Academic literature on the topic 'Binding actif'

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Journal articles on the topic "Binding actif"

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Arias, Paloma, Miguel A. Fernández-Moreno, and Francisco Malpartida. "Characterization of the Pathway-Specific Positive Transcriptional Regulator for Actinorhodin Biosynthesis inStreptomyces coelicolor A3(2) as a DNA-Binding Protein." Journal of Bacteriology 181, no. 22 (1999): 6958–68. http://dx.doi.org/10.1128/jb.181.22.6958-6968.1999.

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ABSTRACT The ActII-ORF4 protein has been characterized as a DNA-binding protein that positively regulates the transcription of the actinorhodin biosynthetic genes. The target regions for the ActII-ORF4 protein were located within the act cluster. These regions, at high copy number, generate a nonproducer strain by in vivo titration of the regulator. The mutant phenotype could be made to revert with extra copies of the wild-type actII-ORF4 gene but not with theactII-ORF4-177 mutant. His-tagged recombinant wild-type ActII-ORF4 and mutant ActII-ORF4-177 proteins were purified fromEscherichia coli
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Pollard, Thomas D. "Actin and Actin-Binding Proteins." Cold Spring Harbor Perspectives in Biology 8, no. 8 (2016): a018226. http://dx.doi.org/10.1101/cshperspect.a018226.

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Ampe, Christophe, and Joël Vandekerckhove. "Actin-actin binding protein interfaces." Seminars in Cell Biology 5, no. 3 (1994): 175–82. http://dx.doi.org/10.1006/scel.1994.1022.

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Kozuka, Jun, Yoshiharu Ishii, and Toshio Yanagida. "2P130 Dynamic cooperative binding of myosin V on actin filament(Molecular motors,Poster Presentations)." Seibutsu Butsuri 47, supplement (2007): S145. http://dx.doi.org/10.2142/biophys.47.s145_3.

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Gross, Stephane R. "Actin binding proteins." Cell Adhesion & Migration 7, no. 2 (2013): 199–213. http://dx.doi.org/10.4161/cam.23176.

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Winder, S. J. "Actin-binding proteins." Journal of Cell Science 118, no. 4 (2005): 651–54. http://dx.doi.org/10.1242/jcs.01670.

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Vandekerckhove, J. "Actin-binding proteins." Current Opinion in Cell Biology 2, no. 1 (1990): 41–50. http://dx.doi.org/10.1016/s0955-0674(05)80029-8.

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Hartwig, John H., and David J. Kwiatkowski. "Actin-binding proteins." Current Opinion in Cell Biology 3, no. 1 (1991): 87–97. http://dx.doi.org/10.1016/0955-0674(91)90170-4.

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Winder, S. J., L. Hemmings, S. K. Maciver, et al. "Utrophin actin binding domain: analysis of actin binding and cellular targeting." Journal of Cell Science 108, no. 1 (1995): 63–71. http://dx.doi.org/10.1242/jcs.108.1.63.

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Utrophin, or dystrophin-related protein, is an autosomal homologue of dystrophin. The protein is apparently ubiquitously expressed and in muscle tissues the expression is developmentally regulated. Since utrophin has a similar domain structure to dystrophin it has been suggested that it could substitute for dystrophin in dystrophic muscle. Like dystrophin, utrophin has been shown to be associated with a membrane-bound glycoprotein complex. Here we demonstrate that expressed regions of the predicted actin binding domain in the NH2 terminus of utrophin are able to bind to F-actin in vitro, but d
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Drubin, David G. "Actin and actin-binding proteins in yeast." Cell Motility and the Cytoskeleton 15, no. 1 (1990): 7–11. http://dx.doi.org/10.1002/cm.970150103.

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Dissertations / Theses on the topic "Binding actif"

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Popescu, Razvan Alexandru. "Dynamique Moléculaire de la petite molécule au biopolymère : une Porphyrine modèle du site actif des hémoprotéines et une Calciprotéine, la Nereis diversicolor Sarcoplasmic calcium binding protein." Paris 6, 2004. http://www.theses.fr/2004PA066270.

