Academic literature on the topic 'Cytoskeletal proteins'

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Journal articles on the topic "Cytoskeletal proteins"

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Letek, Michal, María Fiuza, Almudena F. Villadangos, Luís M. Mateos, and José A. Gil. "Cytoskeletal Proteins ofActinobacteria." International Journal of Cell Biology 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/905832.

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Although bacteria are considered the simplest life forms, we are now slowly unraveling their cellular complexity. Surprisingly, not only do bacterial cells have a cytoskeleton but also the building blocks are not very different from the cytoskeleton that our own cells use to grow and divide. Nonetheless, despite important advances in our understanding of the basic physiology of certain bacterial models, little is known aboutActinobacteria, an ancient group of Eubacteria. Here we review current knowledge on the cytoskeletal elements required for bacterial cell growth and cell division, focusing
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Albrecht, D. L., and R. J. Noelle. "Membrane Ig-cytoskeletal interactions. I. Flow cytofluorometric and biochemical analysis of membrane IgM-cytoskeletal interactions." Journal of Immunology 141, no. 11 (1988): 3915–22. http://dx.doi.org/10.4049/jimmunol.141.11.3915.

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Abstract Membrane IgM (mIgM) and mIgD are the receptors for Ag on the surface of B lymphocytes, mIg is soluble in detergent; however, when mIg is cross-linked with anti-Ig, the mIg becomes associated with the cytoskeletal matrix and is rendered detergent-insoluble. By a novel flow cytofluorometric assay and by biochemical analysis, it has been shown that anti-isotype-specific antibodies induce mIgM and mIgD to associate with the cytoskeleton of B lymphocytes in an isotype-specific fashion. The detergent solubility of other prominent B lymphocyte surface proteins, such as class I and class II M
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Miura, Tetsuji. "Cytoskeletal Proteins." Circulation Journal 74, no. 11 (2010): 2295–96. http://dx.doi.org/10.1253/circj.cj-10-0935.

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Dvořáková, Kateřina, Harry D. M. Moore, Nataša Šebková, and Jiří Paleček. "Cytoskeleton localization in the sperm head prior to fertilization." Reproduction 130, no. 1 (2005): 61–69. http://dx.doi.org/10.1530/rep.1.00549.

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Three major cytoskeletal proteins, actin, tubulin and spectrin, are present in the head of mammalian spermatozoa. Although cytoskeletal proteins are implicated in the regulation of capacitation and the acrosome reaction (AR), their exact role remains poorly understood. The aim of this study was to compare the distribution of the sperm head cytoskeleton before and after the AR in spermatozoa representing a range of acrosome size and shape. Spermatozoa from the human and three rodents (rat, hamster and grey squirrel) were fixed before and after the AR in appropriate mediumin vitro. Indirect immu
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Paradžik, Tina, Iva I. Podgorski, Tanja Vojvoda Zeljko, and Mladen Paradžik. "Ancient Origins of Cytoskeletal Crosstalk: Spectraplakin-like Proteins Precede the Emergence of Cortical Microtubule Stabilization Complexes as Crosslinkers." International Journal of Molecular Sciences 23, no. 10 (2022): 5594. http://dx.doi.org/10.3390/ijms23105594.

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Adhesion between cells and the extracellular matrix (ECM) is one of the prerequisites for multicellularity, motility, and tissue specialization. Focal adhesions (FAs) are defined as protein complexes that mediate signals from the ECM to major components of the cytoskeleton (microtubules, actin, and intermediate filaments), and their mutual communication determines a variety of cellular processes. In this study, human cytoskeletal crosstalk proteins were identified by comparing datasets with experimentally determined cytoskeletal proteins. The spectraplakin dystonin was the only protein found i
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Chifflet, Silvia, and Julio A. Hernández. "The Plasma Membrane Potential and the Organization of the Actin Cytoskeleton of Epithelial Cells." International Journal of Cell Biology 2012 (2012): 1–13. http://dx.doi.org/10.1155/2012/121424.

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The establishment and maintenance of the polarized epithelial phenotype require a characteristic organization of the cytoskeletal components. There are many cellular effectors involved in the regulation of the cytoskeleton of epithelial cells. Recently, modifications in the plasma membrane potential (PMP) have been suggested to participate in the modulation of the cytoskeletal organization of epithelia. Here, we review evidence showing that changes in the PMP of diverse epithelial cells promote characteristic modifications in the cytoskeletal organization, with a focus on the actin cytoskeleto
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Fox, Joan. "Cytoskeletal Proteins and Platelet Signaling." Thrombosis and Haemostasis 86, no. 07 (2001): 198–213. http://dx.doi.org/10.1055/s-0037-1616218.

