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Academic literature on the topic 'Tropomyosins'

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Published: 4 June 2021
Last updated: 21 February 2023

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Journal articles on the topic "Tropomyosins"

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Papia, Francesco, Chiara Bellia, and Carina Gabriela Uasuf. "Tropomyosin: A panallergen that causes a worldwide allergic problem." Allergy and Asthma Proceedings 42, no. 5 (September 1, 2021): e145-e151. http://dx.doi.org/10.2500/aap.2021.42.210057.

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Background: Panallergens are proteins that take part in key processes of organisms and, therefore, are ubiquitously distributed with highly conserved sequences and structures. One class of these panallergens is composed of the tropomyosins. The highly heat-stable tropomyosins comprise the major allergens in crustaceans and mollusks, which make them important food allergens in exposed populations. Tropomyosins are responsible for a widespread immunoglobulin E cross-reactivity among allergens from different sources. Allergic tropomyosins are expressed in many species, including parasites and insects. Methods: This panallergen class is divided, according to it capacity of induced allergic symptoms, into allergenic or nonallergenic tropomyosin. Although vertebrate tropomyosins share ∼55% of sequence homology with invertebrate tropomyosins, it has been thought that the invertebrate tropomyosins would not have allergic properties. Nevertheless, in recent years, this opinion has been changed. In particular, tropomyosin has been recognized as a major allergen in many insects. Results: A high grade of homology has been shown among tropomyosins from different species, such as crustaceans and insects, which supports the hypothesis of cross-reactivity among tropomyosins from divergent species. Moreover, the emerging habit of consuming edible insects has drawn the attention of allergists to invertebrate tropomyosin protein due to its potential allergenic risk. Nevertheless, evidence about tropomyosin involvement in clinical allergic response is still scarce and deserves more investigation. Conclusion: This review intended to report allergic reactions associated with different tropomyosins when considering house dust mites, parasites, seafood, and insects, and to summarize our current knowledge about its cross-reactivity because this could help physicians to accurately diagnose patients with food allergy.
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Fenderson, P. G., V. A. Fischetti, and M. W. Cunningham. "Tropomyosin shares immunologic epitopes with group A streptococcal M proteins." Journal of Immunology 142, no. 7 (April 1, 1989): 2475–81. http://dx.doi.org/10.4049/jimmunol.142.7.2475.

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Abstract Tropomyosin is an alpha-helical coiled-coil protein with structural similarities to the streptococcal M protein. In order to show serologic cross-reactivity between streptococcal M proteins and tropomyosin, we selected from a panel of murine mAb those which reacted with M proteins and tropomyosins in the ELISA. Western blots were used to study the reactions of each mAb with human and rabbit cardiac and rabbit skeletal tropomyosins. The antibodies were further characterized for their reactions with the additional autoantigens myosin, actin, keratin, and DNA. Five mAb were found which reacted with either PepM5 or ColiM6 protein and tropomyosin in Western blots or ELISA. Two of the tropomyosin positive mAb were also antinuclear antibodies and were inhibited with DNA. In Western blots of cardiac tropomyosins, the mAb reacted with either the 70-kDa dimer of tropomyosin, the 35-kDa monomer, or both. Some differences were observed in the reactions of the mAb with the different tropomyosins in Western blots. The heart cross-reactive epitopes shared between M proteins and tropomyosin were in most instances shared with cardiac myosin. Differences were observed among the reactions of the mAb with the different tropomyosins. This report constitutes the first evidence of serologic cross-reactivity between streptococcal M proteins and tropomyosins.
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Gunning, Peter, Geraldine O’neill, and Edna Hardeman. "Tropomyosin-Based Regulation of the Actin Cytoskeleton in Time and Space." Physiological Reviews 88, no. 1 (January 2008): 1–35. http://dx.doi.org/10.1152/physrev.00001.2007.

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Tropomyosins are rodlike coiled coil dimers that form continuous polymers along the major groove of most actin filaments. In striated muscle, tropomyosin regulates the actin-myosin interaction and, hence, contraction of muscle. Tropomyosin also contributes to most, if not all, functions of the actin cytoskeleton, and its role is essential for the viability of a wide range of organisms. The ability of tropomyosin to contribute to the many functions of the actin cytoskeleton is related to the temporal and spatial regulation of expression of tropomyosin isoforms. Qualitative and quantitative changes in tropomyosin isoform expression accompany morphogenesis in a range of cell types. The isoforms are segregated to different intracellular pools of actin filaments and confer different properties to these filaments. Mutations in tropomyosins are directly involved in cardiac and skeletal muscle diseases. Alterations in tropomyosin expression directly contribute to the growth and spread of cancer. The functional specificity of tropomyosins is related to the collaborative interactions of the isoforms with different actin binding proteins such as cofilin, gelsolin, Arp 2/3, myosin, caldesmon, and tropomodulin. It is proposed that local changes in signaling activity may be sufficient to drive the assembly of isoform-specific complexes at different intracellular sites.
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Asturias, Juan A., Nuria Gómez-Bayón, M. Carmen Arilla, Alberto Martínez, Ricardo Palacios, Fernando Sánchez-Gascón, and Jorge Martínez. "Molecular Characterization of American Cockroach Tropomyosin (Periplaneta americana Allergen 7), a Cross-Reactive Allergen." Journal of Immunology 162, no. 7 (April 1, 1999): 4342–48. http://dx.doi.org/10.4049/jimmunol.162.7.4342.

