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  • Elasticity
  • Fracture
  • American Association for the Advancement of Science (AAAS)  (59)
  • Am. Soc. Mech. Eng.
  • Institute of Physics
  • 1
    Publication Date: 2016-04-23
    Description: The microtubule (MT) cytoskeleton can transmit mechanical signals and resist compression in contracting cardiomyocytes. How MTs perform these roles remains unclear because of difficulties in observing MTs during the rapid contractile cycle. Here, we used high spatial and temporal resolution imaging to characterize MT behavior in beating mouse myocytes. MTs deformed under contractile load into sinusoidal buckles, a behavior dependent on posttranslational "detyrosination" of alpha-tubulin. Detyrosinated MTs associated with desmin at force-generating sarcomeres. When detyrosination was reduced, MTs uncoupled from sarcomeres and buckled less during contraction, which allowed sarcomeres to shorten and stretch with less resistance. Conversely, increased detyrosination promoted MT buckling, stiffened the myocyte, and correlated with impaired function in cardiomyopathy. Thus, detyrosinated MTs represent tunable, compression-resistant elements that may impair cardiac function in disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robison, Patrick -- Caporizzo, Matthew A -- Ahmadzadeh, Hossein -- Bogush, Alexey I -- Chen, Christina Yingxian -- Margulies, Kenneth B -- Shenoy, Vivek B -- Prosser, Benjamin L -- HL089847/HL/NHLBI NIH HHS/ -- HL105993/HL/NHLBI NIH HHS/ -- R00-HL114879/HL/NHLBI NIH HHS/ -- R01EB017753/EB/NIBIB NIH HHS/ -- T32AR053461-09/AR/NIAMS NIH HHS/ -- T32HL007954/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2016 Apr 22;352(6284):aaf0659. doi: 10.1126/science.aaf0659.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Pennsylvania Muscle Institute, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104, USA. ; Department of Materials Science and Engineering, University of Pennsylvania School of Engineering and Applied Science, Philadelphia, PA 19104, USA. ; Department of Medicine, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104, USA. ; Department of Physiology, Pennsylvania Muscle Institute, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104, USA. bpros@mail.med.upenn.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27102488" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Desmin/metabolism ; Elasticity ; Heart Failure/metabolism/physiopathology ; Humans ; Male ; Mice ; Microtubules/*metabolism ; Models, Biological ; *Myocardial Contraction ; Myocytes, Cardiac/metabolism/*physiology ; Peptide Synthases/genetics/metabolism ; *Protein Processing, Post-Translational ; RNA, Small Interfering/genetics ; Rats ; Rats, Sprague-Dawley ; Sarcomeres/metabolism ; Tubulin/*metabolism ; Tyrosine/*metabolism
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  • 2
    Publication Date: 2015-07-25
    Description: Superelastic conducting fibers with improved properties and functionalities are needed for diverse applications. Here we report the fabrication of highly stretchable (up to 1320%) sheath-core conducting fibers created by wrapping carbon nanotube sheets oriented in the fiber direction on stretched rubber fiber cores. The resulting structure exhibited distinct short- and long-period sheath buckling that occurred reversibly out of phase in the axial and belt directions, enabling a resistance change of less than 5% for a 1000% stretch. By including other rubber and carbon nanotube sheath layers, we demonstrated strain sensors generating an 860% capacitance change and electrically powered torsional muscles operating reversibly by a coupled tension-to-torsion actuation mechanism. Using theory, we quantitatively explain the complementary effects of an increase in muscle length and a large positive Poisson's ratio on torsional actuation and electronic properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Z F -- Fang, S -- Moura, F A -- Ding, J N -- Jiang, N -- Di, J -- Zhang, M -- Lepro, X -- Galvao, D S -- Haines, C S -- Yuan, N Y -- Yin, S G -- Lee, D W -- Wang, R -- Wang, H Y -- Lv, W -- Dong, C -- Zhang, R C -- Chen, M J -- Yin, Q -- Chong, Y T -- Zhang, R -- Wang, X -- Lima, M D -- Ovalle-Robles, R -- Qian, D -- Lu, H -- Baughman, R H -- New York, N.Y. -- Science. 2015 Jul 24;349(6246):400-4. doi: 10.1126/science.aaa7952.