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  • Cell & Developmental Biology
  • Elasticity
  • LUNAR AND PLANETARY EXPLORATION
  • 2005-2009  (12)
  • 1935-1939
  • 2008  (9)
  • 2007  (3)
  • 1
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    Self-healing and thermoreversible rubber from supramolecular assembly (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-02-22
    Description: Rubbers exhibit enormous extensibility up to several hundred per cent, compared with a few per cent for ordinary solids, and have the ability to recover their original shape and dimensions on release of stress. Rubber elasticity is a property of macromolecules that are either covalently cross-linked or connected in a network by physical associations such as small glassy or crystalline domains, ionic aggregates or multiple hydrogen bonds. Covalent cross-links or strong physical associations prevent flow and creep. Here we design and synthesize molecules that associate together to form both chains and cross-links via hydrogen bonds. The system shows recoverable extensibility up to several hundred per cent and little creep under load. In striking contrast to conventional cross-linked or thermoreversible rubbers made of macromolecules, these systems, when broken or cut, can be simply repaired by bringing together fractured surfaces to self-heal at room temperature. Repaired samples recuperate their enormous extensibility. The process of breaking and healing can be repeated many times. These materials can be easily processed, re-used and recycled. Their unique self-repairing properties, the simplicity of their synthesis, their availability from renewable resources and the low cost of raw ingredients (fatty acids and urea) bode well for future applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cordier, Philippe -- Tournilhac, Francois -- Soulie-Ziakovic, Corinne -- Leibler, Ludwik -- England -- Nature. 2008 Feb 21;451(7181):977-80. doi: 10.1038/nature06669.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Matiere Molle et Chimie, UMR 7167 CNRS-ESPCI, Ecole Superieure de Physique et Chimie Industrielles, 10 rue Vauquelin, 75005 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18288191" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; Elasticity ; Fatty Acids/chemistry ; Hydrogen Bonding ; Mechanics ; Rheology ; Rubber/*chemistry ; Temperature ; Urea/chemistry
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Materials science: the gift of healing (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-02-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mynar, Justin L -- Aida, Takuzo -- England -- Nature. 2008 Feb 21;451(7181):895-6. doi: 10.1038/451895a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18288172" target="_blank"〉PubMed〈/a〉
    Keywords: Biomedical Research ; Conservation of Natural Resources ; Elasticity ; Hydrogen Bonding ; Mechanics ; Rubber/*chemistry ; Temperature
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Self-assembly of large and small molecules into hierarchically ordered sacs and membranes (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-03-29
    Description: We report here the self-assembly of macroscopic sacs and membranes at the interface between two aqueous solutions, one containing a megadalton polymer and the other, small self-assembling molecules bearing opposite charge. The resulting structures have a highly ordered architecture in which nanofiber bundles align and reorient by nearly 90 degrees as the membrane grows. The formation of a diffusion barrier upon contact between the two liquids prevents their chaotic mixing. We hypothesize that growth of the membrane is then driven by a dynamic synergy between osmotic pressure of ions and static self-assembly. These robust, self-sealing macroscopic structures offer opportunities in many areas, including the formation of privileged environments for cells, immune barriers, new biological assays, and self-assembly of ordered thick membranes for diverse applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Capito, Ramille M -- Azevedo, Helena S -- Velichko, Yuri S -- Mata, Alvaro -- Stupp, Samuel I -- 5-P50-NS054287/NS/NINDS NIH HHS/ -- 5-R01-DE015920/DE/NIDCR NIH HHS/ -- 5-R01-EB003806/EB/NIBIB NIH HHS/ -- New York, N.Y. -- Science. 2008 Mar 28;319(5871):1812-6. doi: 10.1126/science.1154586.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for BioNanotechnology in Medicine, Northwestern University, Chicago, IL 60611, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18369143" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Differentiation ; Cell Survival ; Chondrocytes/cytology ; Diffusion ; Elasticity ; Humans ; Hyaluronic Acid/*chemistry ; *Membranes, Artificial ; Mesenchymal Stromal Cells/cytology/physiology ; Microscopy, Electron ; Nanostructures/chemistry ; Osmotic Pressure ; Peptides/*chemistry ; Permeability ; Polymers/*chemistry ; Static Electricity ; Transforming Growth Factor beta1/chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Stress and fold localization in thin elastic membranes (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-05-20