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Abstract Inhalation of allergens produced by the American cockroach (Periplaneta americana) induces IgE Ab production and the development of asthma in genetically predisposed individuals. The cloning and expression in Escherichia coli of P. americana tropomyosin allergen have been achieved. The protein shares high homology with other arthropod tropomyosins (80% identity) but less homology with vertebrate ones (50% identity). The recombinant allergen was produced in E. coli as a nonfusion protein with a yield of 9 mg/l of bacterial culture. Both natural and recombinant tropomyosins were purified by isoelectric precipitation. P. americana allergen 1 (Per a 1) and Per a 7 (tropomyosin) are to date the only cross-reacting allergens found in cockroaches. ELISA and Western blot inhibition experiments, using natural and recombinant purified tropomyosins from shrimp and cockroach, showed that tropomyosin induced cross-reactivity of IgE from patients allergic to these allergens, suggesting that this molecule could be a common allergen among invertebrates.
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Humayun-Zakaria, Nada, Roland Arnold, Anshita Goel, Douglas Ward, Stuart Savill, and Richard Bryan. "Tropomyosins: Potential Biomarkers for Urothelial Bladder Cancer." International Journal of Molecular Sciences 20, no. 5 (March 4, 2019): 1102. http://dx.doi.org/10.3390/ijms20051102.

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Despite the incidence and prevalence of urothelial bladder cancer (UBC), few advances in treatment and diagnosis have been made in recent years. In this review, we discuss potential biomarker candidates: the tropomyosin family of genes, encoded by four loci in the human genome. The expression of these genes is tissue-specific. Tropomyosins are responsible for diverse cellular roles, most notably based upon their interplay with actin to maintain cellular processes, integrity and structure. Tropomyosins exhibit a large variety of splice forms, and altered isoform expression levels have been associated with cancer, including UBC. Notably, tropomyosin isoforms are detectable in urine, offering the potential for non-invasive diagnosis and risk-stratification. This review collates the basic knowledge on tropomyosin and its isoforms, and discusses their relationships with cancer-related phenomena, most specifically in UBC.
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Shafique, Rubaba Hamid, Muhammad Inam, Muhammad Ismail, and Farhana Riaz Chaudhary. "Group 10 Allergens (Tropomyosins) from House-Dust Mites May Cause Covariation of Sensitization to Allergens from Other Invertebrates." Allergy & Rhinology 3, no. 2 (January 2012): ar.2012.3.0036. http://dx.doi.org/10.2500/ar.2012.3.0036.

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Group 10 allergens (tropomyosins) have been assumed to be a major cause of cross-reactivity between house-dust mites (HDMs) and other invertebrates. Despite all of the published data regarding the epidemiology, percent IgE binding and level of sensitization in the population, the role of tropomyosin as a cross-reactive allergen in patients with multiple allergy syndrome still remains to be elucidated. Homology between amino acid sequences reported in allergen databases of selected invertebrate tropomyosins was determined with Der f 10 as the reference allergen. The 66.9 and 54.4% identities were found with selected crustacean and insect species, respectively, whereas only 20.4% identity was seen with mollusks. A similar analysis was performed using reported B-cell IgE-binding epitopes from Met e1 (shrimp allergen) and Bla g7 (cockroach allergen) with other invertebrate tropomyosins. The percent identity in linear sequences was higher than 35% in mites, crustaceans, and cockroaches. The polar and hydrophobic regions in these groups were highly conserved. These findings suggest that tropomyosin may be a major cause of covariation of sensitization between HDMs, crustaceans, and some species of insects and mollusks.
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Goins, Lauren M., and R. Dyche Mullins. "A novel tropomyosin isoform functions at the mitotic spindle and Golgi in Drosophila." Molecular Biology of the Cell 26, no. 13 (July 2015): 2491–504. http://dx.doi.org/10.1091/mbc.e14-12-1619.