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SummaryThe actin filament network fills the cytoplasm of unstimulated platelets and connects with a submembranous latticework of short cross-linked actin filaments, known as the membrane skeleton. One function of the cytoskeleton is to direct the contours of the membrane in the unstimulated platelet and the rapid changes in shape in the activated platelet. Activation-induced changes result from events such as phosphorylation or calpain-induced cleavage of cytoskeletal proteins. The specific reorganizations depend upon the combination of signals to which platelets are exposed. A second function
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Chinthalapudi, Krishna, Erumbi Rangarajan, Dipak Patil, and Tina Izard. "Lipid-directed cytoskeletal protein oligomerization at sites of cell adhesion." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1833. http://dx.doi.org/10.1107/s2053273314081674.

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Vertebrate cell growth, division, migration, morphogenesis, and development, rely on the dynamic interactions of cells with components the extracellular matrix (ECM) via cell surface complexes. These focal adhesions (FAs) are comprised of integrin receptors, associated signaling molecules, and talin, which is required for "inside-out" signaling that stabilizes contacts of integrin receptors with the ECM by linking FAs to the actin cytoskeleton by binding to vinculin. The highly dynamic interactions with the actin cytoskeleton are also essential for the formation of membrane protrusions (lamell
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Ong, Mei Shan, Shuo Deng, Clarissa Esmeralda Halim, et al. "Cytoskeletal Proteins in Cancer and Intracellular Stress: A Therapeutic Perspective." Cancers 12, no. 1 (2020): 238. http://dx.doi.org/10.3390/cancers12010238.

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Cytoskeletal proteins, which consist of different sub-families of proteins including microtubules, actin and intermediate filaments, are essential for survival and cellular processes in both normal as well as cancer cells. However, in cancer cells, these mechanisms can be altered to promote tumour development and progression, whereby the functions of cytoskeletal proteins are co-opted to facilitate increased migrative and invasive capabilities, proliferation, as well as resistance to cellular and environmental stresses. Herein, we discuss the cytoskeletal responses to important intracellular s
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Perry, G., D. A. Zelasko, L. M. Sayre, and M. A. Smith. "Oxidative Damage to Axonal Cytoskeletal Proteins." Microscopy and Microanalysis 3, S2 (1997): 43–44. http://dx.doi.org/10.1017/s1431927600007108.

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Proteins of the axonal cytoskeleton, particularly neurofilament and microtubule-associated protein τ, should be particularly sensitive to the effects of oxidative modification due to their high content of lysine, an amino acid that is particularly susceptible to direct oxidization as well as adduction by carbonyls produced from lipid and sugar oxidation. To understand the susceptibility of the cytoskeleton to oxidative modification and whether such modification is related to the physiological function of the cytoskeleton, we undertook a cytological analysis of motor neurons isolated from mouse
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Dissertations / Theses on the topic "Cytoskeletal proteins"

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Liu, Gang. "Cytoskeletal proteins of Dictyostelium." Thesis, University of Oxford, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.292634.

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Baisden, Joseph M. "AFAP-110 is a cSrc activator." Morgantown, W. Va. : [West Virginia University Libraries], 2003. http://etd.wvu.edu/templates/showETD.cfm?recnum=2766.

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Thesis (Ph. D.)--West Virginia University, 2003.<br>Title from document title page. Document formatted into pages; contains v, 149 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
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Alwash, Ban Hussein Kadhim. "S100 proteins control cytoskeletal dynamics in cancer." Thesis, University of Leicester, 2018. http://hdl.handle.net/2381/42867.

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The S100 family of calcium binding proteins exhibits a unique pattern of cell type specific expression. These proteins are found in the cytoplasm and/or nucleus of a variety of cells, and involved in the control of a wide range of cellular processes such as cell cycle progression and differentiation. S100A4 and S100A6 are members of the S100 protein family that interact with several molecular targets including the heavy chain of non-muscle myosin IIA (NM IIA) and annexin II, respectively. NM IIA is a major actin-associated motor protein, which is involved in cell motility and cytokinesis. Asse
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Snyder, Heidi Ghent. "Fiber type-specific desmin content in human single muscle fibers /." Diss., CLICK HERE for online access, 2006. http://contentdm.lib.byu.edu/ETD/image/etd1253.pdf.