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DEBAECKER-PETIT, NOELE. "Proteines a site actif binucleaire a fer non heminique ou a manganese et analogues synthetiques : correlations magneto-structurales." Université Joseph Fourier (Grenoble), 1996. http://www.theses.fr/1996GRE10108.

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La realisation de mesures d'aimantation a saturation est, dans le cas des proteines a site actif binucleaire a fer non heminique ou a manganese, source d'informations structurales. En effet, de telles mesures permettent de determiner l'interaction d'echange j entre les ions du site actif, parametre qui est correle avec la nature des ligands pontant le site. Au cours de ce travail, nous decrivons tout d'abord le protocole a suivre pour realiser de telles mesures. Nous appliquons ensuite ce protocole a deux proteines a site actif binucleaire a fer non heminique: la ribonucleotide reductase de so
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Wang, Hui. "Structural studies of actin and actin-binding proteins." Thesis, University of British Columbia, 2009. http://hdl.handle.net/2429/10916.

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Actin is involved in cell movement, maintaining cell shape and anchoring cytoskeletal proteins. These functions are regulated by many actin-binding proteins, including those of the gelsolin superfamily. Gelsolin superfamily members regulate actin organization by severing, capping F-actin, nucleating the formation of F-actin and/or bundling F-actin. Although abundant structures are available for gelsolin and gelsolin fragments in complexes with actin, the detailed mechanisms for gelsolin activation, and for gelsolin severing and capping of F-actin are still unknown. Structures for gelsolin fami
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Hull, Richard Alan. "Actin and actin-binding proteins in higher plants." Thesis, University of Oxford, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.279874.

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Scoville, Damon Charles. "Filament dynamics and actin binding factors." Diss., Restricted to subscribing institutions, 2008. http://proquest.umi.com/pqdweb?did=1693066541&sid=1&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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Heisler, David Bruce. "Role of Actin and Actin-binding Proteins in the Pathogenesis of Actin-targeting Bacterial Toxins." The Ohio State University, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=osu1501519777175964.

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Hsu, C. R. "Characterisation of a Salmonella actin-binding protein." Thesis, University of Cambridge, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.604683.

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<i>Salmonella</i> invasion protein C (SipC) and SipA bind actin directly. SipC inserts into the host cell plasma membrane from where it promotes effector delivery and is essential for <i>Salmonella</i> invasion. SipC-C (residues 200-409) directly nucleates actin polymerisation <i>in vitro</i> and induces cytoskeletal rearrangements at the leading edge when expressed in cells. By analysis a panel of SipC-C derivatives in transfected cells, a region spanning residues 377-409 was defined as necessary for actin reorganisation and leading-edge localisation. Residues 377-409 were sufficient to local
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Schmitz, Stephan. "Mutational analysis of proposed myosin binding sites on actin." Thesis, University of York, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.301148.

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Kuhlman, Philip Alan. "Characterisation of the actin-binding site of α-actinin". Thesis, University of Leicester, 1993. http://hdl.handle.net/2381/35270.

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The alpha-actinin residues involved in the interaction of chicken smooth muscle alpha-actinin with F-actin were defined by co-sedimentation. Residues 120 to 140 of alpha-actinin were identified as essential with residues 141 to 159 and 1 to 107 contributing to the interaction. Temperature dependent binding and the lack of inhibition by high salt concentrations implicated hydrophobic interactions in the binding mechanism. Further characterisation of the binding interaction using stopped-flow techniques determined a K for the interaction of 0.82 muM at 15°C and 2.38 muM at 25°C. These techniques
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Moores, Carolyn Ann. "Structure-function analysis of the utrophin actin binding domain." Thesis, University of Cambridge, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.624459.

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Books on the topic "Binding actif"

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Lappalainen, Pekka. Actin-Monomer-Binding Proteins. Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-46407-7.

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Remedios, Cristobal G. Molecular Interactions of Actin: Actin Structure and Actin-Binding Proteins. Springer Berlin Heidelberg, 2001.