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Most eukaryotic cells express multiple isoforms of the actin-binding protein tropomyosin that help construct a variety of cytoskeletal networks. Only one nonmuscle tropomyosin (Tm1A) has previously been described in Drosophila, but developmental defects caused by insertion of P-elements near tropomyosin genes imply the existence of additional, nonmuscle isoforms. Using biochemical and molecular genetic approaches, we identified three tropomyosins expressed in Drosophila S2 cells: Tm1A, Tm1J, and Tm2A. The Tm1A isoform localizes to the cell cortex, lamellar actin networks, and the cleavage furrow of dividing cells—always together with myosin-II. Isoforms Tm1J and Tm2A colocalize around the Golgi apparatus with the formin-family protein Diaphanous, and loss of either isoform perturbs cell cycle progression. During mitosis, Tm1J localizes to the mitotic spindle, where it promotes chromosome segregation. Using chimeras, we identified the determinants of tropomyosin localization near the C-terminus. This work 1) identifies and characterizes previously unknown nonmuscle tropomyosins in Drosophila, 2) reveals a function for tropomyosin in the mitotic spindle, and 3) uncovers sequence elements that specify isoform-specific localizations and functions of tropomyosin.
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Anthony, D. T., R. J. Jacobs-Cohen, G. Marazzi, and L. L. Rubin. "A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors." Journal of Cell Biology 106, no. 5 (May 1, 1988): 1713–21. http://dx.doi.org/10.1083/jcb.106.5.1713.

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Muscle cells infected at the permissive temperature with temperature-sensitive mutants of Rous sarcoma virus and shifted to the non-permissive temperature form myotubes that are unable to cluster acetylcholine receptors (Anthony, D. T., S. M. Schuetze, and L. L. Rubin. 1984. Proc. Natl. Acad. Sci. USA. 81:2265-2269). Work described in this paper demonstrates that the virally-infected cells are missing a 37-kD peptide which reacts with an anti-tropomyosin antiserum. Using a monoclonal antibody specific for the missing peptide, we show that this tropomyosin is absent from fibroblasts and is distinct from smooth muscle tropomyosins. It is also different from the two previously identified striated muscle myofibrillar tropomyosins (alpha and beta). We suggest that, in normal muscle, this novel, non-myofibrillar, tropomyosin-like molecule is an important component of a cytoskeletal network necessary for cluster formation.
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Shanti, K. N., B. M. Martin, S. Nagpal, D. D. Metcalfe, and P. V. Rao. "Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes." Journal of Immunology 151, no. 10 (November 15, 1993): 5354–63. http://dx.doi.org/10.4049/jimmunol.151.10.5354.

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Abstract The major heat-stable shrimp allergen (designated as Sa-II), capable of provoking IgE-mediated immediate type hypersensitivity reactions after the ingestion of cooked shrimp, has been shown to be a 34-kDa heat-stable protein containing 300 amino acid residues. Here, we report that a comparison of amino acid sequences of different peptides generated by proteolysis of Sa-II revealed an 86% homology with tropomyosin from Drosophila melanogaster, suggesting that Sa-II could be the shrimp muscle protein tropomyosin. To establish that Sa-II is indeed tropomyosin, the latter was isolated from uncooked shrimp (Penaeus indicus) and its physicochemical and immunochemical properties were compared with those of Sa-II. Both tropomyosin and Sa-II had the same molecular mass and focused in the isoelectric pH range of 4.8 to 5.4. In the presence of 6 M urea, the mobility of both Sa-II and shrimp tropomyosin shifted to give an apparent molecular mass of 50 kDa, which is a characteristic property of tropomyosins. Shrimp tropomyosin bound to specific IgE antibodies in the sera of shrimp-sensitive patients as assessed by competitive ELISA inhibition and Western blot analysis. Tryptic maps of both Sa-II and tropomyosin as obtained by reverse phase HPLC were superimposable. Dot-blot and competitive ELISA inhibition using sera of shrimp-sensitive patients revealed that antigenic as well as allergenic activities were associated with two peptide fractions. These IgE-binding tryptic peptides were purified and sequenced. Mouse anti-anti-idiotypic antibodies raised against Sa-II specific human idiotypic antibodies recognized not only tropomyosin but also the two allergenic peptides, thus suggesting that these peptides represent the major IgE binding epitopes of tropomyosin. A comparison of the amino acid sequence of shrimp tropomyosin in the region of IgE binding epitopes (residues 50-66 and 153-161) with the corresponding regions of tropomyosins from different vertebrates confirmed lack of allergenic cross-reactivity between tropomyosins from phylogenetically distinct species.
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Yamashiro-Matsumura, S., and F. Matsumura. "Characterization of 83-kilodalton nonmuscle caldesmon from cultured rat cells: stimulation of actin binding of nonmuscle tropomyosin and periodic localization along microfilaments like tropomyosin." Journal of Cell Biology 106, no. 6 (June 1, 1988): 1973–83. http://dx.doi.org/10.1083/jcb.106.6.1973.