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Alan G. MacDiarmid NanoTech Institute, University of Texas at Dallas, Richardson, TX 75080, USA. Jiangsu Collaborative Innovation Center of Photovoltaic Science and Engineering, Changzhou University, Changzhou 213164, China. Jiangnan Graphene Research Institute, Changzhou 213149, China. ; Alan G. MacDiarmid NanoTech Institute, University of Texas at Dallas, Richardson, TX 75080, USA. Jiangnan Graphene Research Institute, Changzhou 213149, China. ; Alan G. MacDiarmid NanoTech Institute, University of Texas at Dallas, Richardson, TX 75080, USA. Applied Physics Department, State University of Campinas, Campinas, SP 13081-970, Brazil. ; Jiangsu Collaborative Innovation Center of Photovoltaic Science and Engineering, Changzhou University, Changzhou 213164, China. Micro/Nano Science and Technology Center, Jiangsu University, Zhenjiang 212013, China. ; Alan G. MacDiarmid NanoTech Institute, University of Texas at Dallas, Richardson, TX 75080, USA. ; High-Performance Materials Institute, Florida State University, Tallahassee, FL 32310, USA. ; Applied Physics Department, State University of Campinas, Campinas, SP 13081-970, Brazil. ; Jiangsu Collaborative Innovation Center of Photovoltaic Science and Engineering, Changzhou University, Changzhou 213164, China. Jiangnan Graphene Research Institute, Changzhou 213149, China. ; Jiangnan Graphene Research Institute, Changzhou 213149, China. Institute of Materials Physics, Tianjin University of Technology, Tianjin 300384, China. ; Jiangnan Graphene Research Institute, Changzhou 213149, China. ; School of Astronautics, Northwestern Polytechnical University, Xi'an 710072, China. Department of Mechanical Engineering, University of Texas at Dallas, Richardson, TX 75080, USA. ; Department of Mechanical Engineering, University of Texas at Dallas, Richardson, TX 75080, USA. ; Lintec of America, Nano-Science and Technology Center, Richardson, TX 75081, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26206929" target="_blank"〉PubMed〈/a〉
    Keywords: *Elastic Tissue ; Elasticity ; Electric Capacitance ; *Electronics ; *Muscle, Skeletal ; *Nanotubes, Carbon ; Torsion, Mechanical
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  • 3
    Publication Date: 2015-01-13
    Description: The mechanical mismatch between soft neural tissues and stiff neural implants hinders the long-term performance of implantable neuroprostheses. Here, we designed and fabricated soft neural implants with the shape and elasticity of dura mater, the protective membrane of the brain and spinal cord. The electronic dura mater, which we call e-dura, embeds interconnects, electrodes, and chemotrodes that sustain millions of mechanical stretch cycles, electrical stimulation pulses, and chemical injections. These integrated modalities enable multiple neuroprosthetic applications. The soft implants extracted cortical states in freely behaving animals for brain-machine interface and delivered electrochemical spinal neuromodulation that restored locomotion after paralyzing spinal cord injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Minev, Ivan R -- Musienko, Pavel -- Hirsch, Arthur -- Barraud, Quentin -- Wenger, Nikolaus -- Moraud, Eduardo Martin -- Gandar, Jerome -- Capogrosso, Marco -- Milekovic, Tomislav -- Asboth, Leonie -- Torres, Rafael Fajardo -- Vachicouras, Nicolas -- Liu, Qihan -- Pavlova, Natalia -- Duis, Simone -- Larmagnac, Alexandre -- Voros, Janos -- Micera, Silvestro -- Suo, Zhigang -- Courtine, Gregoire -- Lacour, Stephanie P -- New York, N.Y. -- Science. 2015 Jan 9;347(6218):159-63. doi: 10.1126/science.1260318.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bertarelli Foundation Chair in Neuroprosthetic Technology, Laboratory for Soft Bioelectronic Interfaces, Centre for Neuroprosthetics, Institute of Microengineering and Institute of Bioengineering, Ecole Polytechnique Federale de Lausanne (EPFL), Switzerland. ; International Paraplegic Foundation Chair in Spinal Cord Repair, Centre for Neuroprosthetics and Brain Mind Institute, EPFL, Switzerland. Pavlov Institute of Physiology, St. Petersburg, Russia. ; International Paraplegic Foundation Chair in Spinal Cord Repair, Centre for Neuroprosthetics and Brain Mind Institute, EPFL, Switzerland. ; Translational Neural Engineering Laboratory, Center for Neuroprosthetics and Institute of Bioengineering, EPFL, Lausanne, Switzerland. ; Bertarelli Foundation Chair in Neuroprosthetic Technology, Laboratory for Soft Bioelectronic Interfaces, Centre for Neuroprosthetics, Institute of Microengineering and Institute of Bioengineering, Ecole Polytechnique Federale de Lausanne (EPFL), Switzerland. International Paraplegic Foundation Chair in Spinal Cord Repair, Centre for Neuroprosthetics and Brain Mind Institute, EPFL, Switzerland. ; School of Engineering and Applied Sciences, Kavli Institute for Bionano Science and Technology, Harvard University, Cambridge, MA, USA. ; Laboratory for Biosensors and