Relevant bibliographies by topics / Myosin A

Contents

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

Academic literature on the topic 'Myosin A'

Author: Grafiati
Published: 25 May 2024

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Journal articles on the topic "Myosin A"

1

Siththanandan, Verl B., and James R. Sellers. "Regulation of myosin 5a and myosin 7a." Biochemical Society Transactions 39, no. 5 (2011): 1136–41. http://dx.doi.org/10.1042/bst0391136.

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The myosin superfamily is diverse in its structure, kinetic mechanisms and cellular function. The enzymatic activities of most myosins are regulated by some means such as Ca2+ ion binding, phosphorylation or binding of other proteins. In the present review, we discuss the structural basis for the regulation of mammalian myosin 5a and Drosophila myosin 7a. We show that, although both myosins have a folded inactive state in which domains in the myosin tail interact with the motor domain, the details of the regulation of these two myosins differ greatly.
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Baines, I. C., H. Brzeska, and E. D. Korn. "Differential localization of Acanthamoeba myosin I isoforms." Journal of Cell Biology 119, no. 5 (1992): 1193–203. http://dx.doi.org/10.1083/jcb.119.5.1193.

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Acanthamoeba myosins IA and IB were localized by immunofluorescence and immunoelectron microscopy in vegetative and phagocytosing cells and the total cell contents of myosins IA, IB, and IC were quantified by immunoprecipitation. The quantitative distributions of the three myosin I isoforms were then calculated from these data and the previously determined localization of myosin IC. Myosin IA occurs almost exclusively in the cytoplasm, where it accounts for approximately 50% of the total myosin I, in the cortex beneath phagocytic cups and in association with small cytoplasmic vesicles. Myosin
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Berg, Jonathan S., Bradford C. Powell, and Richard E. Cheney. "A Millennial Myosin Census." Molecular Biology of the Cell 12, no. 4 (2001): 780–94. http://dx.doi.org/10.1091/mbc.12.4.780.

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The past decade has seen a remarkable explosion in our knowledge of the size and diversity of the myosin superfamily. Since these actin-based motors are candidates to provide the molecular basis for many cellular movements, it is essential that motility researchers be aware of the complete set of myosins in a given organism. The availability of cDNA and/or draft genomic sequences from humans,Drosophila melanogaster, Caenorhabditis elegans, Arabidopsis thaliana,Saccharomyces cerevisiae, Schizosaccharomyces pombe, andDictyostelium discoideum has allowed us to tentatively define and compare the s
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Hammer, J. A., B. Bowers, B. M. Paterson, and 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, no. 2 (1987): 913–25. http://dx.doi.org/10.1083/jcb.105.2.913.

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We have completely sequenced a gene encoding the heavy chain of myosin II, a nonmuscle myosin from the soil ameba Acanthamoeba castellanii. The gene spans 6 kb, is split by three small introns, and encodes a 1,509-residue heavy chain polypeptide. The positions of the three introns are largely conserved relative to characterized vertebrate and invertebrate muscle myosin genes. The deduced myosin II globular head amino acid sequence shows a high degree of similarity with the globular head sequences of the rat embryonic skeletal muscle and nematode unc 54 muscle myosins. By contrast, there is no
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Heintzelman, M. B., T. Hasson, and M. S. Mooseker. "Multiple unconventional myosin domains of the intestinal brush border cytoskeleton." Journal of Cell Science 107, no. 12 (1994): 3535–43. http://dx.doi.org/10.1242/jcs.107.12.3535.

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Representatives of class V and class VI unconventional myosins are identified as components of the intestinal brush border cytoskeleton. With brush border myosin-I and myosin-II, this brings to four the number of myosin classes associated with this one subcellular domain and represents the first characterization of four classes of myosins expressed in a single metazoan cell type. The distribution and cytoskeletal association of each myosin is distinct as assessed by both biochemical fractionation and immunofluorescence localization. Myosin-VI exists in both the microvillus and terminal web alt
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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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Post, P. L., G. M. Bokoch, and M. S. Mooseker. "Human myosin-IXb is a mechanochemically active motor and a GAP for rho." Journal of Cell Science 111, no. 7 (1998): 941–50. http://dx.doi.org/10.1242/jcs.111.7.941.