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Nonmuscle caldesmon purified from cultured rat cells shows a molecular weight of 83,000 on SDS gels, Stokes radius of 60.5 A, and sedimentation coefficient (S20,w) of 3.5 in the presence of reducing agents. These values give a native molecular weight of 87,000 and a frictional ratio of 2.04, suggesting that the molecule is a monomeric, asymmetric protein. In the absence of reducing agents, the protein is self-associated, through disulfide bonds, into oligomers with a molecular weight of 230,000 on SDS gels. These S-S oligomers appear to be responsible for the actin-bundling activity of nonmuscle caldesmon in the absence of reducing agents. Actin binding is saturated at a molar ratio of one 83-kD protein to six actins with an apparent binding constant of 5 X 10(6) M-1. Because of 83-kD nonmuscle caldesmon and tropomyosin are colocalized in stress fibers of cultured cells, we have examined effects of 83-kD protein on the actin binding of cultured cell tropomyosin. Of five isoforms of cultured rat cell tropomyosin, tropomyosin isoforms with high molecular weight values (40,000 and 36,500) show higher affinity to actin than do tropomyosin isoforms with low molecular weight values (32,400 and 32,000) (Matsumura, F., and S. Yamashiro-Matsumura. 1986. J. Biol. Chem. 260:13851-13859). At physiological concentration of KCl (100 mM), 83-kD nonmuscle caldesmon stimulates binding of low molecular weight tropomyosins to actin and increases the apparent binding constant (Ka from 4.4 X 10(5) to 1.5 X 10(6) M-1. In contrast, 83-kD protein has slight stimulation of actin binding of high molecular weight tropomyosins because high molecular weight tropomyosins bind to actin strongly in this condition. As the binding of 83-kD protein to actin is regulated by calcium/calmodulin, 83-kD protein regulates the binding of low molecular weight tropomyosins to actin in a calcium/calmodulin-dependent way. Using monoclonal antibodies to visualize nonmuscle caldesmon along microfilaments or actin filaments reconstituted with purified 83-kD protein, we demonstrate that 83-kD nonmuscle caldesmon is localized periodically along microfilaments or actin filaments with similar periodicity (36 +/- 4 nm) as tropomyosin. These results suggest that 83-kD protein plays an important role in the organization of microfilaments, as well as the control of the motility, through the regulation of the binding of tropomyosin to actin.
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Dissertations / Theses on the topic "Tropomyosins"

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Au, Wing-han. "Brain-derived neurotrophic factor (BDNF)/tropomyosin-related kinase B (TRKB) signaling in ovarian cancer." Click to view the E-thesis via HKUTO, 2007. http://sunzi.lib.hku.hk/HKUTO/record/B39557947.

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Ebrahim, Seham. "Tropomyosins, N-terminal acetylation and their impact on yeast cytoskeletal function : a characterisation of novel tropomyosins from N. crassa and the N-terminal acetyltransferase, Nat3p." Thesis, Queen Mary, University of London, 2009. http://qmro.qmul.ac.uk/xmlui/handle/123456789/531.

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While the fundamental role of tropomyosins (Tms) in the maintenance of the actin cytoskeleton in yeast is established, details of their exact regulatory functions in lower eukaryotes remains to be deciphered. Here, two novel Tms have been identified from the filamentous yeast Neurospora crassa: a 161 residue protein spanning 4 actin monomers (crTm161p), and a 123 residue protein which spans 3 actin monomers (crTm123p). The latter isoform is the shortest naturally occurring Tm known. The isoforms are produced as a result of alternative splicing from a single gene- a phenomenon that has not previously been observed in yeast Tms. Both Tms were cloned, purified and crystallised. They were also characterised biochemically and biophysically, giving some insight into their role in fungal cytoskeleton regulation. The crystals produced provide the potential for future structural studies, as a high resolution structure of a complete Tm is still not available. The N-terminal acetylation of Tms is essential for their function, and is catalysed in Saccaromyces cerevisiae by the N-terminal N-acetyltransferase (NAT) Nat3p. Nat3p was expressed and purified. Its functionality was investigated via acetyl coenzyme A binding assays. The molecular structure of Nat3p was modelled using existing data from structural homologues. The closely related N-terminal NAT, Nat5p, was also expressed, purified and its structure modelled. Nat3p was largely insoluble while Nat5p was soluble and was successfully crystallised. Structural insights from molecular modelling were able to provide some justification for these differences. Finally the in vivo effects of genetic knockouts of the TPM1 and NAT3 genes in yeast were analysed quantitatively. Complementation of the defective knockout phenotypes by over-expression of various Tm and Nat3p constructs was also investigated. Quantifying the overlapping phenotypes of the NAT3Δ and TPM1Δ mutaunts has clarified their distinct impacts upon the cytoskeleton. The ability of the crTms to rescue TPM1Δ phenotypes implies they have roles similar to those of Tpm1p.
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Vlahovich, Nicole. "The role of cytoskeletal tropomyosins in skeletal muscle and muscle disease." Thesis, View thesis, 2007. http://handle.uws.edu.au:8081/1959.7/32176.

