Gotowe bibliografie tematyczne / Tropomyosins

Spis treści

  1. Artykuły w czasopismach
  2. Rozprawy doktorskie
  3. Książki
  4. Części książek
  5. Streszczenia konferencji
  6. Raporty organizacyjne

Gotowa bibliografia na temat „Tropomyosins”

Autor: Grafiati
Data publikacji: 4 czerwca 2021
Data aktualizacji: 21 lutego 2023

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Artykuły w czasopismach na temat "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 ins
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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 r
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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 chan
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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 purifie
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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 asso
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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 we
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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 furr
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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 dist
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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 fro
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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 nonmusc
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Rozprawy doktorskie na temat "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 prev
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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 vari
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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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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 st
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Książki na temat "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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Części książek na temat "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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Streszczenia konferencji na temat "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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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 sys
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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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Raporty organizacyjne na temat "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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