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The heavy chains of the class IX myosins, rat myr5 and human myosin-IXb, contain within their tail domains a region with sequence homology to GTPase activating proteins for the rho family of G proteins. Because low levels of myosin-IXb expression preclude purification by conventional means, we have employed an immunoadsorption strategy to purify myosin-IXb, enabling us to characterize the mechanochemical and rho-GTPase activation properties of the native protein. In this report we have examined the light chain content, actin binding properties, in vitro motility and rho-GTPase activity of huma
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Wylie, Steven R., and Peter D. Chantler. "Myosin IIC: A Third Molecular Motor Driving Neuronal Dynamics." Molecular Biology of the Cell 19, no. 9 (2008): 3956–68. http://dx.doi.org/10.1091/mbc.e07-08-0744.

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Neuronal dynamics result from the integration of forces developed by molecular motors, especially conventional myosins. Myosin IIC is a recently discovered nonsarcomeric conventional myosin motor, the function of which is poorly understood, particularly in relation to the separate but coupled activities of its close homologues, myosins IIA and IIB, which participate in neuronal adhesion, outgrowth and retraction. To determine myosin IIC function, we have applied a comparative functional knockdown approach by using isoform-specific antisense oligodeoxyribonucleotides to deplete expression withi
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O'Halloran, T. J., S. Ravid, and J. A. Spudich. "Expression of Dictyostelium myosin tail segments in Escherichia coli: domains required for assembly and phosphorylation." Journal of Cell Biology 110, no. 1 (1990): 63–70. http://dx.doi.org/10.1083/jcb.110.1.63.

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The assembly of myosins into filaments is a property common to all conventional myosins. The ability of myosins to form filaments is conferred by the tail of the large asymmetric molecule. We are studying cloned portions of the Dictyostelium myosin gene expressed in Escherichia coli to investigate functional properties of defined segments of the myosin tail. We have focused on five segments derived from the 68-kD carboxyl-terminus of the myosin tail. These have been expressed and purified to homogeneity from E. coli, and thus the boundaries of each segment within the myosin gene and protein se
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Hasson, T., and M. S. Mooseker. "Porcine myosin-VI: characterization of a new mammalian unconventional myosin." Journal of Cell Biology 127, no. 2 (1994): 425–40. http://dx.doi.org/10.1083/jcb.127.2.425.

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We have cloned a new mammalian unconventional myosin, porcine myosin-VI from the proximal tubule cell line, LLC-PK1 (CL4). Porcine myosin-VI is highly homologous to Drosophila 95F myosin heavy chain, and together these two myosins comprise a sixth class of myosin motors. Myosin-VI exhibits ATP-sensitive actin-binding activities characteristic of myosins, and it is associated with a calmodulin light chain. Within LLC-PK1 cells, myosin-VI is soluble and does not associate with the major actin-containing domains. Within the kidney, however, myosin-VI is associated with sedimentable structures and
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Dissertations / Theses on the topic "Myosin A"

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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.

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Thesis (M.S.)--West Virginia University, 2010.<br>Title from document title page. Document formatted into pages; contains viii, 37 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 33-37).
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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.

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Guimard, Laurent. "Modélisation et synthèse de peptides interagissant avec une protéine cible : application au complexe calmoduline-RS20." Montpellier 1, 1995. http://www.theses.fr/1995MON1T037.

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Petzoldt, Astrid G. "DE-cadherin regulates unconventional myosin ID through myosin IC in Drosophila melanogaster." Nice, 2009. http://www.theses.fr/2009NICE4048.

