faces on domains 19 and 21 which displace the preceding domain A-strands (18 and 20 respectively), thus opening the individual domain pairs. A single particle cryo-EM map of a nine domain rod 2 fragment (domains 16–24), showed a relatively compact dimeric particle and confirmed the three-branched arrangement as well as the peptide-induced conformation changes. These findings reveal features of filamin structure that are important for its interactions and mechanical properties.

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Tayal, Upasana, i Stuart A. Cook. "Truncating Variants in Filamin C". Journal of the American College of Cardiology 68, nr 22 (grudzień 2016): 2452–53. http://dx.doi.org/10.1016/j.jacc.2016.05.105.

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Holmes, William B., i Carole L. Moncman. "Nebulette interacts with filamin C". Cell Motility and the Cytoskeleton 65, nr 2 (luty 2008): 130–42. http://dx.doi.org/10.1002/cm.20249.

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Wu, Tongbin, Yujun Xu, Lunfeng Zhang, Zhengyu Liang, Xiaohai Zhou, Sylvia M. Evans i Ju Chen. "Filamin C is Essential for mammalian myocardial integrity". PLOS Genetics 19, nr 1 (27.01.2023): e1010630. http://dx.doi.org/10.1371/journal.pgen.1010630.

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FLNC, encoding filamin C, is one of the most mutated genes in dilated and hypertrophic cardiomyopathy. However, the precise role of filamin C in mammalian heart remains unclear. In this study, we demonstrated Flnc global (FlncgKO) and cardiomyocyte-specific knockout (FlnccKO) mice died in utero from severely ruptured ventricular myocardium, indicating filamin C is required to maintain the structural integrity of myocardium in the mammalian heart. Contrary to the common belief that filamin C acts as an integrin inactivator, we observed attenuated activation of β1 integrin specifically in the myocardium of FlncgKO mice. Although deleting β1 integrin from cardiomyocytes did not recapitulate the heart rupture phenotype in Flnc knockout mice, deleting both β1 integrin and filamin C from cardiomyocytes resulted in much more severe heart ruptures than deleting filamin C alone. Our results demonstrated that filamin C works in concert with β1 integrin to maintain the structural integrity of myocardium during mammalian heart development.

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Fürst, Dieter O., Lev G. Goldfarb, Rudolf A. Kley, Matthias Vorgerd, Montse Olivé i Peter F. M. van der Ven. "Filamin C-related myopathies: pathology and mechanisms". Acta Neuropathologica 125, nr 1 (30.10.2012): 33–46. http://dx.doi.org/10.1007/s00401-012-1054-9.

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Widiyanti, Prihartini. "THE ROLE OF HYPERBARIC THERAPY IN THE GROWTH OF CANDIDA ALBICANS". Indonesian Journal of Tropical and Infectious Disease 4, nr 4 (1.10.2013): 23. http://dx.doi.org/10.20473/ijtid.v4i4.228.

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Background: Candida albicans is opportunistic pathogen fungi which cause many disease in human such as reccurrent apthous stomatitis, skin lesions, vulvavaginitis, candiduria and gastrointestinal candidiasis. Aim: Infection mechanism of C. albicans is very complex including adhesion and invasion, morphology alteration from khamir form cell to filamen form (hifa), biofilm forming and the avoidance of host immunity. Method: The ability of C. albicans to adhere to the host cell which is act as important factor in the early colonization and infection. Result: The phenotype alteration to be filament form let the C. albicans to penetrate to the epithelium and play important role in infection and separation C. Albicans to the host cell. Hyperbaric oxygen is the inhalation of 100 percent oxygen inside hyperbaric chamber that is pressurized to greater than 1 atmosphere (atm). Conclusion: The organism was found to be inhibited within a pressure/time range well tolerated by human subjects, suggesting that hyperbaric oxygen might be used successfully in treating human candidiasis.

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Jeon, Young Joo, Joon Seok Choi, Jung Yun Lee, Kyung Ryun Yu, Seung Hyeun Ka, Yongcheol Cho, Eui-Ju Choi i in. "Filamin B Serves as a Molecular Scaffold for Type I Interferon-induced c-Jun NH2-terminal Kinase Signaling Pathway". Molecular Biology of the Cell 19, nr 12 (grudzień 2008): 5116–30. http://dx.doi.org/10.1091/mbc.e08-06-0576.

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Type I interferons (IFNs) activate Janus tyrosine kinase-signal transducer and activator of transcription pathway for exerting pleiotropic biological effects, including antiviral, antiproliferative, and immunomodulatory responses. Here, we demonstrate that filamin B functions as a scaffold that links between activated Rac1 and a c-Jun NH2-terminal kinase (JNK) cascade module for mediating type I IFN signaling. Filamin B interacted with Rac1, mitogen-activated protein kinase kinase kinase 1, mitogen-activated protein kinase kinase 4, and JNK. Filamin B markedly enhanced IFNα-dependent Rac1 activation and the sequential activation of the JNK cascade members. Complementation assays using M2 melanoma cells revealed that filamin B, but not filamin A, is required for IFNα-dependent activation of JNK. Furthermore, filamin B promoted IFNα-induced apoptosis, whereas short hairpin RNA-mediated knockdown of filamin B prevented it. These results establish a novel function of filamin B as a molecular scaffold in the JNK signaling pathway for type I IFN-induced apoptosis, thus providing the biological basis for antitumor and antiviral functions of type I IFNs.

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Sjekloća, Ljiljana, Regina Pudas, Björn Sjöblom, Peter Konarev, Oliviero Carugo, Vladimir Rybin, Tiila-Riikka Kiema, Dmitri Svergun, Jari Ylänne i Kristina Djinović Carugo. "Crystal Structure of Human Filamin C Domain 23 and Small Angle Scattering Model for Filamin C 23–24 Dimer". Journal of Molecular Biology 368, nr 4 (maj 2007): 1011–23. http://dx.doi.org/10.1016/j.jmb.2007.02.018.

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Brodehl, A., R. Ferrier, S. C. Greenway, M. Brundler, W. Yu, N. Alvarez, M. Giuffre i B. Gerull. "MUTATIONS IN FILAMIN C CAUSE FAMILIAL RESTRICTIVE CARDIOMYOPATHY". Canadian Journal of Cardiology 31, nr 10 (październik 2015): S147. http://dx.doi.org/10.1016/j.cjca.2015.07.318.

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Shadman, Shahrad, Leyla Gasimli-Gamache, Sarah Luther i Jamshid Shirani. "FILAMIN C GENE MUTATION IN FAMILIAL HYPERTROPHIC CARDIOMYOPATHY". Journal of the American College of Cardiology 83, nr 13 (kwiecień 2024): 2827. http://dx.doi.org/10.1016/s0735-1097(24)04817-4.