Bioelectronics, Institute for Biomedical Engineering, University and ETH Zurich, Switzerland. ; Translational Neural Engineering Laboratory, Center for Neuroprosthetics and Institute of Bioengineering, EPFL, Lausanne, Switzerland. The BioRobotics Institute, Scuola Superiore Sant'Anna, Pisa 56025, Italy. ; International Paraplegic Foundation Chair in Spinal Cord Repair, Centre for Neuroprosthetics and Brain Mind Institute, EPFL, Switzerland. gregoire.courtine@epfl.ch stephanie.lacour@epfl.ch. ; Bertarelli Foundation Chair in Neuroprosthetic Technology, Laboratory for Soft Bioelectronic Interfaces, Centre for Neuroprosthetics, Institute of Microengineering and Institute of Bioengineering, Ecole Polytechnique Federale de Lausanne (EPFL), Switzerland. gregoire.courtine@epfl.ch stephanie.lacour@epfl.ch.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25574019" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biocompatible Materials/therapeutic use ; Brain-Computer Interfaces ; Drug Delivery Systems/*methods ; *Dura Mater ; Elasticity ; Electric Stimulation/*methods ; Electrochemotherapy/*methods ; *Electrodes, Implanted ; Locomotion ; Mice ; Mice, Inbred Strains ; Motor Cortex/physiopathology ; Multimodal Imaging ; Neurons/physiology ; Paralysis/etiology/physiopathology/*therapy ; Platinum ; *Prostheses and Implants ; Silicon ; Spinal Cord/physiopathology ; Spinal Cord Injuries/complications/physiopathology/*therapy
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  • 4
    Publication Date: 2014-04-05
    Description: When mounted on the skin, modern sensors, circuits, radios, and power supply systems have the potential to provide clinical-quality health monitoring capabilities for continuous use, beyond the confines of traditional hospital or laboratory facilities. The most well-developed component technologies are, however, broadly available only in hard, planar formats. As a result, existing options in system design are unable to effectively accommodate integration with the soft, textured, curvilinear, and time-dynamic surfaces of the skin. Here, we describe experimental and theoretical approaches for using ideas in soft microfluidics, structured adhesive surfaces, and controlled mechanical buckling to achieve ultralow modulus, highly stretchable systems that incorporate assemblies of high-modulus, rigid, state-of-the-art functional elements. The outcome is a thin, conformable device technology that can softly laminate onto the surface of the skin to enable advanced, multifunctional operation for physiological monitoring in a wireless mode.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, Sheng -- Zhang, Yihui -- Jia, Lin -- Mathewson, Kyle E -- Jang, Kyung-In -- Kim, Jeonghyun -- Fu, Haoran -- Huang, Xian -- Chava, Pranav -- Wang, Renhan -- Bhole, Sanat -- Wang, Lizhe -- Na, Yoon Joo -- Guan, Yue -- Flavin, Matthew -- Han, Zheshen -- Huang, Yonggang -- Rogers, John A -- New York, N.Y. -- Science. 2014 Apr 4;344(6179):70-4. doi: 10.1126/science.1250169.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Materials Science and Engineering and Frederick Seitz Materials Research Laboratory, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24700852" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Elasticity ; Electrocardiography/instrumentation/methods ; Electrocardiography, Ambulatory/instrumentation/methods ; Electroencephalography/instrumentation/methods ; Electromyography/instrumentation/methods ; Electrooculography ; Equipment Design ; Humans ; Male ; Microfluidics/*instrumentation ; Monitoring, Ambulatory/*instrumentation/methods ; Monitoring, Physiologic/*instrumentation/methods ; Remote Sensing Technology ; Silicone Elastomers ; *Skin ; Wireless Technology ; Young Adult
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  • 5
    Publication Date: 2012-03-17
    Description: Various plants and fungi have evolved ingenious devices to disperse their spores. One such mechanism is the cavitation-triggered catapult of fern sporangia. The spherical sporangia enclosing the spores are equipped with a row of 12 to 13 specialized cells, the annulus. When dehydrating, these cells induce a dramatic change of curvature in the sporangium, which is released abruptly after the cavitation of the annulus cells. The entire ejection process is reminiscent of human-made catapults with one notable exception: The sporangia lack the crossbar that arrests the catapult arm in its returning motion. We show that much of the sophistication and efficiency of the ejection mechanism lies in the two very different time scales associated with the annulus closure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noblin, X -- Rojas, N O -- Westbrook, J -- Llorens, C -- Argentina, M -- Dumais, J -- New York, N.Y. -- Science. 2012 Mar 16;335(6074):1322. doi: 10.1126/science.1215985.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Universite de Nice Sophia Antipolis (UNS), Laboratoire de Physique de la Matiere Condensee, CNRS UMR 7336, Nice, France. xavier.noblin@unice.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22422975" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Shape ; Elasticity ; Polypodium/cytology/*physiology ; Sporangia/cytology/*physiology ; Spores/*physiology ; Water