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L’établissement précis de l’asymétrie G/D stéréotypée, qui est contrôlé par un programme génétique, est crucial pour le fonctionnement d’un organisme. Ce n’est que depuis récemment que le mécanisme de l’établissement de l’asymétrie G/D est étudié chez l’invertébré Drosophila Melanogaster (Hozumi et al. , 2006 ; Speder et al. , 2006). La Myosine non conventionnelle de type ID (MyoID) a été caractérisée comme un déterminant de la rotation dextrale de la plaque génitale mâme pendant le stade pupal. Afin d’identifier de nouveaux effecteurs de MyoID, nous nous sommes concentrés sur son plus proche
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Ripoll, Léa. "Role of myosin VI and actin dynamics in membrane remodeling during pigmentation." Thesis, Sorbonne Paris Cité, 2017. http://www.theses.fr/2017USPCB102.

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Le trafic intracellulaire consiste en la formation et le transport de vésicules ou tubules qui acheminent des composants protéiques et lipidiques entre les différents organites ou avec la membrane plasmique. L’élaboration de ces tubulo-vésicules est initiée par le remodelage local d’une membrane, tout d’abord en générant une courbure puis un bourgeon qui, s’allongeant, forme la tubulo-vésicule. Enfin, la rupture de la membrane, ou scission, libère le transporteur nouvellement formé. Ces étapes repose sur un sculptage profond de la membrane. Ceci requière des forces générées par des moteurs mol
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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.

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Among 18 family members in the myosin superfamily, myosin IX is unique by possessing a GTPase activating protein (GAP) for Rho. It is also attention-grabbing since it is a single-headed processive motor, as well as a minus-end directed motor. Although many biochemical properties have been revealed, its physiological function is largely unknown. As an initial step to address this question, I attempted to find the binding partner of myosin IXb using the yeast two-hybrid screen. Through the screen using the tail domain of myosin IXb as bait I found BIG1, a guanine nucleotide exchange factor (GEF)
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Cartón, García Fernando. "Myosin VB in intestinal pathogenesis." Doctoral thesis, Universitat Autònoma de Barcelona, 2017. http://hdl.handle.net/10803/458251.

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Miosina VB es una proteína que actúa como un motor molecular usando la energía del ATP para moverse a lo largo de filamentos de actina. Participa en el trafico intracelular de endosomas de reciclaje en la parte subapical de células polarizadas y no polarizadas. Su expresión es muy abundante en el intestino donde participa en el establecimiento y mantenimiento de la polaridad de los enterocitos. Mutaciones en MYO5B causan la enfermedad de inclusión de microvellosidades, in raro trastorno congénito que afecta a las células epiteliales del intestino cursando con diarrea acuosa persistente que sue
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Tyrrell, Graham Philip. "Modelling the myosin molecular motor." Thesis, University of York, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.247144.

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Thomas, Daniel G. "The self-interaction of myosin." Thesis, University of Leicester, 1992. http://hdl.handle.net/2381/35170.

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The first event in thick filament formation must be the interaction of one myosin monomer with another to give a dimer. The energetics of the parallel apposition of the rod portion of myosin were first considered by McLachlan and Karn (Nature 299: 226-231, 1982; J. Mol. Biol. 164: 605-626, 1983). They applied a simple 'point scoring' algorithm to the periodic charge distribution of the myosin rod and suggested that there are peaks in interaction energy when the stagger between parallel rods is close to 14.3 and 43nm. We have modelled the assembly process on a more detailed basis in an attempt
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Carrington, Glenn Stuart Peter. "The flexibility of myosin 7a." Thesis, University of Leeds, 2018. http://etheses.whiterose.ac.uk/22504/.

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Myosin 7a is a molecular motor found in hair cells of the ear and the photoreceptor cells of the eye. Myosin 7a is comprised of an actin-binding motor domain, a lever; which is composed of 5 IQ motifs that can potentially bind 5 light chains followed by a single alpha helical (SAH) domain, and a tail composed of 2 MyTH4-FERM domains. The lever is an essential mechanical element in myosin 7a function, but an understanding of its mechanical properties and how these derive from its substructure is lacking. It has been observed in vitro that myosin 7a is able to regulate its activity through a hea
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Books on the topic "Myosin A"

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Sellers, James R. Motor proteins 2: myosin. Academic Press, 1995.

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Myosins. 2nd ed. Oxford University Press, 1999.