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Wadmore, Kirsty, Amar J. Azad i Katja Gehmlich. "The Role of Z-disc Proteins in Myopathy and Cardiomyopathy". International Journal of Molecular Sciences 22, nr 6 (17.03.2021): 3058. http://dx.doi.org/10.3390/ijms22063058.

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The Z-disc acts as a protein-rich structure to tether thin filament in the contractile units, the sarcomeres, of striated muscle cells. Proteins found in the Z-disc are integral for maintaining the architecture of the sarcomere. They also enable it to function as a (bio-mechanical) signalling hub. Numerous proteins interact in the Z-disc to facilitate force transduction and intracellular signalling in both cardiac and skeletal muscle. This review will focus on six key Z-disc proteins: α-actinin 2, filamin C, myopalladin, myotilin, telethonin and Z-disc alternatively spliced PDZ-motif (ZASP), which have all been linked to myopathies and cardiomyopathies. We will summarise pathogenic variants identified in the six genes coding for these proteins and look at their involvement in myopathy and cardiomyopathy. Listing the Minor Allele Frequency (MAF) of these variants in the Genome Aggregation Database (GnomAD) version 3.1 will help to critically re-evaluate pathogenicity based on variant frequency in normal population cohorts.

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Frasson, Murilo Zomer, i Cristiano Pederneiras Jaeger. "Cardiomiopatia Dilatada: Nova Variante no Gene da Filamina-C". Arquivos Brasileiros de Cardiologia 117, nr 1 Supl. 1 (lipiec 2021): 16–18. http://dx.doi.org/10.36660/abc.20200199.

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Inchingolo, Alessio V., Samantha Beck Previs, Michael J. Previs, David M. Warshaw i Neil M. Kad. "Revealing the mechanism of how cardiac myosin-binding protein C N-terminal fragments sensitize thin filaments for myosin binding". Proceedings of the National Academy of Sciences 116, nr 14 (15.03.2019): 6828–35. http://dx.doi.org/10.1073/pnas.1816480116.

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Cardiac muscle contraction is triggered by calcium binding to troponin. The consequent movement of tropomyosin permits myosin binding to actin, generating force. Cardiac myosin-binding protein C (cMyBP-C) plays a modulatory role in this activation process. One potential mechanism for the N-terminal domains of cMyBP-C to achieve this is by binding directly to the actin-thin filament at low calcium levels to enhance the movement of tropomyosin. To determine the molecular mechanisms by which cMyBP-C enhances myosin recruitment to the actin-thin filament, we directly visualized fluorescently labeled cMyBP-C N-terminal fragments and GFP-labeled myosin molecules binding to suspended actin-thin filaments in a fluorescence-based single-molecule microscopy assay. Binding of the C0C3 N-terminal cMyBP-C fragment to the thin filament enhanced myosin association at low calcium levels. However, at high calcium levels, C0C3 bound in clusters, blocking myosin binding. Dynamic imaging of thin filament-bound Cy3-C0C3 molecules demonstrated that these fragments diffuse along the thin filament before statically binding, suggesting a mechanism that involves a weak-binding mode to search for access to the thin filament and a tight-binding mode to sensitize the thin filament to calcium, thus enhancing myosin binding. Although shorter N-terminal fragments (Cy3-C0C1 and Cy3-C0C1f) bound to the thin filaments and displayed modes of motion on the thin filament similar to that of the Cy3-C0C3 fragment, the shorter fragments were unable to sensitize the thin filament. Therefore, the longer N-terminal fragment (C0C3) must possess the requisite domains needed to bind specifically to the thin filament in order for the cMyBP-C N terminus to modulate cardiac contractility.

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Agarwal, Radhika, Joao A. Paulo, Christopher N. Toepfer, Jourdan K. Ewoldt, Subramanian Sundaram, Anant Chopra, Qi Zhang i in. "Filamin C Cardiomyopathy Variants Cause Protein and Lysosome Accumulation". Circulation Research 129, nr 7 (17.09.2021): 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 haploinsufficiency ( FLNC +/− ) that causes dilated cardiomyopathy. We also studied a heterozygous in-frame deletion ( FLNC +/Δ7aa ) which did not affect FLNC expression but caused aggregate formation, similar to FLNC variants associated with hypertrophic cardiomyopathy. FLNC −/− hiPSC-CMs demonstrated profound sarcomere misassembly and reduced contractility. Although sarcomere formation and function were unaffected in FLNC +/ − and FLNC +/Δ7aa hiPSC-CMs, these heterozygous variants caused increases in lysosome content, enhancement of autophagic flux, and accumulation of FLNC-binding partners and Z-disc proteins. Conclusions: FLNC expression is required for sarcomere organization and physiological function. Variants that produce misfolded FLNC proteins cause the accumulation of FLNC and FLNC-binding partners which leads to increased lysosome expression and activation of autophagic pathways. Surprisingly, similar pathways were activated in FLNC haploinsufficient hiPSC-CMs, likely initiated by the loss of stoichiometric FLNC protein interactions and impaired turnover of proteins at the Z-disc. These results indicate that both FLNC haploinsufficient variants and variants that produce misfolded FLNC protein cause disease by similar proteotoxic mechanisms and indicate the therapeutic potential for augmenting protein degradative pathways to treat a wide range of FLNC -related cardiomyopathies.

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Borch, Josefine de Stricker, Anne-Sofie Vibæk Eisum, Thomas Krag i John Vissing. "Expanding the phenotype of filamin-C-related myofibrillar myopathy". Clinical Neurology and Neurosurgery 176 (styczeń 2019): 30–33. http://dx.doi.org/10.1016/j.clineuro.2018.11.013.

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Zhou, Yangzhao, Ze’e Chen, Lunfeng Zhang, Mason Zhu, Changming Tan, Xinmin Zhou, Sylvia M. Evans, Xi Fang, Wei Feng i Ju Chen. "Loss of Filamin C Is Catastrophic for Heart Function". Circulation 141, nr 10 (10.03.2020): 869–71. http://dx.doi.org/10.1161/circulationaha.119.044061.

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Chanprasertpinyo, Wisit, i Teerapat Yingchoncharoen. "UNVEILING THE MASK: FILAMIN C CARDIOMYOPATHY MASQUERADING AS MYOCARDITIS". Journal of the American College of Cardiology 83, nr 13 (kwiecień 2024): 2732. http://dx.doi.org/10.1016/s0735-1097(24)04722-3.

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Vrettos, Apostolos, Polyvios Demetriades, Martín Ortiz, Pablo García-Pavía, Fernando Domínguez, Maria Paz Suárez-Mier, Thomas Gossios i Konstantinos Savvatis. "Pathogenic Truncating Filamin C Mutations Presenting as Acute Myocarditis". Journal of Cardiovascular Magnetic Resonance 26 (2024): 100641. http://dx.doi.org/10.1016/j.jocmr.2024.100641.

