Relevant bibliographies by topics / Filamine C

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Filamine C'

Author: Grafiati
Published: 25 May 2024

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Journal articles on the topic "Filamine C"

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Kopishinskaia, S. V., A. A. Lesnikova, D. I. Abramova, and I. A. Velichko. "Filaminopathy type C." Medical alphabet, no. 33 (January 14, 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, and Fumihiko Nakamura. "Structure and Function of Filamin C in the Muscle Z-Disc." International Journal of Molecular Sciences 21, no. 8 (April 13, 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, and Christopher A. McCulloch. "Filamin A is required for vimentin-mediated cell adhesion and spreading." American Journal of Physiology-Cell Physiology 298, no. 2 (February 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, and Alessandro Zorzi. "Filamin C." JACC: Clinical Electrophysiology 4, no. 4 (April 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, and Ulla Pentikäinen. "The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended." Biochemical Journal 446, no. 2 (August 14, 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, and Stuart A. Cook. "Truncating Variants in Filamin C." Journal of the American College of Cardiology 68, no. 22 (December 2016): 2452–53. http://dx.doi.org/10.1016/j.jacc.2016.05.105.

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Holmes, William B., and Carole L. Moncman. "Nebulette interacts with filamin C." Cell Motility and the Cytoskeleton 65, no. 2 (February 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, and Ju Chen. "Filamin C is Essential for mammalian myocardial integrity." PLOS Genetics 19, no. 1 (January 27, 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, and Peter F. M. van der Ven. "Filamin C-related myopathies: pathology and mechanisms." Acta Neuropathologica 125, no. 1 (October 30, 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, no. 4 (October 1, 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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Dissertations / Theses on the topic "Filamine C"

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Ader, Flavie. "Identification de variants du gène FLNC dans les cardiomyopathies humaines et modélisations fonctionnelles chez la drosophile et dans des pseudo-tissus cardiaques." Electronic Thesis or Diss., Sorbonne université, 2021. http://www.theses.fr/2021SORUS371.

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Des variants du gène FLNC ont été impliqués dans le développement de cardiomyopathies (CM), toutefois les mécanismes de physiopathologie ne sont pas entièrement élucidés. Ce travail a comporté la caractérisation génétique d’une cohorte clinique puis le développement d’un modèle cellulaire et d’un modèle Drosophile pour confirmer la pathogénicité de variants faux sens et d’évaluer les conséquences fonctionnelles des mutants FLNC. L’étude de 1150 patients atteints de CM a permis d’établir la prévalence du gène FLNC entre 1 et 8 %. De plus, les variants tronquants ont été associés préférentiellement à des CM dilatées (CMD) avec un risque rythmique accru et les variants faux sens (régionalisés dans le ROD2 de la protéine) à des CM hypertrophiques (CMH). Chez la drosophile, la perte de fonction de l’orthologue du gène FLNC (ARN interférence) a montré une dilatation cardiaque et une diminution de la fraction d’éjection chez l’adulte, associées à une désorganisation des sarcomères et du réseau d’actine. Les 3 variants faux sens sélectionnés, identifiés dans des CMH, et introduits par CRISPR/Cas9 dans des Drosophiles n’ont pas montré d’effet fonctionnel ou histologique significatif. L’étude de lignées produisant une protéine tronquée a permis d’établir que le domaine C-terminal de la filamine n’était pas requis pour la fonction cardiaque chez la Drosophile. Un clone hiPSC édité par CRISPR/Cas9 portant une délétion homozygote du site d’épissage de l’exon 42 qui aboutit à un saut en phase de l’exon a été différencié en cardiomyocytes. Les cardiomyocytes amplifiés ont permis de former des pseudo-tissus cardiaques battant dont l’analyse a montré une modification du phénotype rythmique qui correspondrait à un phénotype de CMD. En conclusion, ce travail a permis de montrer l’importance du gène FLNC dans le développement des CM et de développer 2 nouveaux modèles pour étudier les mécanismes de pathogénicité et développer des thérapeutiques ciblées
Variants of FLNC gene have been implicated in the development of cardiomyopathies (CM), however the pathophysiological mechanisms are not fully understood. This work involved the genetic characterization of a clinical cohort and then the development of a cell model and a Drosophila model to confirm the pathogenicity of missense variants and to assess the functional consequences of FLNC mutants. The study of 1150 patients with CM found the prevalence of FLNC gene to be between 1 and 8%. In addition, the truncating variants were preferentially associated with dilated CMs (DCM) with an increased rhythmic risk, and the missense variants (regionalized in the ROD2 of the protein) with hypertrophic CMs (MHC). In Drosophila, loss of function of the ortholog of FLNC gene (RNA interference) showed cardiac dilation and a decrease of the fractionnal shortening in adults, associated with disorganization of the sarcomeres and the actin network. The 3 selected missense variants, identified in MHCs, and introduced by CRISPR / Cas9 in Drosophila did not show any significant functional or histological effect. Study of lines producting a truncated protein revealed that the C-terminal domain of filamine was not required for heart function in Drosophila. A CRISPR / Cas9 edited hiPSC clone carrying a homozygous deletion of the exon 42 splice site that results in exon phase skiping was differentiated into cardiomyocytes. The amplified cardiomyocytes formed beating cardiac pseudo-tissues, and their analysis showed a change in rhythmic phenotype corresponding to DCM patients pattern. In conclusion, this work made it possible to show the importance of the FLNC gene in the development of CM and to develop 2 new complementary models to study the mechanisms of pathogenicity and develop targeted therapies
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Cawston, Erin, and n/a. "A role for filamin-C in the function of the type 2A serotonin receptor." University of Otago. Dunedin School of Medicine, 2008. http://adt.otago.ac.nz./public/adt-NZDU20080313.141311.

