Relevant bibliographies by topics / Muscles Tropomyosins

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

Academic literature on the topic 'Muscles Tropomyosins'

Author: Grafiati
Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "Muscles Tropomyosins"

1

Heeley, D. H., G. K. Dhoot, and S. V. Perry. "Factors determining the subunit composition of tropomyosin in mammalian skeletal muscle." Biochemical Journal 226, no. 2 (1985): 461–68. http://dx.doi.org/10.1042/bj2260461.

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Adult rat fast-twitch skeletal muscle such as extensor digitorum longus contains alpha- and beta-tropomyosin subunits, as is the case in the corresponding muscles of rabbit. Adult rat soleus muscle contains beta-, gamma- and delta-tropomyosins, but no significant amounts of alpha-tropomyosin. Evidence for the presence of phosphorylated forms of at least three of the four tropomyosin subunit isoforms was obtained, particularly in developing muscle. Immediately after birth alpha- and beta-tropomyosins were the major components of skeletal muscle, in both fast-twitch and slow-twitch muscles. Differentiation into slow-twitch skeletal muscles was accompanied by a fall in the amount of alpha-tropomyosin subunit and its replacement with gamma- and delta-subunits. After denervation and during regeneration after injury, the tropomyosin composition of slow-twitch skeletal muscle changed to that associated with fast-twitch muscle. Thyroidectomy slowed down the changes in tropomyosin composition resulting from the denervation of soleus muscle. The results suggest that the ‘ground state’ of tropomyosin-gene expression in the skeletal muscle gives rise to alpha- and beta-tropomyosin subunits. Innervation by a ‘slow-twitch’ nerve is essential for the expression of the genes controlling gamma- and delta-subunits. There appears to be reciprocal relationship between expression of the gene controlling the synthesis of alpha-tropomyosin and those controlling the synthesis of gamma- and delta-tropomyosin subunits.
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Dowling, Paul, Stephen Gargan, Dieter Swandulla, and Kay Ohlendieck. "Fiber-Type Shifting in Sarcopenia of Old Age: Proteomic Profiling of the Contractile Apparatus of Skeletal Muscles." International Journal of Molecular Sciences 24, no. 3 (2023): 2415. http://dx.doi.org/10.3390/ijms24032415.

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The progressive loss of skeletal muscle mass and concomitant reduction in contractile strength plays a central role in frailty syndrome. Age-related neuronal impairments are closely associated with sarcopenia in the elderly, which is characterized by severe muscular atrophy that can considerably lessen the overall quality of life at old age. Mass-spectrometry-based proteomic surveys of senescent human skeletal muscles, as well as animal models of sarcopenia, have decisively improved our understanding of the molecular and cellular consequences of muscular atrophy and associated fiber-type shifting during aging. This review outlines the mass spectrometric identification of proteome-wide changes in atrophying skeletal muscles, with a focus on contractile proteins as potential markers of changes in fiber-type distribution patterns. The observed trend of fast-to-slow transitions in individual human skeletal muscles during the aging process is most likely linked to a preferential susceptibility of fast-twitching muscle fibers to muscular atrophy. Studies with senescent animal models, including mostly aged rodent skeletal muscles, have confirmed fiber-type shifting. The proteomic analysis of fast versus slow isoforms of key contractile proteins, such as myosin heavy chains, myosin light chains, actins, troponins and tropomyosins, suggests them as suitable bioanalytical tools of fiber-type transitions during aging.
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Huang, Ming-Chih, Cheng-Linn Lee, Yoshihiro Ochiai, and Shugo Watabe. "Thermostability of tropomyosins from the fast skeletal muscles of tropical fish species." Fish Physiology and Biochemistry 45, no. 3 (2019): 1189–202. http://dx.doi.org/10.1007/s10695-019-00632-7.

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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 (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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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 (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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MacLeod, A. R., and C. Gooding. "Human hTM alpha gene: expression in muscle and nonmuscle tissue." Molecular and Cellular Biology 8, no. 1 (1988): 433–40. http://dx.doi.org/10.1128/mcb.8.1.433-440.1988.