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Feng, Shuju, Xin Lu i Michael H. Kroll. "Filamin A Binding Stabilizes Nascent Glycoprotein Ibα Trafficking and Thereby Enhances Its Surface Expression." Blood 104, nr 11 (16.11.2004): 3656. http://dx.doi.org/10.1182/blood.v104.11.3656.3656.

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Abstract The glycoprotein (Gp) Ib-IX-V complex is essential for platelet function. The extracellular domain of GpIbα binds to von Willebrand factor (VWF) and rapidly effects shear-dependent platelet rolling, tether formation, adherence and aggregation onto freshly exposed subendothelium. Following VWF binding, GpIbα transduces proaggregatory signals through its cytoplasmic domain, and these signals may be modulated by the activity of GpIbβ and GpV. The expression of GpIbα, GpIbβ and GpIX in megakaryocytes also regulates terminal maturation and platelet release (its absence results in Bernard-Soulier syndrome) and there is human genetic and in vitro evidence that the cytoplasmic domain of GpIbα regulates megakaryocyte growth and surface expression of the complex. The cytoplasmic domain of GpIbα possesses a binding region for filamin A, which links GpIb-IX-V to the platelet cytoskeleton, and there is evidence that filamin A binding to GpIbα directs the surface expression of GpIb-IX in CHO cells. To investigate the mechanism of this effect, we examined GpIbα biosynthesis in CHO cells stably co-expressing wild-type or mutant GpIbα with GpIbβ, GpIX and filamin A. We observed that surface GpIbα expression as measured by flow cytometry is enhanced ~ 1 log-order in CHO cells co-expressing human filamin A. In comparison with CHO-GpIbαβIX cell lysates, lysates from CHO-GpIbαβIX-filamin A cells showed greater amounts of immature (~ 65 kDa), incompletely glycosylated (~ 80 kDa and ~ 90 kDa) and fully mature GpIbα (~ 120 kDa), but lesser amounts of the ~ 15 kDa C-terminal peptide released when the extracellular domain of GpIbα (glycocalycin) is cleaved by surface proteases. To determine if the effect of filamin A is due to its binding to GpIbα, we examined GpIbα biosynthesis using several mutants of GpIbα co-expressed with GpIbβ, GpIX and filamin A. When filamin A binding is eliminated by truncation of GpIbα at C-terminal residue 557 or by a deletion in GpIbα between amino acids 542–570, the decreased synthesis of mature GpIbα is accompanied by nearly complete elimination of all immunodetectable immature GpIbα and by increased immunodetectable C-terminal peptide. To corroborate these data and control for cell selection and non-specific secondary structural changes, we examined the expression of three cell lines expressing two additional mutants of GpIbα in CHO cells stably transfected with GpIbβ, GpIX and filamin A. The expression of GpIbα with a C-terminal deletion between residues 560 and 570 (which inhibits filamin A binding), but not GpIbα with alanine substitutions at C-terminal residues 557 through 559 (which converts the sequence RGS to AAA but doesn’t inhibit filamin binding), results in the near-elimination of immature GpIbα. These results suggest that GpIbα binding to filamin enhances the surface expression of GpIb-IX by directing nascent protein trafficking away from a degradative pathway and towards the golgi. This leads to increased glycosylation, which further stabilizes the complex by attenuating the susceptibility of the extracellular domain to proteolytic cleavage.

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Li, Amy, Shane R. Nelson, Sheema Rahmanseresht, Filip Braet, Anabelle S. Cornachione, Samantha Beck Previs, Thomas S. O’Leary i in. "Skeletal MyBP-C isoforms tune the molecular contractility of divergent skeletal muscle systems". Proceedings of the National Academy of Sciences 116, nr 43 (7.10.2019): 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 longus (EDL) and slow-twitch soleus (SOL) muscles derived from Sprague–Dawley rats? By mass spectrometry, 4 MyBP-C isoforms (1 fast-type MyBP-C and 3 N-terminally spliced slow-type MyBP-C) were expressed in EDL, but only the 3 slow-type MyBP-C isoforms in SOL. Using EDL and SOL native thick filaments in which the MyBP-C stoichiometry and localization are preserved, native thin filament sliding over these thick filaments showed that, only in the C-zone, MyBP-C Ca2+ sensitizes the thin filament and slows thin filament velocity. These modulatory properties depended on MyBP-C’s N terminus as N-terminal proteolysis attenuated MyBP-C’s functional capacities. To determine each MyBP-C isoform’s contribution to thin filament Ca2+ sensitization and slowing in the C-zone, we used a combination of in vitro motility assays using expressed recombinant N-terminal fragments and in silico mechanistic modeling. Our results suggest that each skeletal MyBP-C isoform’s N terminus is functionally distinct and has modulatory capacities that depend on the muscle type in which they are expressed, providing the potential for molecular tuning of skeletal muscle performance through differential MyBP-C expression.

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Collier, Mary, Camille Ettelaie, Benjamin Goult, Anthony Maraveyas i Alison Goodall. "Investigation of the Filamin A–Dependent Mechanisms of Tissue Factor Incorporation into Microvesicles". Thrombosis and Haemostasis 117, nr 11 (2017): 2034–44. http://dx.doi.org/10.1160/th17-01-0009.

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AbstractWe have previously shown that phosphorylation of tissue factor (TF) at Ser253 increases the incorporation of TF into microvesicles (MVs) following protease-activated receptor 2 (PAR2) activation through a process involving filamin A, whereas phosphorylation of TF at Ser258 suppresses this process. Here, we examined the contribution of the individual phosphorylation of these serine residues to the interaction between filamin A and TF, and further examined how filamin A regulates the incorporation of TF into MVs. In vitro binding assays using recombinant filamin A C-terminal repeats 22–24 with biotinylated phospho-TF cytoplasmic domain peptides as bait showed that filamin A had the highest binding affinities for phospho-Ser253 and double-phosphorylated TF peptides, while the phospho-Ser258 TF peptide had the lowest affinity. Analysis of MDA-MB-231 cells using an in situ proximity ligation assay revealed increased proximity between the C-terminus of filamin A and TF following PAR2 activation, which was concurrent with Ser253 phosphorylation and TF-positive MV release from these cells. Knock-down of filamin A expression suppressed PAR2-mediated increases in cell surface TF procoagulant activity without reducing cell surface TF antigen expression. Disrupting lipid rafts by pre-incubation with methyl-β-cyclodextrin prior to PAR2 activation reduced TF-positive MV release and cell surface TF procoagulant activity to the same extent as filamin A knock-down. In conclusion, this study shows that the interaction between TF and filamin A is dependent on the differential phosphorylation of Ser253 and Ser258. Furthermore, the interaction of TF with filamin A may translocate cell surface TF to cholesterol-rich lipid rafts, increasing cell surface TF activity as well as TF incorporation and release into MVs.

