Relevant bibliographies by topics / Myosine-X

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

Academic literature on the topic 'Myosine-X'

Author: Grafiati
Published: 25 May 2024
Last updated: 19 July 2025

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Journal articles on the topic "Myosine-X"

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Berg, J. S., B. H. Derfler, C. M. Pennisi, D. P. Corey, and R. E. Cheney. "Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin." Journal of Cell Science 113, no. 19 (2000): 3439–51. http://dx.doi.org/10.1242/jcs.113.19.3439.

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Myosin-X is the founding member of a novel class of unconventional myosins characterized by a tail domain containing multiple pleckstrin homology domains. We report here the full-length cDNA sequences of human and bovine myosin-X as well as the first characterization of this protein's distribution and biochemical properties. The 235 kDa myosin-X contains a head domain with <45% protein sequence identity to other myosins, three IQ motifs, and a predicted stalk of coiled coil. Like several other unconventional myosins and a plant kinesin, myosin-X contains both a myosin tail homology 4 (M
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2

Novakovic, Valerie A., and Gary E. Gilbert. "Procoagulant activities of skeletal and cardiac muscle myosin depend on contaminating phospholipid." Blood 136, no. 21 (2020): 2469–72. http://dx.doi.org/10.1182/blood.2020005930.

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Abstract Recent reports indicate that suspended skeletal and cardiac myosin, such as might be released during injury, can act as procoagulants by providing membrane-like support for factors Xa and Va in the prothrombinase complex. Further, skeletal myosin provides membrane-like support for activated protein C. This raises the question of whether purified muscle myosins retain procoagulant phospholipid through purification. We found that lactadherin, a phosphatidyl-l-serine–binding protein, blocked >99% of prothrombinase activity supported by rabbit skeletal and by bovine cardiac myosin.
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Rogers, Michael S., and Emanuel E. Strehler. "The Tumor-sensitive Calmodulin-like Protein Is a Specific Light Chain of Human Unconventional Myosin X." Journal of Biological Chemistry 276, no. 15 (2001): 12182–89. http://dx.doi.org/10.1074/jbc.m010056200.

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Human calmodulin-like protein (CLP) is an epithelial-specific Ca2+-binding protein whose expression is strongly down-regulated in cancers. Like calmodulin, CLP is thought to regulate cellular processes via Ca2+-dependent interactions with specific target proteins. Using gel overlays, we identified a ∼210-kDa protein binding specifically and in a Ca2+-dependent manner to CLP, but not to calmodulin. Yeast two-hybrid screening yielded a CLP-interacting clone encoding the three light chain binding IQ motifs of human “unconventional” myosin X. Pull-down experiments showed CLP binding to the IQ doma
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Naydenov, Nayden, Susana Lechuga, Emina Huang, and Andrei Ivanov. "Myosin Motors: Novel Regulators and Therapeutic Targets in Colorectal Cancer." Cancers 13, no. 4 (2021): 741. http://dx.doi.org/10.3390/cancers13040741.

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Colorectal cancer (CRC) remains the third most common cause of cancer and the second most common cause of cancer deaths worldwide. Clinicians are largely faced with advanced and metastatic disease for which few interventions are available. One poorly understood aspect of CRC involves altered organization of the actin cytoskeleton, especially at the metastatic stage of the disease. Myosin motors are crucial regulators of actin cytoskeletal architecture and remodeling. They act as mechanosensors of the tumor environments and control key cellular processes linked to oncogenesis, including cell di
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Brown, Lisa D., and Marie E. Cantino. "Immunocytochemical Localization of Myosin Light Chains in the Abdominal Superficial Flexor Muscles of the American Lobster, Homarus Americanus." Microscopy and Microanalysis 4, S2 (1998): 1118–19. http://dx.doi.org/10.1017/s143192760002571x.

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Myosin is composed of two high-molecular weight heavy chains and four low-molecular weight hght chains. In both vertebrate and invertebrate skeletal muscle, each myosin heavy chain is associated with two myosin light chains. In skeletal muscle myosins studied by X-ray diffraction, each myosin heavy chain binds one of each of two distinct classes of hght chains. Thus, while isoform distributions may vary within and between fibers, the spatial distribution of each class of light chain should be uniform within the A band and between sarcomeres and fibers. Since no such study exists for crustacean
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Squire, John. "Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview." International Journal of Molecular Sciences 20, no. 22 (2019): 5715. http://dx.doi.org/10.3390/ijms20225715.

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Muscular contraction is a fundamental phenomenon in all animals; without it life as we know it would be impossible. The basic mechanism in muscle, including heart muscle, involves the interaction of the protein filaments myosin and actin. Motility in all cells is also partly based on similar interactions of actin filaments with non-muscle myosins. Early studies of muscle contraction have informed later studies of these cellular actin-myosin systems. In muscles, projections on the myosin filaments, the so-called myosin heads or cross-bridges, interact with the nearby actin filaments and, in a m
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Dillmann, W. H. "Methyl palmoxirate increases Ca2+-myosin ATPase activity and changes myosin isoenzyme distribution in the diabetic rat heart." American Journal of Physiology-Endocrinology and Metabolism 248, no. 5 (1985): E602—E606. http://dx.doi.org/10.1152/ajpendo.1985.248.5.e602.