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The serotonin receptor 2A (5-HT₂[A]) is a member of the G-protein coupled receptor family and is of interest due to its role in physiological functions such as smooth muscle contraction, platelet aggregation, thermoregulation, learning and memory. More importantly, 5-HT₂[A] has also been implicated in CNS disorders including schizophrenia, depression and anxiety. A yeast two-hybrid screen had previously been carried out to identify proteins that interacted with 5-HT₂[A] and therefore may modulate intracellular function. The cytoskeletal actin-binding protein filamin-C was identified as a possible 5-HT₂[A] interacting partner. The aim of the research in this thesis was to further investigate the potential interaction between 5-HT₂[A] and filamin-C and to investigate functional roles for the interaction. A fragment of human filamin-C, aa 2162-2725, was shown to interact with the C-terminus of human 5-HT₂[A] using two in vitro techniques, the yeast-two hybrid system and a GST capture assay. The region of filamin-C needed to bind to 5-HT₂[A] was narrowed to the start of repeat 20, aa 2251, through to aa 2424 at the beginning of repeat 22 and comprises 182 residues. The 5-HT₂[A] region needed to bind to filamin-C was ascertained via yeast two-hybrid to be 31 amino acids between 394-423. Work was performed to determine whether FLNC mRNA was expressed in neural and glial cells and whether FLNC and HTR2A mRNA were co-expressed in any cells. FLNC mRNA was identified in seven out of eight neural and glial cell lines and western blot analysis confirmed this finding at the protein level. Two cell lines, U-118MG and A172, were found to contain both HTR2A and FLNC mRNA. Co-immunoprecipitation experiments showed endogenous filamin-C bound to endogenous 5-HT₂[A] and this complex could be precipitated using anti-filamin-C antibody. Additionally, a GST-5-HT₂[A] fusion complex was found to bind to endogenous filamin-C from U-118MG cells. Immunofluorescent labelling of cells was used to study filamin-C and 5-HT₂[A] proteins in vivo. U-118MG cells showed staining for 5-HT₂[A] around the membrane of the cell, as well as in the cytoplasm, whereas filamin-C staining occurred in the cytoplasm. Co-localisation analysis identified some areas of overlap between 5-HT₂[A] and filamin-C in the cytoplasm of U-118MG cells. The functional role for the 5-HT₂[A]/filamin-C colocalisation was investigated. It was postulated that filamin-C may be involved in the internalisation of 5-HT₂[A]. To test this hypothesis, an in vivo model system was used to investigate whether disruption of the filamin-C/5-HT₂[A] interaction affects internalisation of the receptor. The key preliminary findings of this study, which used expression of a competitor peptide, to disrupt and co-interact, suggested that the filamin-C/5-HT₂[A] interaction is not essential for the internalisation of receptors in response to ligand binding. However, this interaction was important for delivery or maintenance of 5-HT₂[A] to the cell membrane, and expression of the competing peptide caused an accumulation of cytoplasmic 5-HT₂[A].
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Yang, Yuanzhang, and Yuanzhang Yang. "Ca2+/CaM Modulates the Functional Effects of cMyBP-C on the Thin Filament." Thesis, The University of Arizona, 2017. http://hdl.handle.net/10150/626398.