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Cells contain an elaborate cytoskeleton which plays a major role in a variety of cellular functions including: maintenance of cell shape and dimension, providing mechanical strength, cell motility, cytokinesis during mitosis and meiosis and intracellular transport. The cell cytoskeleton is made up of three types of protein filaments: the microtubules, the intermediate filaments and the actin cytoskeleton. These components interact with each other to allow the cell to function correctly. When functioning incorrectly, disruptions to many cellular pathway have been observed with mutations in various cytoskeletal proteins causing an assortment of human disease phenotypes. Characterization of these filament systems in different cell types is essential to the understanding of basic cellular processes and disease causation. The studies in this thesis are concerned with examining specific cytoskeletal tropomyosin-defined actin filament systems in skeletal muscle. The diversity of the actin filament system relies, in part, on the family of actin binding proteins, the tropomyosins (Tms). There are in excess of forty Tm isoforms found in mammals which are derived from four genes: α, β, γ and δTm. The role of the musclespecific Tms in striated muscle is well understood, with sarcomeric Tm isoforms functioning as part of the thin filament where it regulates actin-myosin interactions and hence muscle contraction. However, relatively little known about the roles of the many cytoskeletal Tm isoforms. Cytoskeletal Tms have been shown to compartmentalise to form functionally distinct filaments in a range of cell types including neurons (Bryce et al., 2003), fibroblasts (Percival et al., 2000) and epithelial cells (Dalby-Payne et al., 2003). Recently it has been shown that cytoskeletal Tm, Tm5NM1 defines a cytoskeletal structure in skeletal muscle called the Z-line associated cytoskeleton (Z-LAC) (Kee et al., 2004).The disruption of this structure by over-expression of an exogenous Tm in transgenic mice results in a muscular dystrophy phenotype, indicating that the Z-LAC plays an important role in maintenance of muscle structure (Kee et al., 2004). In this study, specific cytoskeletal Tms are further investigated in the context of skeletal muscle. Here, we examine the expression, localisation and potential function of cytoskeletal Tm isoforms, focussing on Tm4 (derived from the δ- gene) and Tm5NM1 (derived from the γ-gene). By western blotting and immuno-staining mouse skeletal muscle, we show that cytoskeletal Tms are expressed in a range of muscles and define separate populations of filaments. These filaments are found in association with a number of muscle structures including the myotendinous junction, neuromuscular junction, the sarcolemma, the t-tubules and the sarcoplasmic reticulum. Of particular interest, Tm4 and Tm5NM1 define cytoskeletal elements in association with the saroplasmic reticulum and T-tubules, respectively, with a separation of less than 90 nm between distinct filamentous populations. The segregation of Tm isoforms indicates a role for Tms in the specification of actin filament function at these cellular regions. Examination of muscle during development, regeneration and disease revealed that Tm4 defines a novel cytoskeletal filament system that is orientated perpendicular to the sarcomeric apparatus. Tm4 is up-regulated in both muscular dystrophy and nemaline myopathy and also during induced regeneration and focal repair in mouse muscle. Transition of the Tm4-defined filaments from a predominsnatly longitudinal to a predominantly Z-LAC orientation is observed during the course of muscle regeneration. This study shows that Tm4 is a marker of regeneration and repair, in response to disease, injury and stress in skeletal muscle. Analysis of Tm5NM1 over-expressing (Tm5/52) and null (9d89) mice revealed that compensation between Tm genes does not occur in skeletal muscle. We found that the levels of cytoskeletal Tms derived from the δ-gene are not altered to compensate for the loss or gain of Tm5NM1 and that the localisation of Tm4 is unchanged in skeletal muscle of these mice. Also, excess Tm5NM1 is sorted correctly, localising to the ZLAC. This data correlates with evidence from previous investigations which indicates that Tm isoforms are not redundant and are functionally distinct (Gunning et al., 2005). Transgenic and null mice have also allowed the further elucidation of cytoskeletal Tm function in skeletal muscle. Analyses of these mice suggest a role for Tm5NM1 in glucose regulation in both skeletal muscle and adipose tissue. Tm5NM1 is found to colocalise with members of the glucose transport p fibres and analysis of both transgenic and null mice has shown an alteration to glucose uptake in adipose tissue. Taken together these data indicate that Tm5NM1 may play a role in the translocation of the glucose transport molecule GLUT4. In addition to this Tm5NM1 may play a role in adipose tissue regulation, since over-expressing mice found to have increased white adipose tissue and an up-regulation of a transcriptional regulator of fat-cell formation, PPAR-γ.
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Vlahovich, Nicole. "The role of cytoskeletal tropomyosins in skeletal muscle and muscle disease." View thesis, 2007. http://handle.uws.edu.au:8081/1959.7/32176.