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dos Remedios, Cristobal G., and Deepak Chhabra, eds. Actin-Binding Proteins and Disease. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-71749-4.

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Hartwig, John H. Actin-binding proteins 1: Spectrin superfamily. Academic Press, 1994.

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Hartwig, John H. Actin-binding proteins 1: spectrin superfamily. Academic Press, 1995.

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Hartwig, John H. Actin-binding proteins 1: spectrin superfamily. Academic Press, 1994.

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Danielle, Pansu, Bronner Felix, and North Atlantic Treaty Organization. Scientific Affairs Division., eds. Calcium transport and intracellular calcium homeostasis. Springer-Verlag, 1990.

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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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Taylor, Catherine Yvonne. Analysis of protein binding motifs in the nucleotide sequence of the human [gamma]-actin gene promoter. National Library of Canada = Bibliothèque nationale du Canada, 1993.

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Malapitan, Irish Ann. Mapping an F-actin and cytoskeletal binding region in the basic domain of the mouse LSP1 protein. National Library of Canada, 1994.

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Book chapters on the topic "Binding actif"

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Carlier, Marie-France, Dominique Pantaloni, Stéphane Romero, and Christophe Le Clainche. "How Actin Assembly Is Modulated at Filament Barbed Ends in Motile Processes." In Actin-Monomer-Binding Proteins. Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-46407-7_1.

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Van Troys, Marleen, Stien Dhaese, Joël Vandekerckhove, and Christophe Ampe. "Multirepeat β-Thymosins." In Actin-Monomer-Binding Proteins. Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-46407-7_7.

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Sparrow, John C., and Nigel G. Laing. "Actin Genetic Diseases." In Actin-Binding Proteins and Disease. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-71749-4_2.

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Mackay, Ian R., Roberto Martinez-Neira, Senga Whittingham, Dan Nicolau, and Ban-Hock Toh. "Autoantigenicity of Actin." In Actin-Binding Proteins and Disease. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-71749-4_4.

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Chhabra, Deepak, and Cristobal G. dos Remedios. "Actin: An Overview of Its Structure and Function." In Actin-Binding Proteins and Disease. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-71749-4_1.

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Van Troys, Marleen, Joël Vandekerckhove, and Christophe Ampe. "Actin and Actin-Binding Proteins in Cancer Progression and Metastasis." In Actin-Binding Proteins and Disease. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-71749-4_10.

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Nunoi, Hiroyuki. "Diseases with Abnormal Actin and Actin-Binding Proteins in Leukocyte and Nonmuscle Cells." In Actin-Binding Proteins and Disease. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-71749-4_11.

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dos Remedios, C. G., and Neil J. Nosworthy. "The Role of PIP2 in Actin, Actin-Binding Proteins and Disease." In Actin-Binding Proteins and Disease. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-71749-4_12.

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Bearer, E. L. "Intracellular Pathogens and the Actin Cytoskeleton." In Actin-Binding Proteins and Disease. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-71749-4_13.

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Stefani, Maurizio, Masako Tsubakihara, Brett D. Hambly, et al. "Actin and Its Binding Proteins in Heart Failure." In Actin-Binding Proteins and Disease. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-71749-4_14.

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Conference papers on the topic "Binding actif"

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Chaudhuri, Ovijit, Sapun H. Parekh, Allen Liu, and Daniel A. Fletcher. "Viscoelasticity of Growing Actin Networks." In ASME 2004 International Mechanical Engineering Congress and Exposition. ASMEDC, 2004. http://dx.doi.org/10.1115/imece2004-60076.

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Actin self-assembles to form filaments that can organize into dendritic networks through interactions with various actin binding proteins. Growing actin filament networks produce significant mechanical forces that play a key role in many dynamic cellular processes such as motility, cytokinesis, and phagocytosis. We investigated the mechanical properties of growing actin networks with atomic force microscopy and found the actin networks to behave as viscoelastic solids.
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Bidone, Tamara C., Marco A. Deriu, Giacomo Di Benedetto, Diana Massai, and Umberto Morbiducci. "Insights Into the Molecular Mechanisms of Actin Dynamics: A Multiscale Modeling Approach." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53417.

