Literatura científica selecionada sobre o tema "Myosin A"
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Artigos de revistas sobre o assunto "Myosin A"
Siththanandan, Verl B., e James R. Sellers. "Regulation of myosin 5a and myosin 7a". Biochemical Society Transactions 39, n.º 5 (21 de setembro de 2011): 1136–41. http://dx.doi.org/10.1042/bst0391136.
Texto completo da fonteBaines, I. C., H. Brzeska e E. D. Korn. "Differential localization of Acanthamoeba myosin I isoforms." Journal of Cell Biology 119, n.º 5 (1 de dezembro de 1992): 1193–203. http://dx.doi.org/10.1083/jcb.119.5.1193.
Texto completo da fonteBerg, Jonathan S., Bradford C. Powell e Richard E. Cheney. "A Millennial Myosin Census". Molecular Biology of the Cell 12, n.º 4 (abril de 2001): 780–94. http://dx.doi.org/10.1091/mbc.12.4.780.
Texto completo da fonteHammer, J. A., B. Bowers, B. M. Paterson e E. D. Korn. "Complete nucleotide sequence and deduced polypeptide sequence of a nonmuscle myosin heavy chain gene from Acanthamoeba: evidence of a hinge in the rodlike tail." Journal of Cell Biology 105, n.º 2 (1 de agosto de 1987): 913–25. http://dx.doi.org/10.1083/jcb.105.2.913.
Texto completo da fonteHeintzelman, M. B., T. Hasson e M. S. Mooseker. "Multiple unconventional myosin domains of the intestinal brush border cytoskeleton". Journal of Cell Science 107, n.º 12 (1 de dezembro de 1994): 3535–43. http://dx.doi.org/10.1242/jcs.107.12.3535.
Texto completo da fonteBerg, J. S., B. H. Derfler, C. M. Pennisi, D. P. Corey e R. E. Cheney. "Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin". Journal of Cell Science 113, n.º 19 (1 de outubro de 2000): 3439–51. http://dx.doi.org/10.1242/jcs.113.19.3439.
Texto completo da fontePost, P. L., G. M. Bokoch e M. S. Mooseker. "Human myosin-IXb is a mechanochemically active motor and a GAP for rho". Journal of Cell Science 111, n.º 7 (1 de abril de 1998): 941–50. http://dx.doi.org/10.1242/jcs.111.7.941.
Texto completo da fonteWylie, Steven R., e Peter D. Chantler. "Myosin IIC: A Third Molecular Motor Driving Neuronal Dynamics". Molecular Biology of the Cell 19, n.º 9 (setembro de 2008): 3956–68. http://dx.doi.org/10.1091/mbc.e07-08-0744.
Texto completo da fonteO'Halloran, T. J., S. Ravid e J. A. Spudich. "Expression of Dictyostelium myosin tail segments in Escherichia coli: domains required for assembly and phosphorylation." Journal of Cell Biology 110, n.º 1 (1 de janeiro de 1990): 63–70. http://dx.doi.org/10.1083/jcb.110.1.63.
Texto completo da fonteHasson, T., e M. S. Mooseker. "Porcine myosin-VI: characterization of a new mammalian unconventional myosin." Journal of Cell Biology 127, n.º 2 (15 de outubro de 1994): 425–40. http://dx.doi.org/10.1083/jcb.127.2.425.
Texto completo da fonteTeses / dissertações sobre o assunto "Myosin A"
Zhu, Jing. "The role of nonmuscle myosin IIA in endothelial cell". Morgantown, W. Va. : [West Virginia University Libraries], 2010. http://hdl.handle.net/10450/11006.
Texto completo da fonteTitle from document title page. Document formatted into pages; contains viii, 37 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 33-37).
Stevens, Richard. "Two light chains of the unconventional myosin Myo2p /". Thesis, Connect to this title online; UW restricted, 1997. http://hdl.handle.net/1773/9226.
Texto completo da fonteGuimard, Laurent. "Modélisation et synthèse de peptides interagissant avec une protéine cible : application au complexe calmoduline-RS20". Montpellier 1, 1995. http://www.theses.fr/1995MON1T037.