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Nakagawa, Kentaro, Misato Sugahara, Tokiwa Yamasaki, Hiroaki Kajiho, Shinya Takahashi, Jun Hirayama, Yasuhiro Minami i in. "Filamin associates with stress signalling kinases MKK7 and MKK4 and regulates JNK activation". Biochemical Journal 427, nr 2 (29.03.2010): 237–45. http://dx.doi.org/10.1042/bj20091011.

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SAPK/JNK (stress-activated protein kinase/c-Jun N-terminal kinase) belongs to the MAPK (mitogen-activated protein kinase) family and is important in many biological contexts. JNK activation is regulated by phosphorylation of specific tyrosine and threonine residues sequentially catalysed by MKK4 and MKK7, which are both dual-specificity MAPKKs (MAPK kinases). Previously, we reported that tyrosine-phosphorylation of JNK by MKK4 precedes threonine-phosphorylation by MKK7, and that both are required for synergistic JNK activation. In the present study, we identify the actin-binding protein-280 (Filamin A) as a presumed ‘binder’ protein that can bind to MKK7, as well as to MKK4, connecting them in close proximity. We show that Filamin family members A, B and C interact with MKK4 and MKK7, but not with JNK. Filamin A binds to an N-terminal region (residues 31–60) present in the MKK7γ and MKK7β splice isoforms, but cannot bind to MKK7α which lacks these amino acids. This same N-terminal region is crucial for the intracellular co-localization of MKK7γ with actin stress fibres and Filamin A. Experiments using Filamin-A-deletion mutants revealed that the MKK7-binding region of Filamin A differs from its MKK4-binding region, and that MKK7γ (but not MKK7α) can form a complex with Filamin A and MKK4. Finally, we used Filamin-A-deficient cells to show that Filamin A enhances MKK7 activation and is important for synergistic stress-induced JNK activation in vivo. Thus Filamin A is a novel member of the group of scaffold proteins whose function is to link two MAPKKs together and promote JNK activation.

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Tolt, Z. Li, L. Heatherly, R. E. Clausing i C. S. Feigerle. "Hot filament assisted diamond growth at low temperatures with oxygen addition". Journal of Materials Research 12, nr 5 (maj 1997): 1344–50. http://dx.doi.org/10.1557/jmr.1997.0183.

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Addition of a small amount of oxygen to the CH4 and H2 feed gas permits hot filament assisted chemical vapor deposition (HFCVD) of diamond at significantly lower filament and substrate temperatures. The former can be reduced to as low as 1400 °C and the latter to 450 °C. The amount of oxygen required is much lower than what has been used in most studies of the oxygen effect. For each CH4%, there is a narrow window in the O/C ratio, where diamond can be deposited at low temperature. This window shifts to higher O/C ratios as the CH4% increases and expands with increases in filament temperature. The effect of changing substrate and filament temperatures on growth rate and film quality are often not consistent with previous experiences with HFCVD of diamond. Increasing the filament temperature does not always improve the growth rate and film quality, and the non-diamond carbon content in the film is dramatically reduced at lower substrate temperatures. Optimum conditions were found that gave reasonable growth rates (∼0.5 μm/h) with high film quality at filament temperatures below 1750 °C and substrate temperatures below 600 °C. With these reductions in operating temperatures, power consumption can be significantly reduced and the filament lifetime extended indefinitely.

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Moll, Roland, Susanne Pitz, Rivka Levy, Wolfgang Weikel, Werner W. Franke i Bernard Czernobilsky. "Complexity of expression of intermediate filament proteins, including glial filament protein, in endometrial and ovarian adenocarcinomas". Human Pathology 22, nr 10 (październik 1991): 989–1001. http://dx.doi.org/10.1016/0046-8177(91)90007-c.

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Gao, Shanshan, Lingaonan He, Chi Keung Lam, Matthew R. G. Taylor, Luisa Mestroni, Raffaella Lombardi i Suet Nee Chen. "Filamin C Deficiency Impairs Sarcomere Stability and Activates Focal Adhesion Kinase through PDGFRA Signaling in Induced Pluripotent Stem Cell-Derived Cardiomyocytes". Cells 13, nr 3 (2.02.2024): 278. http://dx.doi.org/10.3390/cells13030278.

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Truncating mutations in filamin C (FLNC) are associated with dilated cardiomyopathy and arrhythmogenic cardiomyopathy. FLNC is an actin-binding protein and is known to interact with transmembrane and structural proteins; hence, the ablation of FLNC in cardiomyocytes is expected to dysregulate cell adhesion, cytoskeletal organization, sarcomere structural integrity, and likely nuclear function. Our previous study showed that the transcriptional profiles of FLNC homozygous deletions in human pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) are highly comparable to the transcriptome profiles of hiPSC-CMs from patients with FLNC truncating mutations. Therefore, in this study, we used CRISPR-Cas-engineered hiPSC-derived FLNC knockout cardiac myocytes as a model of FLNC cardiomyopathy to determine pathogenic mechanisms and to examine structural changes caused by FLNC deficiency. RNA sequencing data indicated the significant upregulation of focal adhesion signaling and the dysregulation of thin filament genes in FLNC-knockout (FLNCKO) hiPSC-CMs compared to isogenic hiPSC-CMs. Furthermore, our findings suggest that the complete loss of FLNC in cardiomyocytes led to cytoskeletal defects and the activation of focal adhesion kinase. Pharmacological inhibition of PDGFRA signaling using crenolanib (an FDA-approved drug) reduced focal adhesion kinase activation and partially normalized the focal adhesion signaling pathway. The findings from this study suggest the opportunity in repurposing FDA-approved drug as a therapeutic strategy to treat FLNC cardiomyopathy.

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Song, Byeong-Kwan, Hwan-Young Kim, Kun-Su Kim, Jeong-Woo Yang i Nong-Moon Hwang. "Unusual Dependence of the Diamond Growth Rate on the Methane Concentration in the Hot Filament Chemical Vapor Deposition Process". Materials 14, nr 2 (16.01.2021): 426. http://dx.doi.org/10.3390/ma14020426.