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Background. Cardiac myosin binding protein-C (cMyBP-C) is an essential regulator of heart muscle function that is necessary for both normal contraction and for increased contractility in response to inotropic stimuli(1-7). Effects of cMyBP-C on contraction are due to dynamic interactions of cMyBP-C with both actin and myosin, but the mechanism(s) by which cMyBP-C binding to these ligands is modulated are only partly understood. Recently, calmodulin (CaM) was shown to bind to cMyBP-C in the regulatory M-domain(8, 9) near a conserved actin binding site(10). Here we investigated whether CaM competes with actin for binding to cMyBP-C and thus whether CaM affects cMyBP-C function. Methods. Recombinant N’-terminal domains of cMyBP-C were used in pull-down assays, co-sedimentation binding assays, and actin activated myosin ATPase assays to determine effects of CaM binding on cMyBP-C. Results. In accordance with previous reports, we found that CaM binds to N’-terminal domains of cMyBP-C in the presence of Ca2+ (Ca2+/CaM) with a binding affinity comparable to cMyBP-C binding to actin (3-10 μM). We further show that Ca2+/CaM reduces cMyBP-C apparent binding affinity for actin, consistent with the competition between Ca2+/CaM and actin for binding to cMyBP-C. Ca2+/CaM also reversed the inhibitory effects of cMyBP-C N’-terminal domains on actin activated myosin ATPase rates, consistent with reduced cMyBP-C interactions with actin. However, apo-CaM (calcium-free calmodulin) did not influence the ability of cMyBP-C to activate actomyosin ATPase rates at low Ca2+. Phosphorylation of cMyBP-C by PKA significantly increased its binding to both Ca2+/CaM and apo-CaM. Phosphorylated cMyBP-C was also a less potent regulator of cross-bridge cycling in ATPase assays. Conclusions. These data demonstrate that Ca2+/CaM competes with actin for binding to cMyBP-C and selectively reverses the inhibitory effects of cMyBP-C on actomyosin interactions. However, apo-CaM does not compete with cMyBP-C binding to actin and does not affect the ability of cMyBP-C to activate the thin filament at low Ca2+. Ca2+/CaM may serve as additional regulatory mechanism in addition to phosphorylation of cMyBP-C to regulate its function. These data suggest that Ca2+/CaM is a novel modulator of cMyBP-C function that can dynamically tune cMyBP-C effects on contraction potentially as [Ca2+]i rises and falls during the time course of a single heart beat.
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Deville, Sara Sofia. "The intermediate filament synemin promotes non-homologous end joining in an ATM-dependent manner." Technische Universität Dresden, 2019. https://tud.qucosa.de/id/qucosa%3A72378.

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Background: Therapy resistance is a great challenge in cancer treatment. Among numerous factors, cell adhesion to extracellular matrix is a well-known determinant of radiochemo-resistance. It has been shown that targeting focal adhesion proteins (FAPs), e.g. β1 integrin, enhances tumor cell radio(chemo)sensitivity in various entities such as head and neck squamous cell carcinoma (HNSCC), lung carcinoma, glioblastoma, breast carcinoma and leukemia. Previous studies demonstrated a functional crosstalk between specific FAPs and DNA repair processes; however, the molecular circuitry underlying this crosstalk remains largely unsolved. Hence, this study in HNSCC aimed to identify alternative FAPs associated with DNA damage repair mechanisms and radioresistance. Materials and Methods: A novel 3D High Throughput RNAi Screen (3DHT-RNAi-S) using laminin-rich extracellular matrix (lrECM) was established to determine radiation-induced re-sidual DNA double strand breaks (DSBs; foci assay) and clonogenic radiation survival. In the screen, we used UTSCC15 HNSSC cells stably expressing the DSB marker protein 53BP1 tagged to pEGFP. Validations were performed in 10 additional HNSCC cell lines (Cal33, FaDu, SAS, UTSCC5, UTSCC8, UTSCC14, UTSCC15, UTSCC45 and XF354fl2) grown in 3D lrECM. Immunofluorescence staining, immunoblotting, chromatin fractionation were utilized to evaluate protein expression, dynamics and kinetics post irradiation. Investigations of molecular mechanisms of DNA repair and radio(chemo)resistance employed DSB repair reporter assays for non-homologous end joining (NHEJ) and homologous recombination (HR), cell cycle analysis, chromatin fractionation levels evaluation and kinase activity profiling (PamGene) upon protein knockdown in combination with/-out X-ray exposure. Foci assay and clonogenic survival assay were performed after single or multiple knockdowns of synemin and associated proteins such as DNA-PKcs and c-Abl. Protein-protein interactions between synemin and associated proteins were determined using immunoprecipitation and proximity ligation assay. Mutant/depletion constructs of synemin (ΔLink-Tail, ΔHead-Link, Synemin_301-961, Synemin_962-1565, S1114A and S1159A) were generated in order to identify essential synemin’s sites controlling DNA repair functions. Results: Among the targets found in the 3DHT-RNAi-S, synemin was one of the most promising FAP candidates to determine HNSCC cell survival and DNA damage repair. Synemin silencing radiosensitized HNSCC cells, while its exogenous overexpression induced radio-protection. Radiation induced an increased synemin/chromatin interaction and a marked ac-cumulation of synemin in the perinuclear area. Intriguingly, synemin depletion elicited a 40% reduction in NHEJ activity without affecting HR or Alt-EJ. In line, ATM, DNA-PKcs and c-Abl phosphorylation as well as Ku70 expression strongly declined in synemin depleted and irra-diated cells relative to controls, whereas an opposite effect was observed under synemin overexpression. Single, double and triple depletion of synemin, DNA-PKcs and c-Abl resulted in a similar radiosensitizing effect and DSB levels as detected upon single knockdown of synemin, describing its upstream role. In kinome analysis, tyrosine kinases showed signifi-cantly reduced activity after synemin silencing relative to controls. Furthermore, immunoprecipitation assays revealed a protein complex formed between synemin, DNA-PKcs and c-Abl under pre- and post-irradiation conditions. This protein complex dispersed when ATM was pharmacologically inhibited, implying synemin function to be dependent on ATM kinase activity. By means of the different mutation/deletion constructs of synemin, the phosphorylation site at serine 1114 located on the distal portion of synemin’s tail was identified as essential protein-protein interaction site for synemin’s function in DNA repair. Conclusions: The established 3DHT-RNAi-S provides a robust screening platform for identifying novel targets involved in therapy resistance. Based on this screen and detailed mechanistic analyses, the intermediate filament synemin was discovered as a novel important determinant of DNA repair, tyrosine kinase activity and radiochemoresistance of HNSCC cells. These results further support the notion that DNA repair is controlled by cooperative interactions between nuclear and cytoplasmic proteins.
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Norman, Catalina. "Influence of the thin filament calcium activation on muscle force production and rate of contraction in cardiac muscle." Columbus, Ohio : Ohio State University, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1178751966.