    Description: Thin elastic membranes supported on a much softer elastic solid or a fluid deviate from their flat geometries upon compression. We demonstrate that periodic wrinkling is only one possible solution for such strained membranes. Folds, which involve highly localized curvature, appear whenever the membrane is compressed beyond a third of its initial wrinkle wavelength. Eventually the surface transforms into a symmetry-broken state with flat regions of membrane coexisting with locally folded points, reminiscent of a crumpled, unsupported membrane. We provide general scaling laws for the wrinkled and folded states and proved the transition with numerical and experimental supported membranes. Our work provides insight into the interfacial stability of such diverse systems as biological membranes such as lung surfactant and nanoparticle thin films.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pocivavsek, Luka -- Dellsy, Robert -- Kern, Andrew -- Johnson, Sebastian -- Lin, Binhua -- Lee, Ka Yee C -- Cerda, Enrique -- New York, N.Y. -- Science. 2008 May 16;320(5878):912-6. doi: 10.1126/science.1154069.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and James Franck Institute (JFI), University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18487188" target="_blank"〉PubMed〈/a〉
    Keywords: Elasticity ; Gels ; Lipids/chemistry ; Mathematics ; *Membranes/chemistry ; *Membranes, Artificial ; Metal Nanoparticles/chemistry ; *Polyesters/chemistry ; Pulmonary Surfactants/chemistry ; Stress, Mechanical ; Thermodynamics ; Water
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Traction dynamics of filopodia on compliant substrates (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-12-17
    Description: Cells sense the environment's mechanical stiffness to control their own shape, migration, and fate. To better understand stiffness sensing, we constructed a stochastic model of the "motor-clutch" force transmission system, where molecular clutches link F-actin to the substrate and mechanically resist myosin-driven F-actin retrograde flow. The model predicts two distinct regimes: (i) "frictional slippage," with fast retrograde flow and low traction forces on stiff substrates and (ii) oscillatory "load-and-fail" dynamics, with slower retrograde flow and higher traction forces on soft substrates. We experimentally confirmed these model predictions in embryonic chick forebrain neurons by measuring the nanoscale dynamics of single-growth-cone filopodia. Furthermore, we experimentally observed a model-predicted switch in F-actin dynamics around an elastic modulus of 1 kilopascal. Thus, a motor-clutch system inherently senses and responds to the mechanical stiffness of the local environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, Clarence E -- Odde, David J -- R01-GM-76177/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2008 Dec 12;322(5908):1687-91. doi: 10.1126/science.1163595.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomedical Engineering, University of Minnesota, Minneapolis, MN 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19074349" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*physiology ; Actins/*physiology ; Animals ; Biomechanical Phenomena ; Cell Adhesion ; Cells, Cultured ; Chick Embryo ; Compliance ; Computer Simulation ; Elastic Modulus ; Elasticity ; Growth Cones/*physiology/ultrastructure ; Models, Biological ; Myosin Type II/physiology ; Neurons/physiology ; Pseudopodia/*physiology ; Surface Tension
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Materials science. Adaptive composites (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vaia, Richard -- Baur, Jeffery -- New York, N.Y. -- Science. 2008 Jan 25;319(5862):420-1. doi: 10.1126/science.1152931.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, OH 45433, USA. richard.vaia@wpafb.af.mil〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18218885" target="_blank"〉PubMed〈/a〉
    Keywords: Biomimetic Materials ; Elasticity ; Elastomers ; *Nanostructures ; *Polymers ; Temperature
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Stimuli-responsive polymer nanocomposites inspired by the sea cucumber dermis (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-03-08