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Syrový, Ivo. Kontraktilní bílkoviny a funkční požadavky svalu. Academia, 1985.

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1933-, Sugi Haruo, and Pollack Gerald H, eds. Mechanism of myofilament sliding in muscle contraction. Plenum Press, 1993.

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Griffiths, Hazel Sylvia. Studies on the properties and function of myosin light chain kinase. University of Birmingham, 1986.

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Thomas, D. D. Molecular Interactions of Actin: Actin-Myosin Interaction and Actin-Based Regulation. Springer Berlin Heidelberg, 2002.

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Keane, Anita M. Peptide mimetics of an actin-binding site on the myosin head. University of Birmingham, 1991.

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Milankov, Kosta. Immunocytochemical localization of actin and myosin within interphase nuclei in situ. National Library of Canada, 1993.

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Epp, Trevor Allan. Characterization of the human cardiac gas-myosin heavy chain gene. National Library of Canada = Bibliothèque nationale du Canada, 1993.

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Eastwood, Anthony Michael. The use of peptide mimetics in defining the actin-myosin interaction. University of Birmingham, 1994.

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Book chapters on the topic "Myosin A"

1

Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, et al. "Myosin II, “Conventional” Myosin." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100886.

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Lackner, K. J., and D. Peetz. "Myosin." In Lexikon der Medizinischen Laboratoriumsdiagnostik. Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_2210-1.

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Lackner, K. J., and D. Peetz. "Myosin." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_2210.

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Ward, Tony Milford. "Myosin." In Proteins and Tumour Markers May 1995. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0681-8_54.

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Aitchison Smith, David. "Myosin Motors." In The Sliding-Filament Theory of Muscle Contraction. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-030-03526-6_6.

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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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Bugyi, Beáta, and András Kengyel. "Myosin XVI." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_18.

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Taft, Manuel H., and Sharissa L. Latham. "Myosin XVIII." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_19.

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Sweeney, H. Lee, Anne Houdusse, and Julien Robert-Paganin. "Myosin Structures." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_2.

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Bocanegra, Jennifer L., Rebecca Adikes, and Omar A. Quintero. "Myosin XIX." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5_20.

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Conference papers on the topic "Myosin A"

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Egan, Paul F., Philip R. LeDuc, Jonathan Cagan, and 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.

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As technology advances, there is an increasing need to reliably output mechanical work at smaller scales. At the nanoscale, one of the most promising routes is utilizing biomolecular motors such as myosin proteins commonly found in cells. Myosins convert chemical energy into mechanical energy and are strong candidates for use as components of artificial nanodevices and multi-scale systems. Isoforms of the myosin superfamily of proteins are fine-tuned for specific cellular tasks such as intracellular transport, cell division, and muscle contraction. The modular structure that all myosins share
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Egan, Paul F., Jonathan Cagan, Christian Schunn, and 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.

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Recent trends in technology are challenging engineers to configure products at ever smaller scales. At the nano-scale, biological protein machines are commonly chosen as a power-source for a broad-range of nano-devices. This paper explores the challenges in designing these and similar systems, such as improving the emergent system performance that arises from the interactions of many stochastic components. We develop a domain-independent methodology, using multi-agent simulations as a means of modeling and predicting emergent system behavior across scales and structure-behavior-function repres
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Aprodu, Iuliana, Alberto Redaelli, Franco Maria Montevecchi, and 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.

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The knowledge of the mechanical properties of myosin and actin is of a crucial importance in order to better understand the molecular mechanism of sliding force generation in muscle contraction. The aim of our work was to realize a mechanical characterization of myosin II and actin monomer using the molecular mechanics approach, by assessing the elastic properties of the two proteins, and by establishing the interaction forces between the two monomers of the actomyosin complex, and between myosin’s scissure and adenine nucleotides (ATP and ADP). A restraining method was used in order to modify
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Daniel, J. L., and 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.