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Schubert, Jeffrey A. B. S. "The Use of Genetic Analyses and Functional Assays for the Interpretation of Rare Variants in Pediatric Heart Disease." University of Cincinnati / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1535724045195581.

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McNamara, James W., Amy Li, Nicola J. Smith, Sean Lal, Robert M. Graham, Kristina Bezold Kooiker, Dijk Sabine J. van, Cristobal G. dos Remedios, Samantha P. Harris, and Roger Cooke. "Ablation of cardiac myosin binding protein-C disrupts the super-relaxed state of myosin in murine cardiomyocytes." ELSEVIER SCI LTD, 2016. http://hdl.handle.net/10150/621325.

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Cardiac myosin binding protein-C (cMyBP-C) is a structural and regulatory component of cardiac thick filaments. It is observed in electron micrographs as seven to nine transverse stripes in the central portion of each half of the A band. Its C-terminus binds tightly to the myosin rod and contributes to thick filament structure, while the N-terminus can bind both myosin S2 and actin, influencing their structure and function. Mutations in the MYBPC3 gene (encoding cMyBP-C) are commonly associated with hypertrophic cardiomyopathy (HCM). In cardiac cells there exists a population of myosin heads in the super-relaxed (SRX) state, which are bound to the thick filament core with a highly inhibited ATPase activity. This report examines the role cMyBP-C plays in regulating the population of the SRX state of cardiac myosin by using an assay that measures single ATP turnover of myosin. We report a significant decrease in the proportion of myosin heads in the SRX state in homozygous cMyBP-C knockout mice, however heterozygous cMyBP-C knockout mice do not significantly differ from the wild type. A smaller, non-significant decrease is observed when thoracic aortic constriction is used to induce cardiac hypertrophy in mutation negative mice. These results support the proposal that cMyBP-C stabilises the thick filament and that the loss of cMyBP-C results in an untethering of myosin heads. This results in an increased myosin ATP turnover, further consolidating the relationship between thick filament structure and the myosin ATPase. Crown Copyright (C) 2016 Published by Elsevier Ltd. All rights reserved.
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Kulkarni, Apoorv Sandeep. "Ceramic Si-C-N-O cellular structures by integrating Fused Filament Fabrication 3-D printing with Polymer Derived Ceramics." Doctoral thesis, Università degli studi di Trento, 2022. http://hdl.handle.net/11572/349905.