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  • 6
    Publication Date: 2012-03-03
    Description: Although genetic control of morphogenesis is well established, elaboration of complex shapes requires changes in the mechanical properties of cells. In plants, the first visible sign of leaf formation is a bulge on the flank of the shoot apical meristem. Bulging results from local relaxation of cell walls, which causes them to yield to internal hydrostatic pressure. By manipulation of tissue tension in combination with quantitative live imaging and finite-element modeling, we found that the slow-growing area at the shoot tip is substantially strain-stiffened compared with surrounding fast-growing tissue. We propose that strain stiffening limits growth, restricts organ bulging, and contributes to the meristem's functional zonation. Thus, mechanical signals are not just passive readouts of gene action but feed back on morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kierzkowski, Daniel -- Nakayama, Naomi -- Routier-Kierzkowska, Anne-Lise -- Weber, Alain -- Bayer, Emmanuelle -- Schorderet, Martine -- Reinhardt, Didier -- Kuhlemeier, Cris -- Smith, Richard S -- New York, N.Y. -- Science. 2012 Mar 2;335(6072):1096-9. doi: 10.1126/science.1213100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Plant Sciences, University of Bern, Bern, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22383847" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Wall/physiology/ultrastructure ; Elasticity ; Hydrostatic Pressure ; Lycopersicon esculentum/cytology/*growth & development ; Meristem/cytology/*growth & development ; Models, Biological ; *Morphogenesis ; Osmolar Concentration ; Osmotic Pressure ; Plant Shoots/cytology/*growth & development
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  • 7
    Publication Date: 2011-09-24
    Description: We studied the mechanical process of seed pods opening in Bauhinia variegate and found a chirality-creating mechanism, which turns an initially flat pod valve into a helix. We studied con fi gurations of strips cut from pod valve tissue and from composite elastic materials that mimic its structure. The experiments reveal various helical con fi gurations with sharp morphological transitions between them. Using the mathematical framework of "incompatible elasticity," we modeled the pod as a thin strip with a flat intrinsic metric and a saddle-like intrinsic curvature. Our theoretical analysis quantitatively predicts all observed con fi gurations, thus linking the pod's microscopic structure and macroscopic conformation. We suggest that this type of incompatible strip is likely to play a role in the self-assembly of chiral macromolecules and could be used for the engineering of synthetic self-shaping devices.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Armon, Shahaf -- Efrati, Efi -- Kupferman, Raz -- Sharon, Eran -- New York, N.Y. -- Science. 2011 Sep 23;333(6050):1726-30. doi: 10.1126/science.1203874.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Racah Institute of Physics, Hebrew University of Jerusalem, Jerusalem 91904, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21940888" target="_blank"〉PubMed〈/a〉
    Keywords: Bauhinia/*anatomy & histology/physiology ; Biomimetic Materials ; Elasticity ; *Latex ; Mathematical Concepts ; Models, Biological ; Physical Phenomena ; Seeds/*anatomy & histology/*physiology
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2011-09-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Forterre, Yoel -- Dumais, Jacques -- New York, N.Y. -- Science. 2011 Sep 23;333(6050):1715-6. doi: 10.1126/science.1210734.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉IUSTI, CNRS, Aix-Marseille Universite, 13453 Marseille Cedex 13, France. yoel.forterre@polytech.univ-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21940886" target="_blank"〉PubMed〈/a〉
    Keywords: Bauhinia/*anatomy & histology ; Biomimetic Materials ; Elasticity ; Seeds/*anatomy & histology