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McCarthy, David James. "Analysis of the novel Lyn-associated cytoskeletal modular protein, LACM." University of Western Australia. School of Medicine and Pharmacology, 2009. http://theses.library.uwa.edu.au/adt-WU2009.0180.

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A yeast-two hybrid screen with Lyn identified a novel 130 kDa multidomain protein with a 36% identity to Actin Filament Associated Protein (AFAP) 110 and similar domains, including PH domains, potential sites of tyrosine and serine/threonine phosphorylation, a leucine-zipper domain, a potential actin binding site and multimerization site. AFAP110 has been shown to have a role in modulating actin filament integrity and induce lamellipodia formation, and is known to interact with Src family kinases. The aim of this thesis was to characterize this novel protein named Lyn-Associated Cytoskeletal M
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MacDonald, Louisa M. "Characterisation of the benzimidazole-binding site on the cytoskeletal protein tubulin." Thesis, MacDonald, Louisa M. (2003) Characterisation of the benzimidazole-binding site on the cytoskeletal protein tubulin. PhD thesis, Murdoch University, 2003. https://researchrepository.murdoch.edu.au/id/eprint/173/.

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The binding kinetics of several benzimidazole compounds were determined with recombinant tubulin monomers and heterodimers from benzimidazole-sensitive and -insensitive organisms. This study utilised the naturally occurring high efficacy of the benzimdazoles for the parasitic protozoa Giardia duodenalis and Encephalitozoon intestinalis. The benzimidazoles are not active against the protozoan Cryptosporidium parvum or mammalian hosts, including humans. The affinity of several benzimidazole derivatives for monomeric and heterodimeric beta-tubulin was clearly demonstrated, thus supporting previou
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MacDonald, Louisa M. "Characterisation of the benzimidazole-binding site on the cytoskeletal protein tubulin." Murdoch University, 2003. http://wwwlib.murdoch.edu.au/adt/browse/view/adt-MU20050107.94048.

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The binding kinetics of several benzimidazole compounds were determined with recombinant tubulin monomers and heterodimers from benzimidazole-sensitive and -insensitive organisms. This study utilised the naturally occurring high efficacy of the benzimdazoles for the parasitic protozoa Giardia duodenalis and Encephalitozoon intestinalis. The benzimidazoles are not active against the protozoan Cryptosporidium parvum or mammalian hosts, including humans. The affinity of several benzimidazole derivatives for monomeric and heterodimeric â-tubulin was clearly demonstrated, thus supporting previous s
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Ritchie, Sian. "Identification of cytoskeletal proteins as substrates for Ca'2'+ dependent protein kinase." Thesis, University of Reading, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.240317.

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Höng, J. "Investigating the structures of evolutionarily conserved cytoskeletal proteins." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.604097.

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The parasitic protist <i>Giardia intestinalis, </i>considered to be one of the most ancient eukaryotic organisms, contains a typical eukaryotic cytoskeleton composed of microtubules (αβ-tubulin), microfilaments (actin) and intermediate filaments. Proteins associated with the microtubules include kinesins and additional members of the tubulin superfamily. δ-Tubulin is a member of the tubulin superfamily. The methylotropic yeast <i>P. pastoris </i>was identified as the most suitable host for recombinant expression of <i>G. intestinalis </i>δ-tubulin. High-resolution crystal structures of <i>G. i
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Holmes, Fiona Elizabeth. "A study of cytoskeletal proteins in the neuron." Thesis, University of Kent, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.242927.

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Books on the topic "Cytoskeletal proteins"

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Thomas, Kreis, and Vale Ronald, eds. Guidebook to the cytoskeletal and motor proteins. Oxford University Press, 1993.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. Hydrogels of Cytoskeletal Proteins. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8.

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Aebi, Ueli, and Jürgen Engel, eds. Cytoskeletal and Extracellular Proteins. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73925-5.

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M, Osborn, Weber Klaus Dr Prof, and Banbury Center, eds. Cytoskeletal proteins in tumor diagnosis. Cold Spring Harbor Laboratory, 1989.

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W, Cunningham Leon, ed. Structural and contractile proteins. Academic Press, 1987.

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C, Froehner Stanley, and Bennett Vann, eds. Cytoskeletal regulation of membrane function. Rockefeller University Press, 1997.