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Although the growth rate of diamond increased with increasing methane concentration at the filament temperature of 2100 °C during a hot filament chemical vapor deposition (HFCVD), it decreased with increasing methane concentration from 1% CH4 –99% H2 to 3% CH4 –97% H2 at 1900 °C. We investigated this unusual dependence of the growth rate on the methane concentration, which might give insight into the growth mechanism of a diamond. One possibility would be that the high methane concentration increases the non-diamond phase, which is then etched faster by atomic hydrogen, resulting in a decrease in the growth rate with increasing methane concentration. At 3% CH4 –97% H2, the graphite was coated on the hot filament both at 1900 °C and 2100 °C. The graphite coating on the filament decreased the number of electrons emitted from the hot filament. The electron emission at 3% CH4 –97% H2 was 13 times less than that at 1% CH4 –99% H2 at the filament temperature of 1900 °C. The lower number of electrons at 3% CH4 –97% H2 was attributed to the formation of the non-diamond phase, which etched faster than diamond, resulting in a lower growth rate.

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Zhang, Q. M., J. H. Guo, K. V. Tam i A. A. Xu. "Longitudinal filament oscillations enhanced by two C-class flares". Astronomy & Astrophysics 635 (marzec 2020): A132. http://dx.doi.org/10.1051/0004-6361/201937291.

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Context. Large-amplitude, longitudinal filament oscillations triggered by solar flares have been well established in the literature. However, filament oscillations enhanced by flares have never been reported. Aims. In this paper we report the multiwavelength observations of a very long filament in active region (AR) 11112 on 2010 October 18. The filament was composed of two parts, the eastern part (EP) and the western part (WP). We focus on longitudinal oscillations of the EP, which were enhanced by two homologous C-class flares in the same AR. Methods. The filament was observed in Hα wavelength by the Global Oscillation Network Group and in extreme ultraviolet wavelengths by the Atmospheric Imaging Assembly on board the Solar Dynamics Observatory (SDO). Line-of-sight magnetograms were provided by the Helioseismic and Magnetic Imager on board SDO. The global three-dimensional magnetic fields were obtained using the potential field source surface modeling. Soft X-ray light curves of the two flares were recorded by the GOES spacecraft. White light images of the corona were observed by the LASCO/C2 coronagraph on board SOHO. To reproduce part of the observations, we perform one-dimensional, hydrodynamic numerical simulations using the MPI-AMRVAC code. Results. The C1.3 flare was confined without a coronal mass ejection (CME). Both EP and WP of the filament were slightly disturbed and survived the flare. After 5 h, eruption of the WP generated a C2.6 flare and a narrow jet-like CME. Three oscillating threads (thda, thdb, thdc) are obviously identified in the EP, and their oscillations are naturally divided into three phases by the two flares. The initial amplitude ranges from 1.6 to 30 Mm with a mean value of ∼14 Mm. The period ranges from 34 to 73 min with a mean value of ∼53 min. The curvature radii of the magnetic dips are estimated to be 29 to 133 Mm with a mean value of ∼74 Mm. The damping times ranges from ∼62 to ∼96 min with a mean value of ∼82 min. The value of τ/P is between 1.2 and 1.8. For thda in the EP, the amplitudes were enhanced by the two flares from 6.1 Mm to 6.8 Mm after the C1.3 flare, and further to 21.4 Mm after the C2.6 flare. The period variation as a result of perturbation from the flares was within 20%. The attenuation became faster after the C2.6 flare. Conclusions. To the best of our knowledge, this is the first report of large-amplitude, longitudinal filament oscillations enhanced by flares. Numerical simulations reproduce the oscillations of thda very well. The simulated amplitudes and periods are close to the observed values, while the damping time in the last phase is longer, implying additional mechanisms should be taken into account apart from radiative loss.

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Walsh, Michael P., Jacquelyn E. Andrea, Bruce G. Allen, Odile Clément-Chomienne, Elizabeth M. Collins i Kathleen G. Morgan. "Smooth muscle protein kinase C". Canadian Journal of Physiology and Pharmacology 72, nr 11 (1.11.1994): 1392–99. http://dx.doi.org/10.1139/y94-201.

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Protein kinase C (PKC) was first implicated in the regulation of smooth muscle contraction with the observation that phorbol esters induce slowly developing, sustained contractions. In some vascular smooth muscles, e.g., ferret aorta, phorbol ester induced contractions occur without an increase in sarcoplasmic free-Ca2+ concentration ([Ca]i) or myosin light chain phosphorylation. This response appears to be mediated by a Ca2+-independent isoenzyme of PKC (probably PKCε), since saponin-permeabilized single ferret aortic smooth muscle cells, which retain receptor coupling, developed force in response to phenylephrine at low free [Ca2+] (pCa 7.0–8.6) and the constitutively active proteolytic fragment of PKC (PKM) elicited a contraction at pCa 7 comparable with the phenylephrine-induced contraction. Both contractions were reversed by a pseudo-substrate peptide inhibitor of PKC. These observations suggest a mechanism whereby α-adrenergic agonists may elicit a contractile response without a Ca2+ signal: α-adrenergic stimulation of phosphatidylcholine-specific phosphoiipase C or D (the latter in conjunction with phosphatidate phosphohydrolase) generates diacylglycerol. In the absence of an increase in [Ca2+]i, diacylglycerol specifically activates so-called novel PKCs, of which ε is the only isoenzyme known to be expressed in vascular smooth muscle. Recent evidence suggests that PKC may trigger a cascade of phosphorylation reactions, resulting in activation of mitogen-activated protein kinase and phosphorylation of the thin filament associated protein caldesmon. Alternatively, or additionally, PKC may directly phosphorylate calponin, another thin filament associated protein. These phosphorylations are predicted to alleviate inhibition of the cross-bridge cycling rate by these thin-filament proteins. The slow development of force would then result from a slow rate of cross-bridge cycling due to the low basal level of myosin phosphorylation.Key words: protein kinase C, smooth muscle, calcium, caldesmon, calponin.

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Bariani, Riccardo, Giulia Brunetti, Alberto Cipriani, Ilaria Rigato, Rudy Celeghin, Monica De Gaspari, Kalliopi Pilichou i Barbara Bauce. "Clinical management of a pregnant woman with Filamin C cardiomyopathy". Journal of Cardiovascular Medicine 23, nr 3 (10.01.2022): 198–202. http://dx.doi.org/10.2459/jcm.0000000000001294.

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Reinstein, Eyal, Ana Gutierrez-Fernandez, Shay Tzur, Concetta Bormans, Shai Marcu, Einav Tayeb-Fligelman, Chana Vinkler i in. "Congenital dilated cardiomyopathy caused by biallelic mutations in Filamin C". European Journal of Human Genetics 24, nr 12 (7.09.2016): 1792–96. http://dx.doi.org/10.1038/ejhg.2016.110.

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GUO, Donghao, Hui ZHAO i Erik FUNG. "Heterozygous Filamin C Truncating Mutation Disrupts Cardiac Development And Function". Journal of Cardiac Failure 29, nr 4 (kwiecień 2023): 695–96. http://dx.doi.org/10.1016/j.cardfail.2022.10.371.