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Phosphorylation of platelet myosin is thought to be required for activation of the contractile events occurring during platelet activation. At present the only known mechanism for Onitiating myosin phosphorylation is through a Ca2+-calmodulin-dependent activation of myosin light chain kinase. However, our previous studies using the fluorescent Ca2+-indicator quin2 indicated that both platelet shape change and myosin phosphorylation could be induced in an EGTA-containing media in the absence of a measurable change in cytosolic free Ca2+ concentration (Hallam, Daniel, Kendrick-Jones &amp; Rink.
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Haghshenas-Jaryani, Mahdi, and 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.

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This paper presents a multiscale dynamic model for the simulation and analysis of flexibility in myosin V. A three dimensional (3D) flexible multibody model is developed to mechanically model the biological structure of myosin V. Experimental studies have shown that myosin’s neck domain can be considered as three pairs of tandem elements which can bend at junctures between them. Therefore, each neck is modeled by three rigid bodies connected by flexible spherical joints. One of the most important issues in dynamic modeling of micro-nanoscale sized biological structures, likes DNA and motor pro
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Kostcheeva, O. I., V. Yu Ostchepkova, M. R. Sharipov, D. V. Stchepkin, and 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.

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Nikmaneshi, Mohammad Reza, Bahar Firoozabadi, and 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.

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LE GOFF, L., F. AMBLARD, and 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.

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Bidone, Tamara Carla, Haosu Tang, and 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.

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During fission yeast cytokinesis, actin filaments nucleated by cortical formin Cdc12 are captured by myosin motors bound to a band of cortical nodes. The myosin motors exert forces that pull nodes together into a contractile ring. Cross-linking interactions help align actin filaments and nodes into a single bundle. Mutations in the myosin motor domain and changes in the concentration of cross-linkers alpha-actinin and fimbrin alter the morphology of the condensing network, leading to clumps, rings or extended meshworks. How the contractile tension developing during ring formation depends on th
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Chin, LY, Y. Bosse, PD Pare, and 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.

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Reports on the topic "Myosin A"

1

Sadot, Einat, Christopher Staiger, and Mohamad Abu-Abied. Studies of Novel Cytoskeletal Regulatory Proteins that are Involved in Abiotic Stress Signaling. United States Department of Agriculture, 2011. http://dx.doi.org/10.32747/2011.7592652.bard.

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In the original proposal we planned to focus on two proteins related to the actin cytoskeleton: TCH2, a touch-induced calmodulin-like protein which was found by us to interact with the IQ domain of myosin VIII, ATM1; and ERD10, a dehydrin which was found to associate with actin filaments. As reported previously, no other dehydrins were found to interact with actin filaments. In addition so far we were unsuccessful in confirming the interaction of TCH2 with myosin VIII using other methods. In addition, no other myosin light chain candidates were found in a yeast two hybrid survey. Nevertheless
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Sanders, Luraynne. Cell Adhesion, Signaling and Myosin in Breast Cancer. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada392857.

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Sanders, Luraynne C. Cell Adhesion, Signaling and Myosin in Breast Cancer. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada382496.

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Chew, Teng-Leong. Regulation of Actin-Myosin Cytoskeletal Changes Involved in Cancer Metastasis. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada396798.

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Hofmann, Wilma A. The Role of a Novel Myosin Isoform in Prostate Cancer Metastasis. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada593300.

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Zhang, John Q. Post-Myocardial Infarction and Exercise Training on Myosin Heavy Chain and Cardiac Function. Science Repository, 2019. http://dx.doi.org/10.31487/j.jicoa.2019.01.08.

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Schiefelbein, J. Molecular genetics of myosin motors in Arabidopsis. Final report, July 1, 1992--June 30, 1996. Office of Scientific and Technical Information (OSTI), 1997. http://dx.doi.org/10.2172/486111.

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Staiger, 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), 2022. http://dx.doi.org/10.2172/1840725.

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Gabaix, Xavier, and David Laibson. Myopia and Discounting. National Bureau of Economic Research, 2017. http://dx.doi.org/10.3386/w23254.

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Angeletos, George-Marios, and Zhen Huo. Myopia and Anchoring. National Bureau of Economic Research, 2018. http://dx.doi.org/10.3386/w24545.

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