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Ceramic additive manufacturing is gaining popularity with methods like selective laser sintering (SLS), binder jetting, direct ink writing and stereolithography, despite their disadvantages. Laser sintering and binder jetting are too expensive, while direct ink writing lacks resolution and stereolithography lacks scalability. The project aims to combine one of the most versatile, affordable, and readily available 3D printing methods: fused filament fabrication (FFF) with polymer derived ceramics to produce cellular ceramics to overcome the disadvantages posed by the other methods. The process uses a two-step approach. The first step is to 3D print the part using a polymer FFF 3D printer with a thermoplastic polyurethane filament and the second step is to impregnate the part in a polysilazane preceramic polymer and then pyrolyze it in an inert environment up to 1200C. The resulting product is a high-resolution cellular ceramic of the composition SiOC(N). This type of cellular ceramic can find an application in several fields such as scaffolds for bone tissue regeneration, liquid metal filtering, chemical and gas filtering, catalytic converters and electric applications. The process can provide an affordable alternative to the products used in these fields currently.
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Farah, Chuck Shaker. "Funções estruturais e regulatórias das regiões N- e C-terminal da troponina I." Universidade de São Paulo, 1994. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-08082012-152838/.

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O complexo troponina-tropomiosina regula a contração muscular esquelética e cardíaca. A ligação do cálcio nos sítios regulatórios localizados no domínio N-terminal da troponina C (TnC) induz uma mudança conformacional que remove a ação inibitória da troponina I (TnI) e inicia a contração muscular. Nós usamos fragmentos recombinantes da TnI e uma série de mutantes da TnC para estudar as interações estruturais e regulatórias das diferentes regiões da TnI com os domínios da TnC, TnT e actina-tropomiosina. Nossos resultados indicam que a TnI é organizada em regiões que apresentam funções estruturais e regulatórias e que se ligam de modo antiparalelo com os correspondentes domínios estruturais e regulatórios da TnC. Estudos funcionais mostram que a região inibitória (aminoácidos 103-116) em combinação com a região C-terminal da TnI (TnI103-182) pode regular a atividade ATPásica da acto-miosina de maneira dependente de Ca2+. A regulação não é observada com a região inibitória em combinação com a região N-terminal (TnI116) Estudos de ligação mostram que a região N-terminal da TnI (TnI1-98) interage com o domínio C-terminal da TnC na presença e na ausência de Ca2+ e também interage com a TnT. A região inibitória/C-terminal da TnI (TnI103-182) interage com o domínio N-terminal da TnC de maneira dependente de Ca2+. Baseados nestes resultados, propomos um modelo para a mudança conformacional induzida pelo Ca2+. Neste modelo, a região N-terminal da TnI está ligada fortemente com o domínio C-terminal da TnC na presença ou na ausência de Ca2+. As regiões inibitórias e C-terminal da TnI ligam-se à actina-tropomiosina na ausência de Ca2+ e nos domínios N-terminal e C-terminal da TnC na presença de Ca2+.
The troponin-tropomyosin complex regulates skeletal and cardiac muscle contraction. Calcium binding to the regulatory sites in the N-terminal domain of troponin C (TnC). induces a conformational change which removes the inhibitory action of troponin I (TnI) and initiates muscular contraction. We used recombinant TnI fragments and a series of TnC mutants to study the structural and regulatory interactions between different TnI regions and the domains of TnC, TnT and actin-tropomyosin. Our results indicate that TnI is organized into regions with distinct structural and regulatory functions which bind, in an antiparallel manner, with the corresponding structural and regulatory domains of TnC. Functional studies show that a fragment containing the inhibitory and C-terminal regions of TnI (TnIl03-182) can regulate the actomyosin ATPase in a Ca2+- dependent manner. Regulation was not observed with a fragment containing the N-terminal and inhibitory regions (TnIl-116). Binding studies show that the N-terminal region of TnI (TnI1-98) interacts with the C-terminal domain of TnC in the presence of Ca2+ or Mg2+. The inhibitory/C-terminal region of TnI (TnI103-182) binds to the N-terminal domain of TnC in a Ca2+-dependent manner. Based on these results, we propose a model for the Ca2+ -induced conformational change. In this model the N-terminal region of TnI is bound strongly to the C-terminal domain of TnC in the presence or absence of Ca2+. The inhibitory and C-terminal regions of TnI bind to actin-tropomyosin in the absence of Ca2+ and to tne N- and C-terminal domains of TnC in the presence of Ca2+.
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Robinson, Paul John Robert. "The functional effect of disease causing mutations on thin filament regulatory proteins tropomyosin, troponin T troponin I and troponin C." Thesis, University of Oxford, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.670117.