    Description: Sea cucumbers, like other echinoderms, have the ability to rapidly and reversibly alter the stiffness of their inner dermis. It has been proposed that the modulus of this tissue is controlled by regulating the interactions among collagen fibrils, which reinforce a low-modulus matrix. We report on a family of polymer nanocomposites, which mimic this architecture and display similar chemoresponsive mechanic adaptability. Materials based on a rubbery host polymer and rigid cellulose nanofibers exhibit a reversible reduction by a factor of 40 of the tensile modulus, for example, from 800 to 20 megapascals (MPa), upon exposure to a chemical regulator that mediates nanofiber interactions. Using a host polymer with a thermal transition in the regime of interest, we demonstrated even larger modulus changes (4200 to 1.6 MPa) upon exposure to emulated physiological conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Capadona, Jeffrey R -- Shanmuganathan, Kadhiravan -- Tyler, Dustin J -- Rowan, Stuart J -- Weder, Christoph -- R21 NS053798/NS/NINDS NIH HHS/ -- R21 NS053798-02/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2008 Mar 7;319(5868):1370-4. doi: 10.1126/science.1153307.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Macromolecular Science and Engineering, Case Western Reserve University, Cleveland, OH 44106, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18323449" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biomimetic Materials/chemistry ; *Cellulose/chemistry ; Cerebrospinal Fluid ; Dermis ; Elasticity ; Epichlorohydrin/chemistry ; Ethylene Oxide/chemistry ; Hydrogen Bonding ; Microelectrodes ; *Nanocomposites/chemistry ; Phase Transition ; *Polymers/chemistry ; *Sea Cucumbers ; Solvents ; Stress, Mechanical ; Temperature ; Tensile Strength ; Urochordata
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Biophysics. Enigmas of blood clot elasticity (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-04-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weisel, John W -- New York, N.Y. -- Science. 2008 Apr 25;320(5875):456-7. doi: 10.1126/science.1154210.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. weisel@mail.med.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18436761" target="_blank"〉PubMed〈/a〉
    Keywords: Biophysical Phenomena ; Biophysics ; Blood Coagulation/*physiology ; Computer Simulation ; Elasticity ; Fibrin/*chemistry ; Fibrinogen/*chemistry ; Humans ; Protein Folding ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Tough, bio-inspired hybrid materials (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-12-06
    Description: The notion of mimicking natural structures in the synthesis of new structural materials has generated enormous interest but has yielded few practical advances. Natural composites achieve strength and toughness through complex hierarchical designs that are extremely difficult to replicate synthetically. We emulate nature's toughening mechanisms by combining two ordinary compounds, aluminum oxide and polymethyl methacrylate, into ice-templated structures whose toughness can be more than 300 times (in energy terms) that of their constituents. The final product is a bulk hybrid ceramic-based material whose high yield strength and fracture toughness [ approximately 200 megapascals (MPa) and approximately 30 MPa.m(1/2)] represent specific properties comparable to those of aluminum alloys. These model materials can be used to identify the key microstructural features that should guide the synthesis of bio-inspired ceramic-based composites with unique strength and toughness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Munch, E -- Launey, M E -- Alsem, D H -- Saiz, E -- Tomsia, A P -- Ritchie, R O -- New York, N.Y. -- Science. 2008 Dec 5;322(5907):1516-20. doi: 10.1126/science.1164865.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19056979" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Oxide/*chemistry ; Animals ; Calcium Carbonate/chemistry ; Ceramics/*chemistry ; Elasticity ; Freezing ; Gastropoda/chemistry ; Materials Testing ; Mechanical Phenomena ; Polymethyl Methacrylate/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Role of intermolecular forces in defining material properties of protein nanofibrils (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-12-22