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We have isolated a cDNA clone from a human skeletal muscle library which contains the complete protein-coding sequence of a skeletal muscle alpha-tropomyosin. This cDNA sequence defines a fourth human tropomyosin gene, the hTM alpha gene, which is distinct from the hTMnm gene encoding a closely related isoform of skeletal muscle alpha-tropomyosin. In cultured human fibroblasts, the hTM alpha gene encodes both skeletal-muscle- and smooth-muscle-type alpha-tropomyosins by using an alternative mRNA-splicing mechanism.
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MacLeod, A. R., and C. Gooding. "Human hTM alpha gene: expression in muscle and nonmuscle tissue." Molecular and Cellular Biology 8, no. 1 (1988): 433–40. http://dx.doi.org/10.1128/mcb.8.1.433.

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We have isolated a cDNA clone from a human skeletal muscle library which contains the complete protein-coding sequence of a skeletal muscle alpha-tropomyosin. This cDNA sequence defines a fourth human tropomyosin gene, the hTM alpha gene, which is distinct from the hTMnm gene encoding a closely related isoform of skeletal muscle alpha-tropomyosin. In cultured human fibroblasts, the hTM alpha gene encodes both skeletal-muscle- and smooth-muscle-type alpha-tropomyosins by using an alternative mRNA-splicing mechanism.
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Perz-Edwards, Robert J., Thomas C. Irving, Bruce A. J. Baumann, et al. "X-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle." Proceedings of the National Academy of Sciences 108, no. 1 (2010): 120–25. http://dx.doi.org/10.1073/pnas.1014599107.

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Stretch activation is important in the mechanical properties of vertebrate cardiac muscle and essential to the flight muscles of most insects. Despite decades of investigation, the underlying molecular mechanism of stretch activation is unknown. We investigated the role of recently observed connections between myosin and troponin, called “troponin bridges,” by analyzing real-time X-ray diffraction “movies” from sinusoidally stretch-activated Lethocerus muscles. Observed changes in X-ray reflections arising from myosin heads, actin filaments, troponin, and tropomyosin were consistent with the hypothesis that troponin bridges are the key agent of mechanical signal transduction. The time-resolved sequence of molecular changes suggests a mechanism for stretch activation, in which troponin bridges mechanically tug tropomyosin aside to relieve tropomyosin’s steric blocking of myosin–actin binding. This enables subsequent force production, with cross-bridge targeting further enhanced by stretch-induced lattice compression and thick-filament twisting. Similar linkages may operate in other muscle systems, such as mammalian cardiac muscle, where stretch activation is thought to aid in cardiac ejection.
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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 (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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Madan, Aditi, Meera C. Viswanathan, Kathleen C. Woulfe, et al. "TNNT2mutations in the tropomyosin binding region of TNT1 disrupt its role in contractile inhibition and stimulate cardiac dysfunction." Proceedings of the National Academy of Sciences 117, no. 31 (2020): 18822–31. http://dx.doi.org/10.1073/pnas.2001692117.

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Muscle contraction is regulated by the movement of end-to-end-linked troponin−tropomyosin complexes over the thin filament surface, which uncovers or blocks myosin binding sites along F-actin. The N-terminal half of troponin T (TnT), TNT1, independently promotes tropomyosin-based, steric inhibition of acto-myosin associations, in vitro. Recent structural models additionally suggest TNT1 may restrain the uniform, regulatory translocation of tropomyosin. Therefore, TnT potentially contributes to striated muscle relaxation; however, the in vivo functional relevance and molecular basis of this noncanonical role remain unclear. Impaired relaxation is a hallmark of hypertrophic and restrictive cardiomyopathies (HCM and RCM). Investigating the effects of cardiomyopathy-causing mutations could help clarify TNT1’s enigmatic inhibitory property. We tested the hypothesis that coupling of TNT1 with tropomyosin’s end-to-end overlap region helps anchor tropomyosin to an inhibitory position on F-actin, where it deters myosin binding at rest, and that, correspondingly, cross-bridge cycling is defectively suppressed under diastolic/low Ca2+conditions in the presence of HCM/RCM lesions. The impact of TNT1 mutations onDrosophilacardiac performance, rat myofibrillar and cardiomyocyte properties, and human TNT1’s propensity to inhibit myosin-driven, F-actin−tropomyosin motility were evaluated. Our data collectively demonstrate that removing conserved, charged residues in TNT1’s tropomyosin-binding domain impairs TnT’s contribution to inhibitory tropomyosin positioning and relaxation. Thus, TNT1 may modulate acto-myosin activity by optimizing F-actin−tropomyosin interfacial contacts and by binding to actin, which restrict tropomyosin’s movement to activating configurations. HCM/RCM mutations, therefore, highlight TNT1’s essential role in contractile regulation by diminishing its tropomyosin-anchoring effects, potentially serving as the initial trigger of pathology in our animal models and humans.
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Dissertations / Theses on the topic "Muscles Tropomyosins"

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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.<br>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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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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Kalyva, Athanasia. "Tropomyosin heterodimers in cardiac muscle regulation." Thesis, University of Kent, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.508567.