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Book chapters on the topic "Filamine C"

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Breede, Fabian, Raouf Jemmali, Heinz Voggenreiter, and Dietmar Koch. "Design and Testing of a C/C-Sic Nozzle Extension Manufactured Via Filament Winding Technique and Liquid Silicon Infiltration." In Ceramic Transactions Series, 1–14. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2014. http://dx.doi.org/10.1002/9781118889770.ch1.

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Breede, Fabian, Severin Hofmann, Enrico Klatt, and Sandrine Denis. "Influence of Fiber Orientation on the Mechanical Properties and Microstructure of C/C-SiC Composite Plates Produced by Wet Filament Winding Technique." In Ceramic Transactions Series, 1–10. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118144442.ch1.

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Nairn, Angus C., and Alan Aderem. "Calmodulin and Protein Kinase C Cross-Talk: The MARCKS Protein is an Actin Filament and Plasma Membrane Cross-Linking Protein Regulated by Protein Kinase C Phosphorylation and by Calmodulin." In Ciba Foundation Symposium 164 - Interactions Among Cell Signalling Systems, 145–61. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514207.ch10.

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Celio, Marco R. "Troponin C." In Guidebook to the Calcium-binding Proteins, 175–78. Oxford University PressOxford, 1996. http://dx.doi.org/10.1093/oso/9780198599517.003.0022.

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Abstract Troponin C (TnC) is an EF-hand Cal+-binding protein that is a constitutive subunit of the troponin complex on the thin filament of striated muscle. Cyclic binding and release of Cal• from the N-terminal Cal•-binding sites of TnC regulates muscle contraction. There are two isoforms of TnC (see Fig. 1); one is expressed in fast skeletal muscle (sTnC), while another is expressed in cardiac and slow skeletal muscle (cTnC) (for reviews see Leavis and Gergely 1984; Collins 1991; Gergely et al. 1993). The molecular weights of human sTnC and cTnC are 18,102 and 18,382, respectively, with isoelectric points between 4.1 and 4.6. Troponin C, together with troponin I (Tnl) and troponin T (TnT), form the heterotrimer troponin complex which is bound to the thin filament of striated muscle near the overlap region between adjacent tropomyosin dimers.
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Dowling, James, and Elaine Fuchs. "BPAG1." In Guidebook to the Cytoskeletal and Motor Proteins, 329–32. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.00106.

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Abstract The BPAG1 gene locus encodes two major isoforms which share a common C terminal intermediate filament binding domain. The 230 kDa epidermal splice variant, BPAG1e, is a major component of the inner plaque portion of the hemidesmosome and is required for stable interaction of this junction with keratin filaments. The 280 kDa neuronal isoform, BPAG1 n, contains a bona fide actin-binding domain in addition to the intermediate filament binding domain and is essential for primary sensory neurone function. Both BPAG1e and BPAG1n are members of a growing family of intermediate filament linker proteins that also includes desmoplakin, envoplakin, and plectin.
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Cohen, Carolyn. "Paramyosin." In Guidebook to the Cytoskeletal and Motor Proteins, 478–80. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.00144.

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Abstract Genetic experiments in C elegans indicate that paramyosin is probably essential for the functional organization of invertebrate thick filaments. There is a rough correlation between thick filament length and paramyosin content. Since tension development in a muscle is proportional to thick filament length, muscles with large amounts of paramyosin develop large tensions. These same muscles are specialized for catch contraction, and it has been suggested that paramyosin may have a role in this mechanism.
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Flood, David R. Critchley,Geoffrey. "α-Actinins." In Guidebook to the Cytoskeletal and Motor Proteins, 24–26. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.0005.

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Abstract α-Actinin displays homology with erythroid and non-erythroid spectrins, dystrophin, and utrophin. These proteins all share a similar domain structure, with an N-terminal actin-binding domain, a variable number of triple α-helical spectrin-like repeats, and a pair of C-terminal EF hands. The actin-binding domain of α-actinin is homologous to that in filamin, fimbrin, and ABP 120, and there is a more limited match with the N-terminal domain of calponin.
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Bin Maidin, Shajahan, Zulkeflee Abdullah, and Ting Kung Hieng. "Investigation of Recycled Acrylonitrile Butadiene Styrene for Additive Manufacturing." In Advances in Environmental Engineering and Green Technologies, 130–54. IGI Global, 2020. http://dx.doi.org/10.4018/978-1-7998-1374-3.ch007.