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Akademie der Wissenschaften und der Literatur (Germany) International Symposium. Nature and function of cytoskeletal proteins in motility and transport: International Symposium of the Akademie der Wissenschaften und der Literatur, Mainz, October 9th-11th, 1986. Fischer, 1987.

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B, Vallee Richard, ed. Structural and contractile proteins. Academic Press, 1986.

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Society of General Physiologists. Symposium. Cytoskeletal regulation of membrane function: Society of General Physiologists 50th annual symposium, Marine Biological Laboratory, Woods Hole, Massachusetts, 5-7 September 1996. Rockefeller University Press, 1997.

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Ph, Jeanteur, ed. Cytoskeleton and small G proteins. Springer, 1999.

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Book chapters on the topic "Cytoskeletal proteins"

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Why Cytoskeletal Gel?" In Hydrogels of Cytoskeletal Proteins. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_2.

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Isenberg, Gerhard. "Plasmamembrane and Organelle-Associated Cytoskeletal Proteins." In Cytoskeleton Proteins. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79632-6_12.

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Quinlan, Roy. "Cytoskeletal Competence Requires Protein Chaperones." In Small Stress Proteins. Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-56348-5_12.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Why Polymer Gel?" In Hydrogels of Cytoskeletal Proteins. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_1.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Actin Gel." In Hydrogels of Cytoskeletal Proteins. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_3.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Microtubule Gel." In Hydrogels of Cytoskeletal Proteins. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_4.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Tropomyosin Gel." In Hydrogels of Cytoskeletal Proteins. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_5.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Summary of the MHSMG." In Hydrogels of Cytoskeletal Proteins. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_6.

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Osada, Yoshihito, Ryuzo Kawamura, and Ken-Ichi Sano. "Biomimetic Functions of Synthetic Polymer Gels." In Hydrogels of Cytoskeletal Proteins. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-27377-8_7.

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Bershadsky, Alexander D., and Juri M. Vasiliev. "Regulation of Synthesis of Cytoskeletal Proteins." In Cytoskeleton. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5278-5_7.

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Conference papers on the topic "Cytoskeletal proteins"

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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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Allen, Kathleen B., and Bradley Layton. "A Mechanical Model for Cytoskeleton and Membrane Interactions in Neuronal Growth Cones." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-42008.

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Revealing the molecular events of neuronal growth is critical to obtaining a deeper understanding of nervous system development, neural injury response, and neural tissue engineering. Central to this is the need to understand the mechanical interactions among the cytoskeleton and the cell membrane, and how these interactions affect the overall growth mechanics of neurons. Using ANSYS, the force produced by a cytoskeletal protein acting against a deformable membrane was modeled, and the deformation, stress, and strain were computed for the membrane. Parameters to represent the flexural rigiditi
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Pryse, Kenneth M., Teresa M. Abney, Guy M. Genin, and Elliot L. Elson. "Probing Cytoskeletal Mechanics Using Biochemical Inhibitors." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19451.

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Quantifying the mechanics of the cytoskeletons of living cells is important for understanding several physiologic and pathologic cellular functions, such as wound healing and cellular migration in cancer. Our laboratory develops three-dimensional tissue constructs for assaying cytoskeletal mechanics in controlled conditions. These tissue constructs consist of defined components such as chick embryo fibroblasts and reconstituted rat tail collagen; fibroblasts remodel the collagen extracellular matrix (ECM) and develop a structural environment representative of that which would exist in a natura
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Kaazempur-Mofrad, Mohammad R., Peter J. Mack, Helene Karcher, Javad Golji, and Roger G. Kamm. "Stress-Induced Mechanotransduction: Some Preliminaries." In ASME 2003 International Mechanical Engineering Congress and Exposition. ASMEDC, 2003. http://dx.doi.org/10.1115/imece2003-43215.

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Mechanical stimuli affect nearly every aspect of cellular function, yet the underlying mechanisms of transduction of force into biochemical signals are not clearly understood. One hypothesis is that forces transmitted via individual proteins, either at the site of cell adhesion to its surroundings or within the stress-bearing members of the cytoskeleton, cause conformational changes that change their binding affinity to other intracellular molecules. This altered equilibrium state can subsequently initiate biochemical signaling cascades of produce immediate structural changes. This paper addre
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Bathe, Mark, Claus Heussinger, Mireille Claessens, Andreas Bausch, and Erwin Frey. "Cytoskeletal Bundle Mechanics." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176170.