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Liu, Cui Xia, Yan Qing Yang i Xian Luo. "Influence of DepositionTemperature on Tensile Behavior and Fracture Characteristics of SiC Filament by Chemical Vapor Deposition". Advanced Materials Research 146-147 (październik 2010): 1159–62. http://dx.doi.org/10.4028/www.scientific.net/amr.146-147.1159.

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CH3SiCl3-H2-Ar system was adopted to prepare SiC Filament of high tensile strength by high-frequency induction during Chemical Vapor Deposition (CVD) method. Room-temperature tensile strength of SiC filament prepared under different temperature was test. Crystal structure, surface morphology and fracture character of SiC filament was analyzed with “X-ray diffractometer and scanning electron microscope. Influence of temperature to final tensile behavior of SiC filament was discussed synthetically. The result shows that tensile strength is very sensitive to temperature. From 1000°C to 1400°C, tensile strength increases and then decreases as temperature increases. At 1200°C, tensile strength reaches its max value, the reason ofwhich is composed of three parts. The first one is that the deposited product is β-SiC. The second one is that surface of SiC filament is smooth. The third one is that fracture surface shows ductile dimples fracture, brittle fracture and cleavage fracture patterns. 1200°Cis considered as one reasonable temperature in our laboratory to prepare SiC filament.

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37

van der Flier, Arjan, Ingrid Kuikman, Duco Kramer, Dirk Geerts, Maaike Kreft, Toshiro Takafuta, Sandor S. Shapiro i Arnoud Sonnenberg. "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin β subunits". Journal of Cell Biology 156, nr 2 (21.01.2002): 361–76. http://dx.doi.org/10.1083/jcb.200103037.

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Integrins connect the extracellular matrix with the cell interior, and transduce signals through interactions of their cytoplasmic tails with cytoskeletal and signaling proteins. Using the yeast two-hybrid system, we isolated a novel splice variant (filamin-Bvar-1) of the filamentous actin cross-linking protein, filamin-B, that interacts with the cytoplasmic domain of the integrin β1A and β1D subunits. RT-PCR analysis showed weak, but wide, expression of filamin-Bvar-1 and a similar splice variant of filamin-A (filamin-Avar-1) in human tissues. Furthermore, alternative splice variants of filamin-B and filamin-C, from which the flexible hinge-1 region is deleted (ΔH1), were induced during in vitro differentiation of C2C12 mouse myoblasts. We show that both filamin-Avar-1 and filamin-Bvar-1 bind more strongly than their wild-type isoforms to different integrin β subunits. The mere presence of the high-affinity binding site for β1A is not sufficient for targeting the filamin-Bvar-1 construct to focal contacts. Interestingly, the simultaneous deletion of the H1 region is required for the localization of filamin-B at the tips of actin stress fibers. When expressed in C2C12 cells, filamin-Bvar-1(ΔH1) accelerates their differentiation into myotubes. Furthermore, filamin-B variants lacking the H1 region induce the formation of thinner myotubes than those in cells containing variants with this region. These findings suggest that specific combinations of filamin mRNA splicing events modulate the organization of the actin cytoskeleton and the binding affinity for integrins.

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Rastogi, A. C., i S. B. Desu. "Structural development and electronic properties of hot filament low pressure chemical vapor deposited fluorocarbon polymer films". Journal of Materials Research 21, nr 1 (1.01.2006): 242–54. http://dx.doi.org/10.1557/jmr.2006.0021.

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Fluorocarbon polymer films in the poly(tetrafluoroethylene) (PTFE)-like structure are formed by a low-pressure chemical vapor deposition technique using the hot filament excitation of the gaseous C3F6O precursor. The filament and substrate temperatures were found to influence the structure of the deposited films. Infrared absorption and electron spectroscopy studies reveal that a PTFE-like (CF2)2n linear molecular chain structure evolves by an adsorption driven nucleation and CF2 polymerization process in the films deposited with low (450 °C) filament and high (70 °C) substrate temperatures. The films formed at a low substrate temperature (–165 °C) show a higher concentration of CF and C–CF bond defects and shorter (CF2)2n chains. A high (8–10 at.%) oxygen concentration in the films deposited at 600 °C filament temperature is attributed to the reaction of the (CF2)2n chains with COF and peroxyradicals arising from the dissociation of CF3C(O)F and affects the thermal stability of the films. Such reactions are not involved in the film growth at a low (450 °C) filament temperature. These films have much lower (<2 at.%) bonded oxygen content. The films having an ordered (CF2)2n chain structure formed at 70 °C are characterized by low leakage currents ∼7 × 10−11 A cm−2 at 0.1 MV cm−1 field. In comparison, high leakage currents ∼1 × 10−8 A cm−2 are observed for the films having a higher concentration of C–F and C–CF bonds.

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Li, Xin E. "Study on Thermal Resistance of Basalt Filament Yarn". Advanced Materials Research 146-147 (październik 2010): 666–69. http://dx.doi.org/10.4028/www.scientific.net/amr.146-147.666.

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Basalt filament yarn is a new type of high-performance fibers, which is formed by the direct drawing of basalt rock at high temperatures. It is a natural and environmentally friendly textile material. This paper mainly focuses on thermal resistance research of basalt filament yarn that is heated at various temperatures. The change of color and appearance of heated basalt filament yarn was described. The mechanical properties of heated basalt filament yarn were tested. The results showed that although the mechanical properties of basalt filament yarn decreased with the temperature rising, still remained high tensile strength within a certain temperature range. Basalt filament yarn possess higher tenacity under 325°C. Basalt filament yarns still possess certain tenacity when they were placed at 500°C condition. So basalt filament yarn can be used as heat-resistant materials, such as filtration materials for high-temperature gas and liquid, fire-proof fabrics and so on.

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Rajan, Krishna, Katarzyna Bejtka, Sergio Bocchini, Denis Perrone, Annalisa Chiappone, Ignazio Roppolo, Candido Fabrizio Pirri, Carlo Ricciardi i Alessandro Chiolerio. "Highly performing ionic liquid enriched hybrid RSDs". Journal of Materials Chemistry C 5, nr 25 (2017): 6144–55. http://dx.doi.org/10.1039/c7tc01093a.

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Real-time observation of the filament formation and annihilation (grey area corresponds to tungsten nanoprobe). (a) Filament formation at set threshold (orange color path corresponds to the formed filamentary path). (b) Filament dissolution at reset threshold (magenta color corresponds to the annihilation of the filamentary path). (c) Further filament formation.

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Bossie, C. A., i M. M. Sanders. "A cDNA from Drosophila melanogaster encodes a lamin C-like intermediate filament protein". Journal of Cell Science 104, nr 4 (1.04.1993): 1263–72. http://dx.doi.org/10.1242/jcs.104.4.1263.