Texto completo da fontePetzoldt, Astrid G. "DE-cadherin regulates unconventional myosin ID through myosin IC in Drosophila melanogaster". Nice, 2009. http://www.theses.fr/2009NICE4048.
Texto completo da fonteThe accurate establishment of stereotyped L/R asymetry is subject to a strict genetic program and crucial for the functionality of the organism. It is only recently that the mechanism of L/R asymmetry establishment is exploited in the invertebrate species Drosphophila melanogaster (Hozumi et al. , 2006 ; Speder et al. , 2006). The unconventional type ID myosin (MyoID) has been characterised as a dextral determinant accountable for the clockwise (dextral) rotation of the male genital plate during pupae stage. In our attempt to isolate new components of the L/R mechanism, we first focussed on MyoIC, the closest homologue of genitalia, thus L/R axis inversion. We provide evidence that this situs inversus phenotype is du to an inhibition of MyoID function through MyoIC and consequently define MyoIC as an anti-dextral effector of MyoID. An interaction between MyoID and adherents junctions had been suggested by Speder et al. (2006) as the authors could show by two-hybrid screen and GST pull down that MyoID tail and beta-catenin cal physically interact. Our DE-cadherin loss and gain of function studies revealed a linear interaction between DE-cadherin zand the unconventional myosins MyoID and MyoIC. DE-cadherin controls MyoIC expression, acting as inhibitor of MyoIC. As MyoID functionality is regulated by MyoIC expression, myoIC functions as a mediator between DE-cadherin and myoID. In summary, we present in this study a new regulatory network of L/R asymmetry establishment, where DE-cadherin affects MyoID activity through regulation of MyoIC protein expression
Ripoll, Léa. "Role of myosin VI and actin dynamics in membrane remodeling during pigmentation". Thesis, Sorbonne Paris Cité, 2017. http://www.theses.fr/2017USPCB102.
Texto completo da fonteIntracellular transport among organelles and the plasma membrane occurs through the formation and transport of vesicular and tubular membrane carriers. The formation of these carriers requires first the bending of membrane and the generation of a bud, followed by its elongation to form the tubule-vesicle. Lastly, the carrier is released from the membrane source by the scission of the membrane. Importantly, all these different steps need an accurate orchestration to properly deform the membrane. The actions exerted by molecular motors onto microtubule and actin cytoskeletons provide forces onto membrane that contribute to its remodeling during the biogenesis of carrier. Actin filaments (F-actin) and myosins are thought to participate in the initiation and the fission of carriers. However, the role of actin machinery during carrier biogenesis remains elusive. We thus decided to address the role of F-actin and the actin-based motor myosin VI in the formation of tubular intermediates at melanosome. Melanosomes are lysosome-related organelles of skin melanocytes and eye pigment cells that function in the synthesis and storage of the melanin pigment. Melanosomes originate from endosomes and progressively mature into fully pigmented compartments, which fate is to be secreted and transferred to neighboring keratinocytes. Melanosomes are dynamic organelles that constantly receive, but also recycle proteins such as the SNARE VAMP7 through the formation and release of tubular intermediates. Our work reveals that myosin VI, together with Arp2/3- and WASH-mediated branched actin localize at specific melanosomal subdomains where they promote the constriction and scission of tubular intermediates. This fission event allows the export of components such as VAMP7 from melanosomes and promotes their maturation and subsequent transfer to keratinocytes. Altogether, our results uncover a new role for myosin VI and F-actin in the constriction and scission of membrane tubules at melanosome that is required for organelle homeostasis and function
Saeki, Nobutaka. "The Function of Myosin IX: the Ninth Class of Myosin Superfamily: a Dissertation". eScholarship@UMMS, 2005. http://escholarship.umassmed.edu/gsbs_diss/294.
Texto completo da fonteCartón, García Fernando. "Myosin VB in intestinal pathogenesis". Doctoral thesis, Universitat Autònoma de Barcelona, 2017. http://hdl.handle.net/10803/458251.