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Boussouf, Sabrina Eida. "Regulation of cardiac muscle contraction : effect of tropomyosin isoform expression and cardiomyopathy mutations in tropomyosin and troponin." Thesis, University of Kent, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.408903.

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Mackenzie, Cassidy. "The properties and function of tropomyosin dimers in muscle regulation." Thesis, University of Kent, 2017. https://kar.kent.ac.uk/69463/.

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Myosin binding to actin, and thus muscle contraction, is regulated by Tropomyosin (Tpm), Troponin (Tn) and calcium (Ca2+). Tpm, is an α-helical coiled-coil dimer, which exists as a homo- or heterodimer. Two major isoforms of Tpm are found in striated muscle, α and β. Though it is known that different dimers exist, the mechanism by which they form and exchange is not fully understood. The thermal stability and exchange between dimers was explored with the use of circular dichroism and SDS PAGE densitometry analysis. Homodimers showed little exchange to form heterodimers at temperatures up to 20 °C . Dimer stability at these temperatures reduces the need for chemical cross-linking samples. While extensive exchange was seen at 37 °C . Reverse exchange of WT and mutant (E54K - dilated cardiomyopathy mutant) containing heterodimers to form homodimers did not show the same extent of exchange, suggesting a dimer preference. Results showed the ability to determine dimer content of a solution with the use of polyacrylamide gels and chemical cross-linking. The thermal melting curves of Tpm highlighted a significant destabilisation of β Tpm against the α isoform. Tpm heterodimer containing E54K mutant showed a decreased thermal stability. Notable differences were seen not only for isoforms and homo- and heterodimers, but also for buffer conditions and protein tags. Increased salt concentrations led to an increase in thermal stability. Crosslinking dimers increased thermal stability, whereas addition of His-tags led to a decrease in thermal stability. Changes in thermal stability highlighted the need for caution when tagging or cross-linking the protein. Dimer exchange on actin provided conflicting results between SDS PAGE cosedimentation assays and pyrene fluorescence cosedimendation assays, which highlighted limitations of cross-linking Tpm and using fluorescent labels. The stiffness of Tpm dimers was explored using atomic force microscopy (AFM) to image Tpm particles. Significant differences were seen between the relatively stiff α Tpm and less stiff β isoform. Changes in stiffness of Tpm affect its ability to cooperatively activate the thin filament, and provides insight into the assembly of dimers in vivo.
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Pieples, Kathy. "THE FUNCTIONAL SIGNIFICANCE OF THE STRIATED ISOFORM OF TROPOMYOSIN 3 IN NORMAL AND PATHOLOGICAL STATES." University of Cincinnati / OhioLINK, 2001. http://rave.ohiolink.edu/etdc/view?acc_num=ucin997992638.

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Graham, Ian R. "Alternative splicing of tropomyosin pre-mRNA : control in non-muscle cells." Thesis, University of Leicester, 1992. http://hdl.handle.net/2381/35232.

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Alternative splicing of tropomyosin pre-mRNA: control in non-muscle cells. Ian R. Graham The human tropomyosin gene hTMnm contains a pair of mutually exclusive exons, NM and SK, which are used in non-muscle and skeletal muscle cells, respectively. I have undertaken an analysis of the factors affecting the splicing of these exons in the non-muscle cell line COS-1. I used a strategy involving mutation of the gene, followed by recloning of the appropriate region into a mammalian expression vector containing a tropomyosin cDNA clone. The wild-type and mutant mini-genes were transfected into the cell line, and the RNA produced after 48 hours' expression was isolated, then analysed by S1 nuclease protection mapping, and by a reverse transcriptase-polymerase chain reaction (RT-PCR) process. The results showed that exons NM and SK are not in competition in this non-muscle cell line; rather, I have shown that exon SK is not recognised as a splicing substrate when any other exons are present that can be used instead. Improvement, by mutation, of the branchpoint associated with exon SK restored use of that exon, as did replacement of the extreme 5' and 3' ends of the exon with the corresponding sequences from exon NM. The observation that exon SK is still overlooked by the cell's splicing apparatus, when it is placed in the exact context normally occupied by exon NM, strongly suggests that the exon itself is contributing to its deficiency. I have proposed a model in which the poor branchpoint sequence and elements within exon SK are responsible for preventing its recognition in the non-muscle cell, which is overcome, in skeletal muscle, by stimulation of the exon 4 to exon SK splice. Additionally, by studying the alternative splicing of the chick a-actinin gene, I have attempted to compare the regulation of splicing in smooth and skeletal muscle.
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Halsall, D. J. "The effects of troponin and tropomyosin on rabbit skeletal actomyosin subfragment 1 interactions." Thesis, University of Bristol, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.378788.