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A novel intermediate filament cDNA, pG-IF, has been isolated from a Drosophila melanogaster embryonic expression library screened with a polyclonal antiserum produced against a 46 kDa cytoskeletal protein isolated from Kc cells. This 46 kDa protein is known to be immunologically related to vertebrate intermediate filament proteins. The screen resulted in the isolation of four different cDNA groups. Of these, one has been identified as the previously characterized Drosophila nuclear lamin cDNA, Dm0, and a second, pG-IF, demonstrates homology to Dm0 by cross hybridization on Southern blots. DNA sequence analysis reveals that pG-IF encodes a newly identified intermediate filament protein in Drosophila. Its nucleotide sequence is highly homologous to nuclear lamins with lower homology to cytoplasmic intermediate filament proteins. pG-IF predicts a protein of 621 amino acids with a predicted molecular mass of 69,855 daltons. In vitro transcription and translation of pG-IF yielded a protein with a SDS-PAGE estimated molecular weight of approximately 70 kDa. It contains sequence principles characteristic of class V intermediate filament proteins. Its near neutral pI (6.83) and the lack of a terminal CaaX motif suggests that it may represent a lamin C subtype in Drosophila. In situ hybridization to polytene chromosomes detects one band of hybridization on the right arm of chromosome 2 at or near 51A. This in conjunction with Southern blot analysis of various genomic digests suggests one or more closely placed genes while Northern blot analysis detects two messages in Kc cells.

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Brunello, Elisabetta, Luca Fusi, Andrea Ghisleni, So-Jin Park-Holohan, Jesus G. Ovejero, Theyencheri Narayanan i Malcolm Irving. "Myosin filament-based regulation of the dynamics of contraction in heart muscle". Proceedings of the National Academy of Sciences 117, nr 14 (27.03.2020): 8177–86. http://dx.doi.org/10.1073/pnas.1920632117.

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Myosin-based mechanisms are increasingly recognized as supplementing their better-known actin-based counterparts to control the strength and time course of contraction in both skeletal and heart muscle. Here we use synchrotron small-angle X-ray diffraction to determine the structural dynamics of local domains of the myosin filament during contraction of heart muscle. We show that, although myosin motors throughout the filament contribute to force development, only about 10% of the motors in each filament bear the peak force, and these are confined to the filament domain containing myosin binding protein-C, the “C-zone.” Myosin motors in domains further from the filament midpoint are likely to be activated and inactivated first in each contraction. Inactivated myosin motors are folded against the filament core, and a subset of folded motors lie on the helical tracks described previously. These helically ordered motors are also likely to be confined to the C-zone, and the associated motor conformation reforms only slowly during relaxation. Myosin filament stress-sensing determines the strength and time course of contraction in conjunction with actin-based regulation. These results establish the fundamental roles of myosin filament domains and the associated motor conformations in controlling the strength and dynamics of contraction in heart muscle, enabling those structures to be targeted to develop new therapies for heart disease.

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Oliphant, Clive J., Christopher J. Arendse, Sigqibo T. Camagu i Hendrik Swart. "EBSD Analysis of Tungsten-Filament Carburization During the Hot-Wire CVD of Multi-Walled Carbon Nanotubes". Microscopy and Microanalysis 20, nr 1 (15.01.2014): 4–13. http://dx.doi.org/10.1017/s1431927613014001.

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AbstractFilament condition during hot-wire chemical vapor deposition conditions of multi-walled carbon nanotubes is a major concern for a stable deposition process. We report on the novel application of electron backscatter diffraction to characterize the carburization of tungsten filaments. During the synthesis, the W-filaments transform to W2C and WC. W-carbide growth followed a parabolic behavior corresponding to the diffusion of C as the rate-determining step. The grain size of W, W2C, and WC increases with longer exposure time and increasing filament temperature. The grain size of the recrystallizing W-core and W2C phase grows from the perimeter inwardly and this phenomenon is enhanced at filament temperatures in excess of 1,400°C. Cracks appear at filament temperatures >1,600°C, accompanied by a reduction in the filament operational lifetime. The increase of the W2C and recrystallized W-core grain size from the perimeter inwardly is ascribed to a thermal gradient within the filament, which in turn influences the hardness measurements and crack formation.

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Granzier, H. L., i K. Wang. "Interplay between passive tension and strong and weak binding cross-bridges in insect indirect flight muscle. A functional dissection by gelsolin-mediated thin filament removal." Journal of General Physiology 101, nr 2 (1.02.1993): 235–70. http://dx.doi.org/10.1085/jgp.101.2.235.

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The interplay between passive and active mechanical properties of indirect flight muscle of the waterbug (Lethocerus) was investigated. A functional dissection of the relative contribution of cross-bridges, actin filaments, and C filaments to tension and stiffness of passive, activated, and rigor fibers was carried out by comparing mechanical properties at different ionic strengths of sarcomeres with and without thin filaments. Selective thin filament removal was accomplished by treatment with the actin-severving protein gelsolin. Thin filament, removal had no effect on passive tension, indicating that the C filament and the actin filament are mechanically independent and that passive tension is developed by the C filament in response to sarcomere stretch. Passive tension increased steeply with sarcomere length until an elastic limit was reached at only 6-7% sarcomere extension, which corresponds to an extension of 350% of the C filament. The passive tension-length relation of insect flight muscle was analyzed using a segmental extension model of passive tension development (Wang, K, R. McCarter, J. Wright, B. Jennate, and R Ramirez-Mitchell. 1991. Proc. Natl. Acad. Sci. USA. 88:7101-7109). Thin filament removal greatly depressed high frequency passive stiffness (2.2 kHz) and eliminated the ionic strength sensitivity of passive stiffness. It is likely that the passive stiffness component that is removed by gelsolin is derived from weak-binding cross-bridges, while the component that remains is derived from the C filament. Our results indicate that a significant number of weak-binding cross-bridges exist in passive insect muscle at room temperature and at an ionic strength of 195 mM. Analysis of rigor muscle indicated that while rigor tension is entirely actin based, rigor stiffness contains a component that resists gelsolin treatment and is therefore likely to be C filament based. Active tension and active stiffness of unextracted fibers were directly proportional to passive tension before activation. Similarly, passive stiffness due to weak bridges also increased linearly with passive tension, up to a limit. These correlations lead us to propose a stress-activation model for insect flight muscle in which passive tension is a prerequisite for the formation of both weak-binding and strong-binding cross-bridges.

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Stahlhut, Martin, i Bo van Deurs. "Identification of Filamin as a Novel Ligand for Caveolin-1: Evidence for the Organization of Caveolin-1–associated Membrane Domains by the Actin Cytoskeleton". Molecular Biology of the Cell 11, nr 1 (styczeń 2000): 325–37. http://dx.doi.org/10.1091/mbc.11.1.325.