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Actin dynamics, which is at the basis of many fundamental cellular processes as cell migration [1], is governed by the self-assembly and disassembly of actin monomers (G-actin) that, in turn, are determined by the kinetics of ATP hydrolysis and by the local concentrations of Mg2+ and Ca2+ [2]. During cell migration, interactions of the actin filaments (F-actin) with different nucleotide-cation complexes induce local topological rearrangements, because the filament building G-actins undergo conformational shifts between multiple equilibrium states separated by low-energy barriers. For example,
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Boyles, J. K., JE B. Fox, and M. C. Berndt. "THE DISTRIBUTION OF GP lb AND THE STABILITY OF THE PLASMA MEMBRANE ARE DEPENDENT UPON AN INTACT MEMBRANE SKELETON." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643626.

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Platelets are know to have a cytoskeleton of actin filaments. We have presented evidence that they also have a membrane skeleton linked to the cytoskeletal filaments and that the membrane skeleton is linked to GP Ib-IX on the plasma membrane via actin-binding protein. In the current study, electron microscopy of thick (0.2 ym) epoxy sections was used to identify the distribution of GP lb. After various treatments, platelets were fixed and incubated with affinity-purified GP lb antibody and colloidal gold-labeled Protein-A. The entire cell surface was covered with a network of short intersectin
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Chou, Szu-Yuan, Chao-Min Cheng, Yi-Wen Lin, Chih-Cheng Chen, and Philip R. LeDuc. "Effects of Mechanical Strain on Structural and Actin-Binding Proteins in Neuroblasts." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-204747.

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Mechanical stimulation affects the functioning and outgrowth of neurons and has the potential capacity for regeneration. Mechanoreceptors in sensory neurons act as a conduit to respond to pain and touch while neurites experience mechanical stimulation during the process of animal growth. To understand mechanotransduction in neural outgrowth, we used a custom fabricated device to investigate the effects of static mechanical stretching while examining molecular connections such as advillin and actin. Our results have the potential of providing greater understanding of mechanotransduction in neur
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Capitanio, Marco, Lucia Gardini, and Francesco Saverio Pavone. "Ultra-fast optical manipulation of single proteins binding to the actin cytoskeleton." In SPIE BiOS, edited by Kirill V. Larin and David D. Sampson. SPIE, 2014. http://dx.doi.org/10.1117/12.2039219.

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Golji, Javad, and Mohammad R. K. Mofrad. "Focal Adhesion Mechanotransduction: Molecular Events Leading to Vinculin Activation." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19711.

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Focal adhesions are formed as a molecular glue linking cytoskeletal actin filaments to the extracellular matrix (ECM). They are formed at the site of mechanical stimulation (1) and involve and initial recruitment of talin and vinculin to ECM bound integrin molecules at the site of external stimulation. Talin recruitment and its force-induced activation and subsequent interaction with vinculin have been extensively studied (2–4). Vinculin is natively in an auto-inhibited conformation and its activation involves removal of a steric hindrance preventing binding of Vt with actin (5) (Figure 1). Se
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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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"Serum actin-binding proteins as markers of metastasisof larynx and laryngeal pharynx cancer." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-279.

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Fang, Shijing, Joungjoa Park, Anne Crews, Kenneth B. Adler, and Troy Ghashghaei. "MARCKS Trafficking In Airway Epithelial Cells: Dynamics Of Phosphorylation And Membrane/Actin Binding." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a6375.

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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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Reports on the topic "Binding actif"

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Staiger, C. J. Identification of Actin-Binding Proteins from Maize Pollen. Office of Scientific and Technical Information (OSTI), 2004. http://dx.doi.org/10.2172/820708.

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Kotterman, M. J. J. Waterbodem immobilisatieonderzoek Noordzeekanaal: fase 2 : Binding van dioxines, tributyltin en PAKs aan actief kool. Wageningen Marine Research, 2021. http://dx.doi.org/10.18174/543912.

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