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Hamshere, Marion. "Alternative pre-messenger RNA splicing of murine N-CAM and human tropomyosin in non-muscle and muscle cells." Thesis, University of Leicester, 1993. http://hdl.handle.net/2381/35245.

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A quantitative RT-PCR method for analysis of alternative isoforms of RNA, and a method for the transient expression of mini-genes in differentiated muscle cells have been developed. This has enabled the analysis of endogenous RNA transcribed from rodent N-CAM and from human tropomyosin mini-genes which were expressed in COS cells and mouse C-2 myoblasts and myotubes. The sequences of the previously unreported mouse homologues of human exons MSD1b and MSD1c of N-CAM have been determined, and deposited in the EMBL data base. The tissue- and stage-specific alternative splicing patterns of exons within the muscle-specific domain (MSD) of N-CAM have also been established; the exons were normally incorporated as a unit in muscle cells, but were not included in transcripts derived from non-muscle myoblasts and neural cells. The triplet AAG exon was also included in a stage- and tissue-specific manner, but independently of inclusion of other exons of the MSD. Transfection of C-2 myoblasts with mutant mini-gene constructs of human tropomyosin determined the cis-acting elements which regulate the mutually exclusive alternative splicing of the central exons (NM and SK) in both non-muscle and muscle cells. In non-muscle, these were found to be due either to cis-acting repressor sequences within the SK exon or cis-acting activator sequences within the NM exon. In differentiated cells, exclusion of the NM exon is not via cis-acting repressor sequences within the NM exon, but because the upstream (NM) exon site is dormant and is therefore skipped by the splicing machinery. The evolution of alternative pre-mRNA splicing has also been discussed, and on this basis and from analysis of the data presented here, I conclude that regulation of alternative pre-mRNA splicing of transcripts from different genes may be founded upon a common mechanism which is largely dependent upon the presence of sub- optimal splice-signals and the potential for variation in the relative concentrations of certain splicing factors.
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Books on the topic "Muscles Tropomyosins"

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1922-, Ebashi Setsurō, and Ohtsuki Iwao, eds. Regulatory mechanisms of striated muscle contraction. 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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Ebashi, Setsuro, and Iwao Ohtsuki. Regulatory Mechanisms of Striated Muscle Contraction. Springer Japan, 2016.

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Regulatory mechanisms of striated muscle contraction. Springer, 2007.

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(Editor), Setsuro Ebashi, and Iwao Ohtsuki (Editor), eds. Regulatory Mechanisms of Striated Muscle Contraction (Advances in Experimental Medicine and Biology). Springer, 2007.

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Book chapters on the topic "Muscles Tropomyosins"

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Payne, Michael R., and Suzanne E. Rudnick. "Tropomyosin." In Cell and Muscle Motility. Springer US, 1985. http://dx.doi.org/10.1007/978-1-4757-4723-2_6.

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

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Miegel, Andrea, Lan Lee, Zbigniew Dauter, and Yuichiro Maéda. "A New Crystal Form of Tropomyosin." In Mechanism of Myofilament Sliding in Muscle Contraction. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2872-2_3.

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Wieczorek, D. F., P. Howies, and T. Doetschman. "Regulation of a-Tropomyosin Expression in Embryonic Stem Cells." In The Dynamic State of Muscle Fibers, edited by Dirk Pette. De Gruyter, 1990. http://dx.doi.org/10.1515/9783110884784-010.

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Lehman, William, and Roger Craig. "Tropomyosin and the Steric Mechanism of Muscle Regulation." In Advances in Experimental Medicine and Biology. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-85766-4_8.

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Molloy, Justin, Andrew Kreuz, Rehae Miller, Terese Tansey, and David Maughan. "Effects of Tropomyosin Deficiency in Flight Muscle of Drosophila Melanogaster." In Mechanism of Myofilament Sliding in Muscle Contraction. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2872-2_15.