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Reports on the ultrastructure of cells as well as biochemical data have, for several years, been indicating a connection between caveolae and the actin cytoskeleton. Here, using a yeast two-hybrid approach, we have identified the F-actin cross-linking protein filamin as a ligand for the caveolae-associated protein caveolin-1. Binding of caveolin-1 to filamin involved the N-terminal region of caveolin-1 and the C terminus of filamin close to the filamin-dimerization domain. In in vitro binding assays, recombinant caveolin-1 bound to both nonmuscle and muscle filamin, indicating that the interaction might not be cell type specific. With the use of confocal microscopy, colocalization of caveolin-1 and filamin was observed in elongated patches at the plasma membrane. Remarkably, when stress fiber formation was induced with Rho-stimulating Escherichia coli cytotoxic necrotizing factor 1, the caveolin-1–positive structures became coaligned with stress fibers, indicating that there was a physical link connecting them. Immunogold double-labeling electron microscopy confirmed that caveolin-1–labeled racemose caveolae clusters were positive for filamin. The actin network, therefore, seems to be directly involved in the spatial organization of caveolin-1–associated membrane domains.

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BOLDRINI, RAFAEL, FREDERICO FALCÃO SALLES i ANA MARIA OLIVEIRA PES. "Imagos of Camelobaetidius francischettii Salles, Andrade & Da-Silva (Ephemeroptera: Baetidae)". Zootaxa 2476, nr 1 (18.05.2010): 65. http://dx.doi.org/10.11646/zootaxa.2476.1.7.

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The genus Camelobaetidius Demoulin (Ephemeroptera: Baetidae) is represented in South America by 28 species: 20 of them are described based on nymphs, three based solely on adults, and five based on nymphs and adults (Dominguez et al., 2006; Boldrini & Salles, 2009; Salles & Nascimento, 2009). As mentioned by Boldrini & Salles (2009), the species of the genus can be divided into three morphological groups: a) those species with the terminal filament reduced and with a projection on the inner margin of the fore femora; b) species with the terminal filament reduced and without a projection on the inner margin of the fore femora; and c) species with the terminal filament almost as long as cerci. Of these five species described based on nymphs and adults, nymphs of four of them present the terminal filament well developed, whereas in only one, C. billi Thomas & Dominique, nymphs present the terminal filament reduced (Dominguez et al., 2006). Importantly, adults of Camelobaetidius whose nymphs present the terminal filament reduced and a projection on the inner margin of the fore femora, as C. leentvaari Demoulin, the type-species, remain unknown.

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Nafis Syahmi Zainal Azali, Nuzaimah Mustafa, Ridhwan Jumaidin, Syahibudil Ikhwan Abdul Kudus, Nadlene Razali, Mastura Mohammad Taha, Yusliza Yusuf i Mohd Radzi Ali. "Thermal Properties of Wood Dust Fibre and Recycled Polypropylene (r-WoPPc) for Development of Thermoplastic Composites Filaments of Fused Deposition Modeling". Journal of Advanced Research in Fluid Mechanics and Thermal Sciences 96, nr 2 (23.07.2022): 42–50. http://dx.doi.org/10.37934/arfmts.96.2.4250.

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The thermal behaviour of filament materials is one of the most important characteristics to study to produce quality filament since the FDM process strongly relies on heating operations such as mixing and printing. To develop composite filament FDM using recycled polypropylene and wood dust fibre (r-WoPPc), the thermal properties of these recycled materials were investigated. Wood dust and recycled PP are by-products of the furniture and plastics industries, and their thermal characteristics may change during manufacturing. Furthermore, wood dust is typically subjected to several cleaning and treatment processes to have a cleaner and impurity-free dust as well as better adhesion with the recycled PP matrix, which both processes may affect its thermal properties. Therefore, TGA and DSC analyses are conducted to ensure its thermal properties before developing the filament. Untreated, NaOH and silane treated wood dust and recycled PP was subjected to TGA and DSC analyses. Wood dust treated with silane had the highest combustion resistance at 372°C compared to untreated wood dust at 360°C and NaOH treated at 320°C. Meanwhile, DSC analysis of recycled PP indicated that it melted at 167°C, which was used to establish the filament extrusion and printing temperatures. In a conclusion, these studies provided a point of reference for determining filament extrusion and printing temperatures.

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Harris, Elizabeth S., Fang Li i Henry N. Higgs. "The Mouse Formin, FRLα, Slows Actin Filament Barbed End Elongation, Competes with Capping Protein, Accelerates Polymerization from Monomers, and Severs Filaments". Journal of Biological Chemistry 279, nr 19 (29.02.2004): 20076–87. http://dx.doi.org/10.1074/jbc.m312718200.

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Formins are a conserved class of proteins expressed in all eukaryotes, with known roles in generating cellular actin-based structures. The mammalian formin, FRLα, is enriched in hematopoietic cells and tissues, but its biochemical properties have not been characterized. We show that a construct composed of the C-terminal half of FRLα (FRLα-C) is a dimer and has multiple effects on muscle actin, including tight binding to actin filament sides, partial inhibition of barbed end elongation, inhibition of barbed end binding by capping protein, acceleration of polymerization from monomers, and actin filament severing. These multiple activities can be explained by a model in which FRLα-C binds filament sides but prefers the topology of sides at the barbed end (end-sides) to those within the filament. This preference allows FRLα-C to nucleate new filaments by side stabilization of dimers, processively advance with the elongating barbed end, block interaction between C-terminal tentacles of capping protein and filament end-sides, and sever filaments by preventing subunit re-association as filaments bend. Another formin, mDia1, does not reduce the barbed end elongation rate but does block capping protein, further supporting an end-side binding model for formins. Profilin partially relieves barbed end elongation inhibition by FRLα-C. When non-muscle actin is used, FRLα-C's effects are largely similar. FRLα-C's ability to sever filaments is the first such activity reported for any formin. Because we find that mDia1-C does not sever efficiently, severing may not be a property of all formins.

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Monda, Emanuele, Martina Caiazza i Giuseppe Limongelli. "The Expanding Spectrum of FLNC Cardiomyopathy". Cardiogenetics 12, nr 4 (22.11.2022): 276–77. http://dx.doi.org/10.3390/cardiogenetics12040027.

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Schänzer, Anne, Elisabeth Schumann, Diana Zengeler, Lisann Gulatz, Giovanni Maroli, Uwe Ahting, Anke Sprengel i in. "The p.Ala2430Val mutation in filamin C causes a "hypertrophic myofibrillar cardiomyopathy"". Journal of Muscle Research and Cell Motility 42, nr 2 (12.03.2021): 381–97. http://dx.doi.org/10.1007/s10974-021-09601-1.

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