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Filamentous actin (F-actin) is a stiff biopolymer that is tightly crosslinked in vivo by actin-binding proteins (ABPs) to form stiff bundles that form major constituents of a multitude of slender cytoskeletal processes including stereocilia, filopodia, microvilli, neurosensory bristles, cytoskeletal stress fibers, and the acrosomal process of sperm cells (Fig. 1). The mechanical properties of these cytoskeletal processes play key roles in a broad range of cellular functions — the bending stiffness of stereocilia mediates the mechanochemical transduction of mechanical stimuli such as acoustic w
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verhallen, P. F. J., E. M. Bevers, P. Comfurius, W. M. A. Linkskens, and R. F. A. Zwaal. "CALPAIN-MEDIATED CYTOSKELETAL DEGRADATION CORRELATES WITH STIMULATION OF PLATELET PROCOAGULANT ACTIVITY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642821.

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We have shown earlier that the negatively charged phospholipid phosphatidylserine (PS), which becomes translocated from the inner surface to the outer surface of the plasma membrane upon platelet activation, is responsible for platelet procoagulant activity. Studies with erythrocytes have suggested a role for cytoskeletal proteins in the regulation of transmembrane asymmetry of PS. The possibility that platelet cytoskeletal proteins are involved in the loss of transmembrane asymmetry of PS, was explored by correlative investigations of both platelet prooagulant activity and activity of calpain
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Ronan, William, Vikram S. Deshpande, Robert M. McMeeking, and J. Patrick McGarry. "Simulation of Stress Fiber Remodeling and Mixed-Mode Focal Adhesion Assembly During Cell Spreading and for Cells Adhered to Elastic Substrates." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53878.

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Cell spreading is governed by two cooperative cellular processes: the association of binding proteins to form focal adhesions, and the active remodeling of the actin cytoskeleton as the cell spreads [1]. The interaction between these two processes is poorly understood, and previous computational models have only examined each process in isolation. Previous studies have established that cells possess the ability to sense and react to their physical environment, for example cells seeded on substrates of varying stiffness exhibit a different cytoskeletal response [2,3].
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Dangaria, Jhanvi H., and Peter J. Butler. "Interaction of Shear Stress, Myosin II, and Actin in Dynamic Modulation of Endothelial Cell Microrheology." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192947.

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The endothelial cell (EC) cytoskeleton mediates several biological functions such as adhesion, migration, phagocytosis, cell division, and mechanosensitivity. These functions are carried out in part through dynamic cytoskeletal polymerization, modulation of crosslinking, and development of tension between intracellular organelles and the extracellular matrix via focal adhesion plaques. One important component of the cytoskeleton is actin which polymerizes into filaments and is thought to be prestressed by virtue of crosslinking proteins such as α-actinin, filamin and myosin II molecular motors
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Anders, Katie L., Kylie B. R. Belchamber, Peter J. Barnes, and Louise E. Donnelly. "Differential phosphorylation patterns of macrophage cytoskeletal proteins in COPD following phagocytosis." In ERS International Congress 2019 abstracts. European Respiratory Society, 2019. http://dx.doi.org/10.1183/13993003.congress-2019.pa1671.

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Wilkinson, J. M., N. Hack, L. I. Thorsen, and J. A. Thomas. "MONOCLONAL ANTIBODIES RECOGNISING PROTEINS OF THE OUTER AND INNER SURFACE OF THE PLATELET PLASMA MEMBRANE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644493.

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Platelet membrane preparations can be fractionated into two major subpopulations by free flow electrophoresis and these have been shown to correspond to the plasma membrane and the endoplasmic reticulum of the platelet. The plasma membrane fraction can be shown, by two-dimensional electrophoresis, to contain the major surface glycoproteins together with considerable amounts of actin and actin-associated proteins such as the 250 kDa actin-binding protein (filamin), P235 (talin), myosin, α-actinin and tropomyosin (Hack, N. … Crawford, N., Biochem. J. 222, 235 (1984). These cytoskeletal proteins
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Reports on the topic "Cytoskeletal proteins"

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Sadot, Einat, Christopher Staiger, and Zvi Kam Weizmann. functional genomic screen for new plant cytoskeletal proteins and the determination of their role in actin mediated functions and guard cells regulation. United States Department of Agriculture, 2003. http://dx.doi.org/10.32747/2003.7587725.bard.