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One of the disadvantages of fused deposition modeling (FDM) is waste produced during the printing processes. This investigation focuses on using 100% recycled Acrylonitrile Butadiene Styrene (ABS) for the FDM process. The recycling begins with re-granule the waste ABS material and produces it into a new filament. The new recycled filament was used to print the test specimen. Investigation on the mechanical properties and the surface quality of the test specimen and comparison with standard ABS specimen was done. The result shows that the recycled ABS can be produced into filament with 335°C of extrusion temperature and 1.5 mm/s travel speed of the extruder conveyor. The surface roughness of recycled specimen is 6.94% higher than the standard ABS specimen. For ultimate tensile strength, there is a small difference in X and Y orientation between the standard and the recycled ABS specimen which are 22.93% and 19.98%, respectively. However, in Z orientation, it is 52.33% lower. This investigation proves that ABS can be recycled without significantly affecting its mechanical properties.
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Alpert, Norman R., Gerd Hasenfuss, Christian Holubarsch, and Louis A. Mulicri. "Energetic aspects of altering myocardial sensitivity to calcium." In Modulation of Cardiac Calcium Sensitivity, 320–28. Oxford University PressNew York, NY, 1993. http://dx.doi.org/10.1093/oso/9780192623478.003.0014.

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Abstract It is now generally accepted that myocardial contraction is preceded by and causally related to an increase in cytosolic free calcium following depolarization of the plasma membrane. Relaxation occurs when the free calcium concentration is lowered by the sarcoplasmic reticulum and plasma membrane calcium pumps. The degree of contractile activation depends on the level of free calcium and the calcium sensitivity of the thin-filament regulatory protein troponin C.
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Sellers, James R. "Myosin binding proteins." In Myosins, 87–90. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198505099.003.0006.

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Abstract There are many proteins that interact with class II myosins (Table 16). The most studied interactions are the proteins that bind in a regular manner to vertebrate skeletal muscle thick filaments. These include MyBP-C (formerly known as C protein), M-protein, creatine phosphokinase, myomesin, MyBP-H (H-protein, 86-kDa protein), and titin. Electron micrographs of thick filaments show eleven transverse stripes that begin just inside the bare zone (0.07 µm from the centre of the thick filament) and are spaced at 43 nm intervals [1422,1444]. MyBP-C is located in seven of these bands (5-11) and is found in both fast and slow muscles [2368,2379]. MyBP-H, also called 86-kDa protein, also labels the stripes, but the labelling pattern varies between chicken and rabbit muscles [2364,2368]. Molecular cloning indicates that MyBP-H and MyBP-C share significant homology, both having C2-type IgG and type II fibronectin homology regions [2453,2475]. MyBP-C interacts with myosin primarily through its carboxyl-terminal portion via a particular set of IgG repeats [2392].
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Conference papers on the topic "Filamine C"

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Roschli, A., M. Borish, B. Post, P. Chesser, J. Heineman, and C. Atkins. "Design for Slicing in Large Format Fused Filament Fabrication." In CAMX 2019. NA SAMPE, 2019. http://dx.doi.org/10.33599/nasampe/c.19.0707.

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Schuld, J., Z. Orfanos, F. Chevessier, B. Eggers, G. Kirfel, PFM van der Ven, A. Unger, et al. "Sarkomerische Pathologie durch die homozygote Expression der Myofibrilläre Myopathie-assoziierten W2711X Filamin-C Mutante." In 24. Kongress des Medizinisch-Wissenschaftlichen Beirates der Deutschen Gesellschaft für Muskelkranke (DGM) e.V. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1684974.

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PINEDA, EVAN J., MAREK FASSIN, BRETT A. BEDNARCYK, STEFANIE REESE, and JAAN-WILLEM SIMON. "Comparison of Multiscale Method of Cells-Based Models for Predicting Elastic Properties of Filament Wound C/C-SiC." In American Society for Composites 2017. Lancaster, PA: DEStech Publications, Inc., 2017. http://dx.doi.org/10.12783/asc2017/15333.

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Berretta, S., O. Lietaer, R. McKay, and C. Strasser. "Leveraging simulation and soluble support to 3D print semicrystalline thermoplastic polymers in cold chamber using filament fusion." In CAMX 2023. NA SAMPE, 2023. http://dx.doi.org/10.33599/nasampe/c.23.0148.

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Fujita, Takeshige, Takeo Ichihara, Tomio Tanaka, and Tsutomu Yamamoto. "Development of 2-Lamp System Headlamp Using Halogen Bulb with C-8/C-8 Filament Structure and Multi-Focus Reflector." In SAE International Congress and Exposition. 400 Commonwealth Drive, Warrendale, PA, United States: SAE International, 1988. http://dx.doi.org/10.4271/880274.

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Belduque, M., M. Khadka, J. Khan, A. Sargordi, J. Tate, and R. Woods. "Mechanical Properties of Extruded PA12 and SrFe12O19 Filaments Via Twin-Screw Extrusion for Magnetic Field Assisted Fused Filament Fabrication." In CAMX 2022. NA SAMPE, 2022. http://dx.doi.org/10.33599/nasampe/c.22.0136.