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Clarke, Nigel F. "Skeletal Muscle Disease Due to Mutations in Tropomyosin, Troponin and Cofilin." In Advances in Experimental Medicine and Biology. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-84847-1_4.

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Marston, Steve, and M. El-Mezgueldi. "Role of Tropomyosin in the Regulation of Contraction in Smooth Muscle." In Advances in Experimental Medicine and Biology. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-85766-4_9.

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Murakami, Kenji, Fumiaki Yumoto, Shin-ya Ohki, Takuo Yasunaga, Masaru Tanokura, and Takeyuki Wakabayashi. "Structural Basis for Calcium-Regulated Relaxation of Striated Muscles at Interaction Sites of Troponin with Actin and Tropomyosin." In Regulatory Mechanisms of Striated Muscle Contraction. Springer Japan, 2007. http://dx.doi.org/10.1007/978-4-431-38453-3_8.

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Smillie, Lawrence B. "Tropomyosin." In Biochemistry of Smooth Muscle Contraction. Elsevier, 1996. http://dx.doi.org/10.1016/b978-012078160-7/50008-1.

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Conference papers on the topic "Muscles Tropomyosins"

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Lakkaraju, Sirish Kaushik, and Wonmuk Hwang. "Length and Sequence Dependence of the Elasticity of Alpha Helices and Coiled-Coils." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206252.

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Abstract:
Fibrous proteins made by α-helices, one of the most elementary protein secondary structures, have various mechanical roles in a sub cellular environment. An α-helix is wound in a right-handed fashion due to hydrogen bonding between the C=O and the N-H atoms across every i and i+4th residues in the polypeptide chain. Previous approaches characterizing mechanical properties of α-helices treated them as homogenous and linear elastic rods. Stiffness is typically expressed in terms of persistence length lp (∼100nm from Kb∼3×10−28 Nm2, lp = Kb/kT: Kb, the bending stiffness, k the Boltzmann constant and T = 300 K, the temperature) [1–3]. In this study, we show that bending stiffness depends on the length of the filament, due to inherent non-bonded attractions. In particular, non-bonded attraction introduces a new length scale, critical buckling length, beyond which the filament can no longer remain linearly elastic. These results suggest that non-bonded attractions can significantly affect elastic properties of biofilament systems such as the cytoskeleton. Furthermore, we find that while elasticity of a single α-helix is largely independent of its amino acid sequence, α-helical coiled-coils have stronger sequence dependence, and in the case of tropomyosin molecule, we find regional variations in the flexibility which may have functional implications in its actin binding properties and muscle contraction.
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Wilkinson, J. M., N. Hack, L. I. Thorsen, and J. A. Thomas. "MONOCLONAL ANTIBODIES RECOGNISING PROTEINS OF THE OUTER AND INNER SURFACE OF THE PLATELET PLASMA MEMBRANE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644493.

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Platelet membrane preparations can be fractionated into two major subpopulations by free flow electrophoresis and these have been shown to correspond to the plasma membrane and the endoplasmic reticulum of the platelet. The plasma membrane fraction can be shown, by two-dimensional electrophoresis, to contain the major surface glycoproteins together with considerable amounts of actin and actin-associated proteins such as the 250 kDa actin-binding protein (filamin), P235 (talin), myosin, α-actinin and tropomyosin (Hack, N. … Crawford, N., Biochem. J. 222, 235 (1984). These cytoskeletal proteins are associated with the cytoplasmic face of the plasma membrane and probably interact with transmembrane glycoproteins. We have raised monoclonal antibodies to the purified plasma membrane preparation in order to investigate the nature of these glycoprotein-cytoskeletal interactions. In two fusion experiments, out of 804 tested, 104 hybrids secreted antibody to the membrane preparation and of these 24 were selected for further study. Initial assays were by ELISA using either the membrane preparation or whole fixed platelets as the target antigen. The specificity of the antibodies was investigated further by immunoblotting of SDS gels of total platelet proteins prepared under reducing and nonreducing conditions, by immunofluorescence, by immunohisto-chemistry and by crossed immunoelectrophoresis. The majority of the antibodies recognise major surface glycoproteins; of these, four bind to glycoprotein Ib under all conditions examined while another seven recognise the glycoprotein IIb/IIIa complex as detected by crossed immunoelectrophoresis. Three antibodies recognise the actin binding protein and these cross-react with the smooth muscle protein filamin in a number of different species. Further characterisation of these antibodies in both structural and functional terms will be presented.We are grateful to the Smith and Nephew Foundation for financial support for these studies
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