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The original objectives of the approved proposal were: 1. To construct a YFP fused Arabidopsis cDNA library in a mammalian expression vector. 2. To infect the library into a host fibroblast cell line and to screen for new cytoskeletal associated proteins using an automated microscope. 3. Isolate the new genes. 4. Characterize their role in plants. The project was approved as a feasibility study to allow proof of concept that would entail building the YFP library and picking up a couple of positive clones using the fluorescent screen. We report here on the construction of the YFP library, the d
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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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Epel, Bernard, and Roger Beachy. Mechanisms of intra- and intercellular targeting and movement of tobacco mosaic virus. United States Department of Agriculture, 2005. http://dx.doi.org/10.32747/2005.7695874.bard.

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To cause disease, plant viruses must replicate and spread locally and systemically within the host. Cell-to-cell virus spread is mediated by virus-encoded movement proteins (MPs), which modify the structure and function of plasmodesmata (Pd), trans-wall co-axial membranous tunnels that interconnect the cytoplasm of neighboring cells. Tobacco mosaic virus (TMV) employ a single MP for cell- cell spread and for which CP is not required. The PIs, Beachy (USA) and Epel (Israel) and co-workers, developed new tools and approaches for study of the mechanism of spread of TMV that lead to a partial iden
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Zilberstein, Aviah, Bo Liu, and Einat Sadot. Studying the Involvement of the Linker Protein CWLP and its Homologue in Cytoskeleton-plasma Membrane-cell Wall Continuum and in Drought Tolerance. United States Department of Agriculture, 2012. http://dx.doi.org/10.32747/2012.7593387.bard.

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The study has been focused on proline-rich proteins from the HyPRP family. Three proline-rich proteins have been characterized with the CWLP as the main objective. We showed that this unique protein is assembled in the plasma membrane (PM) and forms a continuum between the cell wall (CW) and cytosol via the PM. While spanning the PM, it is arranged in lipid rafts as CWLP-aquaporin complexes that recruit PP2A-β”, as a part of PP2A enzyme, close to the aquaporin moiety where it dephosphorylates two crucial Ser residues and induces closure of the aquaporin water channels. The closure of water cha
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Ramesh, Vijaya. Neurofibromatosis 2 Tumor Suppressor Protein, Merlin, in Cellular Signaling to Actin Cytoskeleton. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada395581.

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Woloschak, G. E., P. Felcher, and Chin-Mei Chang-Liu. Expression of cytoskeletal and matrix genes following exposure to ionizing radiation: Dose-rate effects and protein synthesis requirements. Office of Scientific and Technical Information (OSTI), 1994. http://dx.doi.org/10.2172/10148882.

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Woloschak, G. E., P. Felcher, and Chin-Mei Chang-Liu. Expression of cytoskeletal and matrix genes following exposure to ionizing radiation: Dose-rate effects and protein synthesis requirements. Office of Scientific and Technical Information (OSTI), 1995. http://dx.doi.org/10.2172/70715.

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Woloschak, G. E., P. Felcher, and Chin-Mei Chang-Liu. Expression of cytoskeletal and matrix genes following exposure to ionizing radiation: Dose-rate effects and protein synthesis requirements. Office of Scientific and Technical Information (OSTI), 1992. http://dx.doi.org/10.2172/10185724.

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Woloschak, G. E., P. Felcher, and Chin-Mei Chang-Liu. Expression of cytoskeletal and matrix genes following exposure to ionizing radiation: Dose-rate effects and protein synthesis requirements. Office of Scientific and Technical Information (OSTI), 1993. http://dx.doi.org/10.2172/10130291.

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Philosoph-Hadas, Sonia, Peter Kaufman, Shimon Meir, and Abraham Halevy. Signal Transduction Pathway of Hormonal Action in Control and Regulation of the Gravitropic Response of Cut Flowering Stems during Storage and Transport. United States Department of Agriculture, 1999. http://dx.doi.org/10.32747/1999.7695838.bard.

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Original objectives: The basic goal of the present project was to increase our understanding of the cellular mechanisms operating during the gravitropic response of cut flowers, for solving their bending problem without affecting flower quality. Thus, several elements operating at the 3 levels o the gravity-induced signal transduction pathway, were proposed to be examined in snapdragon stems according to the following research goals: 1) Signaling: characterize the signal transduction pathway leading to the gravitropic response, regarding the involvement of [Ca2+]cyt as a mediator of IAA moveme
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