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Devra, Rajdeep Singh, Nishkarsh Srivastava, Madhu Vadali, and Amit Arora. "Polymer Filament Extrusion Using LDPE Waste Polymer: Effect of Processing Temperature." In ASME 2022 17th International Manufacturing Science and Engineering Conference. American Society of Mechanical Engineers, 2022. http://dx.doi.org/10.1115/msec2022-85586.

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Abstract Low-density polyethylene (LDPE) is a soft thermoplastic with extensive application as a packing material such as plastic bags, dispensing bottles, milk pouches, etc. Many LDPE bags are used and dumped in landfills every year, leading to millions of tons of persistent waste. In addition, the recycling of LDPE is of no commercial interest due to its low stiffness, poor mechanical properties, and limited commercial application. In the current work, we attempt to recycle milk pouches made of LDPE to create polymer filaments for fused deposition modeling (FDM), thereby adding value to waste plastic by converting it into high-value 3D printer filament. This research examines the feasibility of reclamation of waste LDPE milk pouches as filament for 3D printers and studies the changes in filament’s chemical and mechanical properties when produced at different temperatures. The waste milk pouches are cleaned thoroughly, shredded, and extruded using a single screw extruder at three nozzle temperatures, i.e., 150°C, 180°C, 210°C. The extruded specimens are analyzed using an optical microscope and scanning electron microscope (SEM) for surface texture. The effect of change in process temperature on flow behaviors is also studied by integrating a current sensor and an encoder. Fourier transform infrared spectroscopy (FTIR) analysis is performed on the filaments and the used LDPE milk pouches to compare the chemical bondings of the polymer. The mechanical properties of the extruded filaments are examined using dynamic mechanical analysis (DMA). The morphological analysis, chemical characterization, and mechanical characterization of prepared filaments are presented. The results show that the chemical bondings are intact after extrusion at all the temperatures examined in this work. The surface texture and the mechanical properties are better at higher temperatures owing to better fluidity and are more suitable for fused deposition modeling. Thus, it is possible to valorize waste LDPE milk pouches by transforming them into filaments for 3D printing.
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Mit'ko, S. V., F. A. van Goor, A. R. van der Holst, W. J. Witteman, and V. N. Ochkin. "Formed-ferrite plasma source for optical pumping the XeF (C→A) laser." In The European Conference on Lasers and Electro-Optics. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/cleo_europe.1994.ctub2.

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The most important problem encountered in the design of the blue-green optically pumped XeF (C→A) laser is the development of a reliable light source with maximum energy emission at wavelengths between 150 and 160 nm, a geometrical length of ~1 m, and permitting operation in pulse-repetitive mode. A linear formed ferrite plasma source fulfilling these requirements has been developed and tested. To excite the high-brightness light source we used an 800-mm-long ferrite rod, assembled from 1.7 × 4 × 140-mm-long ferrite strips placed end to end, to guide the high-current surface discharge. The ferrite rod was placed near the wall of the 50-mm diameter laser tube, which was made of teflon. The conductive path on the surface of each ferrite strip was prepared by a method, described in Ref. 1. To prevent broadening of the conductive filament due to the discharge plasma, we embedded the ferrite strips in alumina.
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Freeman, Thomas B., Kaloki Nabutola, David Spitzer, Patrick N. Currier, and Sandra K. S. Boetcher. "3D-Printed PCM/HDPE Composites for Battery Thermal Management." In ASME 2018 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2018. http://dx.doi.org/10.1115/imece2018-86081.

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Phase-change materials (PCMs) are a useful alternative to more traditional methods of thermal management of Li-ion batteries in electric or hybrid-electric vehicles. PCMs are materials which absorb large amounts of latent heat and undergo solid-to-liquid phase change at near-constant temperature. The goal of the research is to experimentally investigate the thermal properties of a novel shape-stabilized PCM/HDPE composite extruded filament. The extruded filament can then be used in a 3D printer for custom PCM/HDPE shapes. The PCM used in the study is PureTemp PCM 42, which is an organic-based material that melts around 42° C. Four PCM/HDPE mixtures were investigated (all percentages by mass): 20/80, 30/70, 40/60, and 50/50. Preliminary findings include differential scanning calorimeter (DSC) measurements of melting temperature and latent heat as well as scanning electron microscope (SEM) pictures of filament composition.
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"Delineating molecular mechanisms of c-FLIP isoforms as control checkpoints of DED filament assembly and caspase-8 activation." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-592.

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