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-08-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhatia, Mickie -- New York, N.Y. -- Science. 2010 Aug 27;329(5995):1024-5. doi: 10.1126/science.1194919.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stem Cell and Cancer Research Institute, McMaster University, Hamilton, Ontario L8N 3Z5, Canada. mbhatia@mcmaster.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20798306" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Culture Techniques/*methods ; Cell Differentiation ; Cell Division ; Cells, Cultured ; Elasticity ; Humans ; Hydrogels ; Mice ; Muscle Fibers, Skeletal/*cytology/physiology ; Myoblasts, Skeletal/cytology/physiology ; Regeneration ; Stem Cell Niche/*physiology ; Stem Cell Transplantation ; Stem Cells/*physiology
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  • 10
    Publication Date: 2010-08-07
    Description: Using optical trapping and fluorescence imaging techniques, we measured the step size and stiffness of single skeletal myosins interacting with actin filaments and arranged on myosin-rod cofilaments that approximate myosin mechanics during muscle contraction. Stiffness is dramatically lower for negatively compared to positively strained myosins, consistent with buckling of myosin's subfragment 2 rod domain. Low stiffness minimizes drag of negatively strained myosins during contraction at loaded conditions. Myosin's elastic portion is stretched during active force generation, reducing apparent step size with increasing load, even though the working stroke is approximately constant at about 8 nanometers. Taking account of the nonlinear nature of myosin elasticity is essential to relate myosin's internal structural changes to physiological force generation and filament sliding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaya, Motoshi -- Higuchi, Hideo -- New York, N.Y. -- Science. 2010 Aug 6;329(5992):686-9. doi: 10.1126/science.1191484.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyou-ku, Tokyo, 113-0033 Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20689017" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*physiology ; Actomyosin/chemistry/physiology ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Compliance ; Elasticity ; Models, Biological ; *Muscle Contraction ; Muscle Fibers, Skeletal/chemistry/physiology ; Muscle, Skeletal ; Myosin Subfragments/physiology ; Myosins/chemistry/*physiology ; Quantum Dots ; Rabbits
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-03-27
    Description: Recent advances in mechanics and materials provide routes to integrated circuits that can offer the electrical properties of conventional, rigid wafer-based technologies but with the ability to be stretched, compressed, twisted, bent, and deformed into arbitrary shapes. Inorganic and organic electronic materials in microstructured and nanostructured forms, intimately integrated with elastomeric substrates, offer particularly attractive characteristics, with realistic pathways to sophisticated embodiments. Here, we review these strategies and describe applications of them in systems ranging from electronic eyeball cameras to deformable light-emitting displays. We conclude with some perspectives on routes to commercialization, new device opportunities, and remaining challenges for research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rogers, John A -- Someya, Takao -- Huang, Yonggang -- New York, N.Y. -- Science. 2010 Mar 26;327(5973):1603-7. doi: 10.1126/science.1182383.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, 1304 West Green Street, Urbana, IL 61801, USA. jrogers@illinois.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20339064" target="_blank"〉PubMed〈/a〉
    Keywords: Biocompatible Materials ; Diagnostic Equipment ; Elasticity ; Elastomers ; *Electrical Equipment and Supplies ; Equipment Design ; Humans ; Mechanical Phenomena ; Nanostructures ; *Semiconductors ; Therapeutics/instrumentation
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2009-08-01
    Description: Mathew-Fenn et al. (Reports, 17 October 2008, p. 446) reported unexpected distance fluctuations in short end-labeled DNA constructs and interpreted them as evidence for cooperative DNA stretching modes. We show that when accounting for a subtle linker leverage effect, their data can be understood within standard noncooperative DNA elasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Becker, Nils B -- Everaers, Ralf -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):538; author reply 538. doi: 10.1126/science.1168786.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre Blaise Pascal et Laboratoire de Physique, CNRS UMR 5672, Ecole Normale Superieure, Universite de Lyon, 46 Allee d'Italie, 69007 Lyon, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644093" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/*chemistry ; Elasticity ; Gold ; Metal Nanoparticles ; Models, Molecular ; Monte Carlo Method ; *Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry