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Previous studies have shown that in rats diabetes mellitus leads to a decrease in cardiac ventricle myosin V1 and an increase in myosin V3 levels. Insulin administration reverts myosin isoenzyme distribution to normal levels. It is currently unclear whether the effects of insulin on myosin isoenzyme distribution are a direct effect of the hormone or are mediated through insulin-induced alterations in cardiac metabolism. To gain further insight into this question diabetic rats received methyl palmoxirate, a potent inhibitor of long-chain fatty acid oxidation. Administration of 25 mg methyl palm
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Courson, David S., and Richard E. Cheney. "Myosin-X and disease." Experimental Cell Research 334, no. 1 (2015): 10–15. http://dx.doi.org/10.1016/j.yexcr.2015.03.014.

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Almagro, Sébastien, Claire Durmort, Adeline Chervin-Pétinot, et al. "The Motor Protein Myosin-X Transports VE-Cadherin along Filopodia To Allow the Formation of Early Endothelial Cell-Cell Contacts." Molecular and Cellular Biology 30, no. 7 (2010): 1703–17. http://dx.doi.org/10.1128/mcb.01226-09.

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ABSTRACT Vascular endothelium (VE), the monolayer of endothelial cells that lines the vascular tree, undergoes damage at the basis of some vascular diseases. Its integrity is maintained by VE-cadherin, an adhesive receptor localized at cell-cell junctions. Here, we show that VE-cadherin is also located at the tip and along filopodia in sparse or subconfluent endothelial cells. We observed that VE-cadherin navigates along intrafilopodial actin filaments. We found that the actin motor protein myosin-X is colocalized and moves synchronously with filopodial VE-cadherin. Immunoprecipitation and pul
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Ikebe, Mitsuo, Osamu Sato, and Tsuyoshi Sakai. "Myosin X and Cytoskeletal Reorganization." Applied Microscopy 48, no. 2 (2018): 33–42. http://dx.doi.org/10.9729/am.2018.48.2.33.

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Dissertations / Theses on the topic "Myosine-X"

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Crozet, Flora. "Somatic cells enhance the oocyte developmental potential through cytoplasmic protrusions." Electronic Thesis or Diss., Sorbonne université, 2021. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2021SORUS166.pdf.

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Chez les femelles mammifères, les cellules somatiques qui entourent l’ovocyte, les cellules de la granulosa, coordonnent le développement ovocytaire post-partum, la croissance ovocytaire et la maturation méiotique, en dialoguant avec l’ovocyte. Ce dialogue est principalement établi par contact intercellulaire grâce à des protrusions des cellules de la granulosa, les projections transzonales (TZPs). Les TZPs ressemblent à des filopodes, résident dans la matrice extracellulaire entourant l’ovocyte, la zone pellucide, et établissent des jonctions gap et d’adhérence avec la membrane de l’ovocyte.
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Planelles, Herrero Vicente José. "Bases mécanistiques et structurales de la régulation de l'activité des myosines." Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066465.

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Les moteurs moléculaires sont des protéines capables de produire une force : elles transforment l'énergie chimique de l'hydrolyse de l'ATP en énergie mécanique. Cette thèse se focalise sur l'étude d'une famille de moteurs moléculaires, les myosines, qui se déplacent le long des filaments d'actine et assurent d'importantes fonctions cellulaires.La myosine VI est une myosine très particulière car elle est la seule à se déplacer vers l'extrémité négative des filaments d'actine. Elle est produite dans la cellule sous forme auto-inhibée, inactive. Dans la cellule, son activité est également régulée
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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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Planelles, Herrero Vicente José. "Bases mécanistiques et structurales de la régulation de l'activité des myosines." Electronic Thesis or Diss., Paris 6, 2017. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2017PA066465.pdf.

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Les moteurs moléculaires sont des protéines capables de produire une force : elles transforment l'énergie chimique de l'hydrolyse de l'ATP en énergie mécanique. Cette thèse se focalise sur l'étude d'une famille de moteurs moléculaires, les myosines, qui se déplacent le long des filaments d'actine et assurent d'importantes fonctions cellulaires.La myosine VI est une myosine très particulière car elle est la seule à se déplacer vers l'extrémité négative des filaments d'actine. Elle est produite dans la cellule sous forme auto-inhibée, inactive. Dans la cellule, son activité est également régulée
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Bohil, Aparna Bhaskar Cheney Richard E. "Myosin-X is a molecular motor central to filopodia formation, adhesion, and signaling." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2006. http://dc.lib.unc.edu/u?/etd,713.

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Thesis (Ph. D.)--University of North Carolina at Chapel Hill, 2006.<br>Title from electronic title page (viewed Oct. 10, 2007). "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Cell and Molecular Physiology - School of Medicine." Discipline: Cell and Molecular Physiology; Department/School: Medicine.
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Prestidge, M. C. "Data analysis and processing in X-ray diffraction studies from myosin heads in muscle." Thesis, Open University, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.292345.