    Description: Protein molecules have the ability to form a rich variety of natural and artificial structures and materials. We show that amyloid fibrils, ordered supramolecular nanostructures that are self-assembled from a wide range of polypeptide molecules, have rigidities varying over four orders of magnitude, and constitute a class of high-performance biomaterials. We elucidate the molecular origin of fibril material properties and show that the major contribution to their rigidity stems from a generic interbackbone hydrogen-bonding network that is modulated by variable side-chain interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knowles, Tuomas P -- Fitzpatrick, Anthony W -- Meehan, Sarah -- Mott, Helen R -- Vendruscolo, Michele -- Dobson, Christopher M -- Welland, Mark E -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2007 Dec 21;318(5858):1900-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nanoscience Centre, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0FF, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18096801" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/*chemistry ; Amyloid beta-Peptides/chemistry ; Chemistry, Physical ; Elasticity ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Insulin/chemistry ; Lactalbumin/chemistry ; Lactoglobulins/chemistry ; Microscopy, Atomic Force ; Models, Molecular ; Muramidase/chemistry ; Nanostructures/*chemistry ; Peptide Termination Factors ; Peptides/*chemistry ; Physicochemical Phenomena ; Prealbumin/chemistry ; Prions/chemistry ; Protein Conformation ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins/chemistry ; Surface Tension ; alpha-Crystallin B Chain/chemistry
    Print ISSN: 0036-8075
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  • 11
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    Single-molecule experiments in vitro and in silico (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-05-26
    Description: Single-molecule force experiments in vitro enable the characterization of the mechanical response of biological matter at the nanometer scale. However, they do not reveal the molecular mechanisms underlying mechanical function. These can only be readily studied through molecular dynamics simulations of atomic structural models: "in silico" (by computer analysis) single-molecule experiments. Steered molecular dynamics simulations, in which external forces are used to explore the response and function of macromolecules, have become a powerful tool complementing and guiding in vitro single-molecule experiments. The insights provided by in silico experiments are illustrated here through a review of recent research in three areas of protein mechanics: elasticity of the muscle protein titin and the extracellular matrix protein fibronectin; linker-mediated elasticity of the cytoskeleton protein spectrin; and elasticity of ankyrin repeats, a protein module found ubiquitously in cells but with an as-yet unclear function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sotomayor, Marcos -- Schulten, Klaus -- 1 R01 GM073655/GM/NIGMS NIH HHS/ -- P41 RR05969/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2007 May 25;316(5828):1144-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of Illinois at Urbana-Champaign, and Beckman Institute for Advanced Science and Technology, 405 North Mathews Avenue, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525328" target="_blank"〉PubMed〈/a〉
    Keywords: Ankyrin Repeat/*physiology ; Computer Simulation ; Connectin ; Elasticity ; Fibronectins/*physiology ; Humans ; Models, Biological ; Muscle Proteins/*physiology ; Protein Kinases/*physiology ; Spectrin/*physiology ; Spectrum Analysis/*methods
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 12
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    Nonequilibrium mechanics of active cytoskeletal networks (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-01-20
    Description: Cells both actively generate and sensitively react to forces through their mechanical framework, the cytoskeleton, which is a nonequilibrium composite material including polymers and motor proteins. We measured the dynamics and mechanical properties of a simple three-component model system consisting of myosin II, actin filaments, and cross-linkers. In this system, stresses arising from motor activity controlled the cytoskeletal network mechanics, increasing stiffness by a factor of nearly 100 and qualitatively changing the viscoelastic response of the network in an adenosine triphosphate-dependent manner. We present a quantitative theoretical model connecting the large-scale properties of this active gel to molecular force generation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mizuno, Daisuke -- Tardin, Catherine -- Schmidt, C F -- Mackintosh, F C -- New York, N.Y. -- Science. 2007 Jan 19;315(5810):370-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and Astronomy, Vrije Universiteit, 1081HV Amsterdam, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17234946" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*physiology ; Actins/*physiology ; Adenosine Triphosphate/*metabolism ; Biomechanical Phenomena ; Cytoskeleton/*physiology ; Elasticity ; Mathematics ; *Models, Biological ; Molecular Motor Proteins/*physiology ; Myosin Type II/*physiology ; Rheology ; Stress, Mechanical ; Viscosity
    Print ISSN: 0036-8075
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