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  • 13
    Publication Date: 2009-03-21
    Description: Improved electrically powered artificial muscles are needed for generating force, moving objects, and accomplishing work. Carbon nanotube aerogel sheets are the sole component of new artificial muscles that provide giant elongations and elongation rates of 220% and (3.7 x 10(4))% per second, respectively, at operating temperatures from 80 to 1900 kelvin. These solid-state-fabricated sheets are enthalpic rubbers having gaslike density and specific strength in one direction higher than those of steel plate. Actuation decreases nanotube aerogel density and can be permanently frozen for such device applications as transparent electrodes. Poisson's ratios reach 15, a factor of 30 higher than for conventional rubbers. These giant Poisson's ratios explain the observed opposite sign of width and length actuation and result in rare properties: negative linear compressibility and stretch densification.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aliev, Ali E -- Oh, Jiyoung -- Kozlov, Mikhail E -- Kuznetsov, Alexander A -- Fang, Shaoli -- Fonseca, Alexandre F -- Ovalle, Raquel -- Lima, Marcio D -- Haque, Mohammad H -- Gartstein, Yuri N -- Zhang, Mei -- Zakhidov, Anvar A -- Baughman, Ray H -- New York, N.Y. -- Science. 2009 Mar 20;323(5921):1575-8. doi: 10.1126/science.1168312.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Alan G. MacDiarmid NanoTech Institute, University of Texas at Dallas, Richardson, TX 75083, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19299612" target="_blank"〉PubMed〈/a〉
    Keywords: Biomimetic Materials/chemistry ; Elasticity ; Muscle, Skeletal ; *Nanotubes, Carbon/chemistry ; Static Electricity ; Temperature ; Tensile Strength
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  • 14
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    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
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  • 15
    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
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  • 16
    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
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  • 17
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    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
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  • 18
    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
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  • 19
    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
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  • 20
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    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
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  • 21
    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
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  • 22
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    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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  • 23
    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
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  • 24
    Publication Date: 2006-08-05
    Description: Blood clots perform an essential mechanical task, yet the mechanical behavior of fibrin fibers, which form the structural framework of a clot, is largely unknown. By using combined atomic force-fluorescence microscopy, we determined the elastic limit and extensibility of individual fibers. Fibrin fibers can be strained 180% (2.8-fold extension) without sustaining permanent lengthening, and they can be strained up to 525% (average 330%) before rupturing. This is the largest extensibility observed for protein fibers. The data imply that fibrin monomers must be able to undergo sizeable, reversible structural changes and that deformations in clots can be accommodated by individual fiber stretching.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1950267/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1950267/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, W -- Jawerth, L M -- Sparks, E A -- Falvo, M R -- Hantgan, R R -- Superfine, R -- Lord, S T -- Guthold, M -- P41 EB002025/EB/NIBIB NIH HHS/ -- R01 HL31048/HL/NHLBI NIH HHS/ -- R41 CA10312/CA/NCI NIH HHS/ -- R41 CA103120/CA/NCI NIH HHS/ -- R41 CA103120-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):634.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Wake Forest University, Winston-Salem, NC 27109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16888133" target="_blank"〉PubMed〈/a〉