Texto completo da fonteMyosin VB is a molecular motor protein that uses the energy of ATP to move along actin filaments. It participates in the recycling endosomes trafficking in the subapical cytoplasmic region of non-polarized and polarized cells. It is highly expressed in the small and large intestine, where its role in the establishment of polarized function in enterocytes is also well known. Inactivating mutations of MYO5B have been associated with microvillus inclusion disease (MVID), a rare congenital disorder of the intestinal epithelial cells that presents with persistent life-threatening watery diarrhea. It is characterized by morphological enterocyte abnormalities such as microvillus atrophy and mislocalization of apical and basolateral protein transporters. The molecular pathology of the disease is not well known mainly due to the lack of animal models. In the present study, we report a versatile murine model with targeted inactivation of Myo5b. This model allowed us to generate and characterized a constitutive Myo5b knockout mice and a tamoxifen-inducible intestinal-epithelium-specific Myo5b knockout. In both cases, the mice closely resemble the phenotype of MVID patients, developing watery diarrhea and dehydration causing the death of the animal. Histological study of the intestine showed all the characteristic enterocyte defects observed in MVID patients, including microvillus atrophy and mislocalization of protein markers. Moreover, the inactivation of MYO5B also originated hyperproliferation of the intestinal crypts. Therefore, our mice constitute a useful model to further investigate the underlying molecular mechanism of this disease and to preclinically assess the efficacy of novel therapeutic approaches. In addition, hyperproliferation as well as loss of cell polarity, differentiation, and tissue architecture are hallmarks of advanced metastatic carcinomas and strongly correlate with poor patient prognosis. Specifically, for colorectal cancer, the third most common type of cancer worldwide, we have previously demonstrated that the loss of brush border MYO1A, also involved in cell polarity, promotes cancer progression and has tumor suppressor activity. Other studies have indicated a relationship between MYO5B inactivation and gastric cancer, promoting invasion and motility, but little is known regarding its role in colorectal cancer. To address this question, we have developed novel doxycycline-inducible in vitro models of MYO5B overexpression and downregulation. Moreover, we have generated MYO5B knockout Caco2-BBE cells using CRISPR/Cas9 technology. Our results showed changes in the polarization and differentiation of colon cancer cells, in agreement with previous observations in the normal intestine. Moreover, we have observed a relationship between MYO5B and the motility and invasion capacity of colon cancer cells, indicating a possible role of MYO5B in colon cancer progression. However, the effect of MYO5B loss in cell proliferation observed in our Myo5b knockout mice could not be confirmed in our models in vitro and in vivo, employing cell line-derived xenografts. In addition, using a tissue microarray containing triplicate samples from 155 primary Dukes C colorectal tumors, reduced MYO5B expression was found to be associated with shorter disease-free and overall survival of the patients. Moreover, poorly differentiated tumors showed significantly reduced expression of MYO5B. Collectively, our results indicate that MYO5B plays an important role in the differentiation of the normal intestinal epithelium and colon cancer cells, as well as a possible role in cancer progression promoting cell motility and invasion.
Tyrrell, Graham Philip. "Modelling the myosin molecular motor". Thesis, University of York, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.247144.
Texto completo da fonteThomas, Daniel G. "The self-interaction of myosin". Thesis, University of Leicester, 1992. http://hdl.handle.net/2381/35170.
Texto completo da fonteCarrington, Glenn Stuart Peter. "The flexibility of myosin 7a". Thesis, University of Leeds, 2018. http://etheses.whiterose.ac.uk/22504/.
Texto completo da fonteLivros sobre o assunto "Myosin A"
Sellers, James R. Motor proteins 2: myosin. London: Academic Press, 1995.
Encontre o texto completo da fonteMyosins. 2a ed. Oxford: Oxford University Press, 1999.
Encontre o texto completo da fonteSyrový, Ivo. Kontraktilní bílkoviny a funkční požadavky svalu. Praha: Academia, 1985.
Encontre o texto completo da fonte1933-, Sugi Haruo, e Pollack Gerald H, eds. Mechanism of myofilament sliding in muscle contraction. New York: Plenum Press, 1993.