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Da, Silva Ambrose Gihan. "X-ray diffraction studies of the conformation of myosin heads in relaxed frog muscle." Thesis, King's College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300318.

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Juanhuix, Gibert Jordi. "Estructura molecular i funció dels músculs vius." Doctoral thesis, Universitat Autònoma de Barcelona, 2001. http://hdl.handle.net/10803/3330.

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El múscul és un fabulós motor orgànic que a nivell molecular és capaç de convertir energia química, provinent essencialment del menjar, en força mecànica. Al seu estudi s'hi han dedicat grans esforços des de molts camps d'investigació, l'objectiu últim dels quals és trobar la resposta a la pregunta 'd'or': Com fa força i provoca moviment el múscul?<br/>Aquesta tesi resol precisament un aspecte essencial de la pregunta: l'orientació dels caps de miosina en diferents estats musculars. Aquests caps són les proteïnes que enllacen els dos elements actius de la contracció: els filaments prims i grui
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岩野, さやか. "細胞の分裂軸を制御するPCTK1-KAP0-myosin Xシグナル伝達経路の解明". Kyoto University, 2015. http://hdl.handle.net/2433/199560.

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Addisu, Anteneh. "Natriuretic peptides as a humoral link between the heart and the gastrointestinal system." [Tampa, Fla] : University of South Florida, 2008. http://purl.fcla.edu/usf/dc/et/SFE0002406.

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Book chapters on the topic "Myosine-X"

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Tokuo, Hiroshi. "Myosin X." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_17.

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Tokuo, Hiroshi. "Myosin X." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_404.

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Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, et al. "Myosin X." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_404.

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Cecchi, Giovanni, M. Angela Bagni, Barbara Colombini, et al. "Use of Sinusoidal Length Oscillations to Detect Myosin Conformation by Time- Resolved X-Ray Diffraction." In Advances in Experimental Medicine and Biology. Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9029-7_25.

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Arata, T., S. Kimura, Y. Sugimoto, Y. Takezawa, N. Iwasaki, and K. Wakabayashi. "Structure of the Monomeric Actin-Myosin Head Complex as Revealed by X-Ray Solution Scattering." In Advances in Experimental Medicine and Biology. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4684-6039-1_9.

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Reconditi, Massimo, Ian Dobbie, Malcolm Irving, et al. "Myosin Head Movements during Isometric Contraction Studied by X-Ray Diffraction of Single Frog Muscle Fibres." In Advances in Experimental Medicine and Biology. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4684-6039-1_31.

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Oshima, Kanji, Yasunori Takezawa, Yasunobu Sugimoto, Maya Kiyotoshi, and Katsuzo Wakabayashi. "Modeling Analysis of Myosin-Based Meridional X-Ray Reflections from Frog Skeletal Muscles in Relaxed and Contracting States." In Advances in Experimental Medicine and Biology. Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9029-7_23.

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Takezawa, Yasunori, Yasunobu Sugimoto, and Katsuzo Wakabayashi. "Extensibility of the Actin and Myosin Filaments in Various States of Skeletal Muscle as Studied by X-Ray Diffraction." In Advances in Experimental Medicine and Biology. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4684-6039-1_36.

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Conference papers on the topic "Myosine-X"

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Fujimura, K., T. Fujimoto, M. Takemoto, K. Oda, S. Maehama, and A. Kuramoto. "INTERACTION OF MEMBRANE GLYCOPROTEIN GPIIb AND Ilia WITH CYTOSKELETAL PROTEINS DURING PLATELET ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643515.

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Experiments were designed and performed to analyse the cytoskeleton assembly and the interaction of glycoprotein (GP)IIb, IIIa and cytoskeletal proteins during platelet activation. A23187 stimulated 125I labeled platelets were solubilised with Triton X-100 solution and centrifuged. The insoluble fraction were analysed by two dimensional electrophoresis and the soluble fraction were fractionated with 5-25% sucrose gradient centrifugation and analysed by SDS PAGE. In Triton X-100 insoluble fraction, high molecular weight protein fraction(MW &gt; 106) was present after stimulation which were cons
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Shibatay, N., K. Tanaka, K. Okamoto, and T. Onji. "REORGANIZATION OF ACTIN AND MYOSIN IN THE ACTIVATED PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643539.

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This study was done to clarify the intracellular dynamic arrangements of myosin(My) and actin(Ac) in activation process of human platelets (PLs) from unactivated to activated stage (clot retraction) in electron microscopy. The observation of unactivated PLs was done either in the fresh whole blood fixed directly with 0.1 % glutaraldehyde or in PLs isolated by gel filtration of platelet rich plasma(PRP) containing prostaglandin I2 (10 ng/ml). The isolated PLs mounted on a glass cover slip were used as activated PLs (adrerent ones). The contracted PLs were prepared in PRP incubated with thrombin
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