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Thesis (Ph.D.)--University of Western Sydney, 2007.
A thesis presented to the University of Western Sydney, College of Health and Science, School of Natural Sciences, in fulfilment of the requirements for the degree of Doctor of Philosophy. Includes bibliographies.
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歐穎嫻 and Wing-han Au. "Brain-derived neurotrophic factor (BDNF)/tropomyosin-related kinaseB (TRKB) signaling in ovarian cancer." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2007. http://hub.hku.hk/bib/B39557947.

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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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Patel, Dipesh A. Root Douglas. "Luminescence resonance energy transfer-based modeling of troponin in the presence of myosin and troponin/tropomyosin defining myosin binding target zones in the reconstituted thin filament." [Denton, Tex.] : University of North Texas, 2009. http://digital.library.unt.edu/permalink/meta-dc-9834.

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Kotadiya, Preeyal. "Regulation Of Osteoclast Function By Alpha Gene Tropomyosins, TM-2/3 And TM-5a/5b." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1250612152.

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McMichael, Brooke Kristin Trinrud. "Tropomyosin 4, myosin IIA, and myosin X enhance osteoclast function through regulation of cellular attachment structures." Columbus, Ohio : Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view.cgi?acc%5Fnum=osu1206052974.

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McKay, Janet A. "A feasibility and exploratory study of cardiac rehabilitation in acute coronary syndrome." Thesis, University of Stirling, 2013. http://hdl.handle.net/1893/20346.

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Background: Cardiac Rehabilitation (CR) has been shown to be effective in reducing mortality and morbidity in Coronary Heart Disease (CHD). There is a limited amount of research that evaluates the impact of menu-based CR, in patients with Acute Coronary Syndrome with Low Troponin levels (ACSLT). Aim: This thesis contains a feasibility study and an exploratory study. The feasibility study aimed to examine the feasibility of a Randomised Controlled Trial (RCT) which would test the impact of a menu-based CR programme, on individuals diagnosed with ACSLT, against standard care. This feasibility study included staff views. The exploratory study aimed to explore the impact that ACSLT and CR can have on this client group. Method: The feasibility study was a repeated measures case-control trial of menu-based CR based on the theoretical framework of the Common Sense Model of Self-Regulation (CSM), using a range of health assessments. The areas assessed included misconceptions, symptoms, anxiety, depression and Health Related Quality of Life (HRQoL). In addition, focus groups were held with both ward and specialist CR staff to seek their views on the feasibility of a RCT of menu-based CR for ACSLT. The exploratory study consisted of description and analysis of the data that had been collected from the participants over the two year period as above. In addition it included qualitative data that had been collected during interviews with the participants. Findings: Participants (n=33) were recruited from cardiology wards following an admission with ACSLT. They were assessed at baseline (T1), nine months (T3) and 24 months (T4). Twenty-five participants completed the studies. The feasibility study was successful in its aim of testing the CR intervention and protocols for a further RCT. The intervention was acceptable to the participants and to the specialist staff, although the ward staff did not see the need for a RCT. The measures used, with the exception of the self-reporting measures, were suitable and provided a wide range of data that could be utilised in a RCT. However the changes to diagnostic categories meant that a RCT would no longer be feasible. The exploratory study found that both groups were similar on a range of baseline demographic and clinical factors. There was a tendency to benefit within the exploratory study which favoured the intervention. An additional finding from the exploratory study was the degree of uncertainty experienced by the participants, within the context of a changing political and clinical landscape. Discussion and conclusions: The studies presented in this thesis add to our knowledge by highlighting some of the difficulties in designing a RCT of menu-based CR in a specific subgroup of CHD and by presenting outcome data for a small group of participants that have not previously been studied within the literature. This data suggests that there was a tendency to benefit for the intervention that requires further study. Implications for practice: Patients with ACSLT are now being included in CR programmes due to the changes within the diagnostic criteria. Clinicians have little understanding of the impact of CR on this group of patients, or what type of interventions would work best. Large RCT’s will however be problematic and this thesis has highlighted that further work is required to explore how CR can best improve the well-being of individuals with ACSLT.
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Books on the topic "Tropomyosins"

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Gunning, Peter, ed. Tropomyosin. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-85766-4.