Encontre o texto completo da fonteGriffiths, Hazel Sylvia. Studies on the properties and function of myosin light chain kinase. Birmingham: University of Birmingham, 1986.
Encontre o texto completo da fonteThomas, D. D. Molecular Interactions of Actin: Actin-Myosin Interaction and Actin-Based Regulation. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002.
Encontre o texto completo da fonteKeane, Anita M. Peptide mimetics of an actin-binding site on the myosin head. Birmingham: University of Birmingham, 1991.
Encontre o texto completo da fonteMilankov, Kosta. Immunocytochemical localization of actin and myosin within interphase nuclei in situ. Ottawa: National Library of Canada, 1993.
Encontre o texto completo da fonteEpp, Trevor Allan. Characterization of the human cardiac gas-myosin heavy chain gene. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1993.
Encontre o texto completo da fonteEastwood, Anthony Michael. The use of peptide mimetics in defining the actin-myosin interaction. Birmingham: University of Birmingham, 1994.
Encontre o texto completo da fonteCapítulos de livros sobre o assunto "Myosin A"
Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, Matthias Gaestel, Shiri Procaccia, Rony Seger, Shin Yasuda et al. "Myosin II, “Conventional” Myosin". In Encyclopedia of Signaling Molecules, 1169. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100886.
Texto completo da fonteLackner, K. J., e D. Peetz. "Myosin". In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_2210-1.
Texto completo da fonteLackner, K. J., e D. Peetz. "Myosin". In Springer Reference Medizin, 1711. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_2210.
Texto completo da fonteWard, Tony Milford. "Myosin". In Proteins and Tumour Markers May 1995, 1286–87. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0681-8_54.
Texto completo da fonteAitchison Smith, David. "Myosin Motors". In The Sliding-Filament Theory of Muscle Contraction, 237–91. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-030-03526-6_6.
Texto completo da fonteTokuo, Hiroshi. "Myosin X". In Advances in Experimental Medicine and Biology, 391–403. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_17.
Texto completo da fonteBugyi, Beáta, e András Kengyel. "Myosin XVI". In Advances in Experimental Medicine and Biology, 405–19. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_18.
Texto completo da fonteTaft, Manuel H., e Sharissa L. Latham. "Myosin XVIII". In Advances in Experimental Medicine and Biology, 421–38. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_19.
Texto completo da fonteSweeney, H. Lee, Anne Houdusse e Julien Robert-Paganin. "Myosin Structures". In Advances in Experimental Medicine and Biology, 7–19. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_2.
Texto completo da fonteBocanegra, Jennifer L., Rebecca Adikes e Omar A. Quintero. "Myosin XIX". In Advances in Experimental Medicine and Biology, 439–51. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_20.
Texto completo da fonteTrabalhos de conferências sobre o assunto "Myosin A"
Egan, Paul F., Philip R. LeDuc, Jonathan Cagan e Christian Schunn. "A Design Exploration of Genetically Engineered Myosin Motors". In ASME 2011 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2011. http://dx.doi.org/10.1115/detc2011-48568.
Texto completo da fonteEgan, Paul F., Jonathan Cagan, Christian Schunn e Philip R. LeDuc. "Design of Complex Nano-Scale Systems Using Multi-Agent Simulations and Structure-Behavior-Function Representations". In ASME 2012 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/detc2012-70291.
Texto completo da fonteAprodu, Iuliana, Alberto Redaelli, Franco Maria Montevecchi e Monica Soncini. "Mechanical Characterization of Myosin II, Actin and Their Complexes by Molecular Mechanics Approach". In ASME 8th Biennial Conference on Engineering Systems Design and Analysis. ASMEDC, 2006. http://dx.doi.org/10.1115/esda2006-95670.
Texto completo da fonteDaniel, J. L., e M. Rigmaiden. "Evidence for Ca2+-independent phosphorylation of human platelet myosin". In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644527.
Texto completo da fonteHaghshenas-Jaryani, Mahdi, e Alan Bowling. "Multiscale Dynamic Modeling of Flexibility in Myosin V". 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/detc2013-13154.
Texto completo da fonteKostcheeva, O. I., V. Yu Ostchepkova, M. R. Sharipov, D. V. Stchepkin e G. V. Kopylova. "Influence of the myosin activator omecamptive-mecarbil onto the actin-myosin interaction in the myocard". In VI Information school of a young scientist. Central Scientific Library of the Urals Branch of the Russian Academy of Sciences, 2018. http://dx.doi.org/10.32460/ishmu-2018-6-0023.
Texto completo da fonteNikmaneshi, Mohammad Reza, Bahar Firoozabadi e Mohammad Said Saidi. "Continuum model of actin-myosin flow". In 2013 20th Iranian Conference on Biomedical Engineering (ICBME). IEEE, 2013. http://dx.doi.org/10.1109/icbme.2013.6782200.
Texto completo da fonteLE GOFF, L., F. AMBLARD e E. M. FURST. "VISCOELASTICITY OF ACTIVE ACTIN-MYOSIN NETWORKS". In Proceedings of the International Symposium. WORLD SCIENTIFIC, 2003. http://dx.doi.org/10.1142/9789812704931_0010.
Texto completo da fonteBidone, Tamara Carla, Haosu Tang e Dimitrios Vavylonis. "Insights Into the Mechanics of Cytokinetic Ring Assembly Using 3D Modeling". In ASME 2014 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2014. http://dx.doi.org/10.1115/imece2014-39006.
Texto completo da fonteChin, LY, Y. Bosse, PD Pare e CY Seow. "Myosin Filament Assembly in Airway Smooth Muscle." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2063.
Texto completo da fonteRelatórios de organizações sobre o assunto "Myosin A"
Sadot, Einat, Christopher Staiger e Mohamad Abu-Abied. Studies of Novel Cytoskeletal Regulatory Proteins that are Involved in Abiotic Stress Signaling. United States Department of Agriculture, setembro de 2011. http://dx.doi.org/10.32747/2011.7592652.bard.
Texto completo da fonteSanders, Luraynne. Cell Adhesion, Signaling and Myosin in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, agosto de 2000. http://dx.doi.org/10.21236/ada392857.
Texto completo da fonteSanders, Luraynne C. Cell Adhesion, Signaling and Myosin in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, agosto de 1999. http://dx.doi.org/10.21236/ada382496.
Texto completo da fonteChew, Teng-Leong. Regulation of Actin-Myosin Cytoskeletal Changes Involved in Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, julho de 2001. http://dx.doi.org/10.21236/ada396798.
Texto completo da fonteHofmann, Wilma A. The Role of a Novel Myosin Isoform in Prostate Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, outubro de 2013. http://dx.doi.org/10.21236/ada593300.
Texto completo da fonteZhang, John Q. Post-Myocardial Infarction and Exercise Training on Myosin Heavy Chain and Cardiac Function. Science Repository, abril de 2019. http://dx.doi.org/10.31487/j.jicoa.2019.01.08.
Texto completo da fonteSchiefelbein, J. Molecular genetics of myosin motors in Arabidopsis. Final report, July 1, 1992--June 30, 1996. Office of Scientific and Technical Information (OSTI), fevereiro de 1997. http://dx.doi.org/10.2172/486111.
Texto completo da fonteStaiger, Christopher. Regulation of Cell Wall Assembly: Myosin and Exocyst Involvement in Cellulose Synthase Delivery to the Plasma Membrane. Office of Scientific and Technical Information (OSTI), janeiro de 2022. http://dx.doi.org/10.2172/1840725.
Texto completo da fonteGabaix, Xavier, e David Laibson. Myopia and Discounting. Cambridge, MA: National Bureau of Economic Research, março de 2017. http://dx.doi.org/10.3386/w23254.
Texto completo da fonteAngeletos, George-Marios, e Zhen Huo. Myopia and Anchoring. Cambridge, MA: National Bureau of Economic Research, abril de 2018. http://dx.doi.org/10.3386/w24545.
Texto completo da fonte