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Gaze, David Christopher. Getting to the heart of the matter: Cardiac troponin as a cardiovascular biomarker. Hauppauge, N.Y: Nova Science, 2011.

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Swanwick, Richard Stephen. Mapping the interactions of the C-terminus of rabbit skeletal troponin T with troponin C and tropomyosin. Birmingham: University of Birmingham, 2003.

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Gunning, Peter. Tropomyosin. Springer, 2010.

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Gunning, Peter. Tropomyosin. Springer London, Limited, 2009.

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Gunning, Peter. Tropomyosin. Springer New York, 2010.

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1950-, Gunning Peter, ed. Tropomyosin. New York, N.Y: Springer Science+Business Media, 2008.

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1922-, Ebashi Setsurō, and Ohtsuki Iwao, eds. Regulatory mechanisms of striated muscle contraction. Tokyo: Springer, 2007.

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Ebashi, Setsuro, and Iwao Ohtsuki. Regulatory Mechanisms of Striated Muscle Contraction. Springer, 2008.

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Ebashi, Setsuro, and Iwao Ohtsuki. Regulatory Mechanisms of Striated Muscle Contraction. Springer London, Limited, 2007.

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Book chapters on the topic "Tropomyosins"

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Gimona, Mario. "Dimerization of Tropomyosins." In Advances in Experimental Medicine and Biology, 73–84. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-85766-4_6.

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Martin, Claire, and Peter Gunning. "Isoform Sorting of Tropomyosins." In Advances in Experimental Medicine and Biology, 187–200. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-85766-4_15.

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Kee, Anthony J., and Edna C. Hardeman. "Tropomyosins in Skeletal Muscle Diseases." In Advances in Experimental Medicine and Biology, 143–57. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-85766-4_12.

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Das, Kiron M., and Manisha Bajpai. "Tropomyosins in Human Diseases: Ulcerative Colitis." In Advances in Experimental Medicine and Biology, 158–67. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-85766-4_13.

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Ostap, E. Michael. "Tropomyosins as Discriminators of Myosin Function." In Advances in Experimental Medicine and Biology, 273–82. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-85766-4_20.

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Curthoys, Nikki Margarita, Peter William Gunning, and Thomas Fath. "Tropomyosins in Neuronal Morphogenesis and Development." In Advances in Neurobiology, 411–45. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6787-9_18.

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Reese, Gerald, Deborah Tracey, Carolyn B. Daul, and Samuel B. Lehrer. "IGE and Monoclonal Antibody Reactivities to the Major Shrimp Allergen Pen a 1 (Tropomyosin) and Vertebrate Tropomyosins." In Advances in Experimental Medicine and Biology, 225–30. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5855-2_31.

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Lindberg, Uno, Clarence E. Schutt, Robert D. Goldman, Maria Nyåkern-Meazza, Louise Hillberg, Li-Sophie Zhao Rathje, and Staffan Grenklo. "Tropomyosins Regulate the Impact of Actin Binding Proteins on Actin Filaments." In Advances in Experimental Medicine and Biology, 223–31. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-85766-4_17.

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Mäkelä, P. Helena, Pertti Koski, Petri Riikonen, Suvi Taira, Harry Holthöfer, and Mikael Rhen. "The Virulence Plasmid of Salmonella Encodes a Protein Resembling Eukaryotic Tropomyosins." In Biology of Salmonella, 115–20. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2854-8_14.

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Ferraz, C., J. P. Liautard, J. Sri Widada, G. Travé, and F. Heitz. "Conformational stabilities of various human ß-tropomyosins obtained by site-directed mutagenesis." In Peptides 1990, 587–88. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_245.

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Conference papers on the topic "Tropomyosins"

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Turło, Marta, and Piotr Minkiewicz. "Peptide markers of seafood tropomyosins, stable during food processingompounds." In 1st International PhD Student’s Conference at the University of Life Sciences in Lublin, Poland: ENVIRONMENT – PLANT – ANIMAL – PRODUCT. Publishing House of The University of Life Sciences in Lublin, 2022. http://dx.doi.org/10.24326/icdsupl1.t038.

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Lo, Jun-chih, and Richard D. Ludescher. "Tropomyosin rotational dynamics in thin filaments." In OE/LASE '94, edited by Joseph R. Lakowicz. SPIE, 1994. http://dx.doi.org/10.1117/12.182760.

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Torre, Ricarda, Maria Freitas, Estefanía Costa-Rama, Henri P. A. Nouws, and Cristina Delerue-Matos. "Tropomyosin Analysis in Foods Using an Electrochemical Immunosensing Approach." In CSAC2021. Basel Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/csac2021-10471.

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Ferraz, C., G. Travé, J. Sri Widada, F. Heitz, and J. P. Liautard. "Dynamics of tropomyosin studied by denaturation of site-directed mutants." In The living cell in four dimensions. AIP, 1991. http://dx.doi.org/10.1063/1.40600.

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Gunning, Peter, Yao Wang, Jeff H. Stear, Ashleigh Swain, Xing Xu, Nicole Bryce, Irina B. Alieva, et al. "Abstract 5817: Anti-tropomyosin drugs prevent the rescue of vincristine-induced mitotic spindle defects." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-5817.

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Faulkner, S., S. Roselli, C. Oldmeadow, J. Attia, JF Forbes, MM Walker, and H. Hondermarck. "Abstract P6-03-03: Tropomyosin-related kinase A is overexpressed in HER2-positive breast cancers." In Abstracts: 2016 San Antonio Breast Cancer Symposium; December 6-10, 2016; San Antonio, Texas. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.sabcs16-p6-03-03.

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Nagel, Jacquelyn K. S. "Design of a Biologically-Inspired Chemical Sensor." In ASME 2013 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/detc2013-12378.

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Abstract:
Sensors are an integral part of many engineered products and systems. Biological inspiration has the potential to improve current sensor designs as well as inspire innovative ones. Mimicking nature offers more than just the observable aspects that conjure up engineering solutions performing similar functions, but also less obvious strategic and sustainable aspects. This paper presents the design of an innovative, biologically-inspired chemical sensor that performs “up-front” processing through mechanical filtering. Functional representation and abstraction were used to place the biological system information in an engineering context, and facilitate the bioinspired design process. Inspiration from the physiology (function) of the guard cell coupled with the morphology (form) and physiology of tropomyosin resulted in multiple concept variants for the chemical sensor. The chemical sensor conceptual designs are provided along with detailed descriptions. Applications of the sensor design include environmental monitoring of harmful gases, and a non-invasive approach to detect illnesses including diabetes, liver disease, and cancer on the breath.
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Klink, Andrew, Abhishek Kavati, Ruth Antoine, Awa Gassama, Tom Kozlek, and Ajeet Gajra. "Abstract P022: Clinical and genomic characteristics of tropomyosin receptor kinase (TRK) fusion cancer in community oncology practice." In Abstracts: AACR-NCI-EORTC Virtual International Conference on Molecular Targets and Cancer Therapeutics; October 7-10, 2021. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1535-7163.targ-21-p022.

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Mok, Stephen, Colm Duffy, Reginald Du, and James P. Allison. "Abstract A146: Increase antitumor activity of immunotherapy by blocking colony stimulating factor 1 receptor and tropomyosin receptor kinase." In Abstracts: Second CRI-CIMT-EATI-AACR International Cancer Immunotherapy Conference: Translating Science into Survival; September 25-28, 2016; New York, NY. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/2326-6066.imm2016-a146.

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"Identification of Squamous Cell Carcinoma Associated Proteins by Proteomics and Loss of Beta Tropomyosin Expression in Esophageal Cancer." In 2016 International Conference on Biological and Environmental Science. Universal Researchers, 2016. http://dx.doi.org/10.17758/ur.u0616224.

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Reports on the topic "Tropomyosins"

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Mielnicki, Lawrence M. Deregulation of Tropomyosin Expression in Human Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 1998. http://dx.doi.org/10.21236/ada353884.

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Prasad, Gaddamanugu L. Tropomyosin-1, A Putative Tumor-Suppressor and a Biomarker of Human Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2004. http://dx.doi.org/10.21236/ada437915.

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Prasad, Gaddamanugu L. Tropomyosin-1, A Putative Tumor-Suppressor and a Biomarker of Human Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2003. http://dx.doi.org/10.21236/ada421752.

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Prasad, Gaddamanugu. Tropomyosin-1: A Putative Tumor Suppressor and a Biomarker of Human Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada393259.

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Prasad, Gaddamanugau L. Tropomyosin-1, A Novel Class II Tumor Suppressor and a Biomarker of Human Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2001. http://dx.doi.org/10.21236/ada405435.

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Prasad, Gaddamanugu L. Tropomyosin-1, a Novel Class II Tumor-Suppressor and a Biomarker of Human Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2002. http://dx.doi.org/10.21236/ada410784.

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Prasad, Gaddamanugu L. Tropomyosin-1 A Novel Class II Tumor-Suppressor and a Biomarker of Human Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2003. http://dx.doi.org/10.21236/ada421793.

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