    Keywords: Blood Coagulation ; Elasticity ; Factor XIII/chemistry ; Fibrin/*chemistry ; Microscopy, Atomic Force ; Stress, Mechanical
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  • 25
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-06-24
    Description: The orb web is a spectacular evolutionary innovation that enables spiders to catch flying prey. This elegant, geometric structure is woven with silk fibers that are renowned for their superior mechanical properties. We used silk gland expression libraries to address a long-standing controversy concerning the evolution of the orb-web architecture. Contrary to the view that the orb-web design evolved multiple times, we found that the distribution and phylogeny of silk proteins support a single, ancient origin of the orb web at least 136 million years ago. Furthermore, we substantially expanded the repository of silk sequences that can be used for the synthesis of high-performance biomaterials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Penalver, Enrique -- Grimaldi, David A -- Delclos, Xavier -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1761.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, American Museum of Natural History, New York, NY 10024, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794072" target="_blank"〉PubMed〈/a〉
    Keywords: *Amber ; Animals ; Biological Evolution ; Elasticity ; *Fossils ; Insects ; Mites ; Selection, Genetic ; *Silk ; *Spiders/classification/genetics
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  • 26
    Publication Date: 2006-03-11
    Description: A biosynthetic approach was developed to control and probe cooperativity in multiunit biomotor assemblies by linking molecular motors to artificial protein scaffolds. This approach provides precise control over spatial and elastic coupling between motors. Cooperative interactions between monomeric kinesin-1 motors attached to protein scaffolds enhance hydrolysis activity and microtubule gliding velocity. However, these interactions are not influenced by changes in the elastic properties of the scaffold, distinguishing multimotor transport from that powered by unorganized monomeric motors. These results highlight the role of supramolecular architecture in determining mechanisms of collective transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diehl, Michael R -- Zhang, Kechun -- Lee, Heun Jin -- Tirrell, David A -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1468-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. diehl@rice.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527982" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry ; Amino Acid Sequence ; Elasticity ; Elastin/chemistry ; Hydrolysis ; Kinesin/chemistry ; Microtubules/physiology ; Models, Biological ; Molecular Motor Proteins/*physiology ; Molecular Sequence Data ; Protein Engineering ; Protein Structure, Tertiary ; Proteins/chemistry/*physiology ; Recombinant Proteins/chemistry ; Structure-Activity Relationship
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  • 27
    Publication Date: 2005-12-13
    Description: Practical components for three-dimensional molecular nanofabrication must be simple to produce, stereopure, rigid, and adaptable. We report a family of DNA tetrahedra, less than 10 nanometers on a side, that can self-assemble in seconds with near-quantitative yield of one diastereomer. They can be connected by programmable DNA linkers. Their triangulated architecture confers structural stability; by compressing a DNA tetrahedron with an atomic force microscope, we have measured the axial compressibility of DNA and observed the buckling of the double helix under high loads.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goodman, R P -- Schaap, I A T -- Tardin, C F -- Erben, C M -- Berry, R M -- Schmidt, C F -- Turberfield, A J -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1661-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Clarendon Laboratory, Department of Physics, University of Oxford, Parks Road, Oxford OX1 3PU, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16339440" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Base Sequence ; Chemistry, Physical ; DNA/*chemistry ; Dimerization ; Elasticity ; Microscopy, Atomic Force ; Models, Molecular ; Molecular Structure ; *Nanostructures ; *Nanotechnology ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry ; Physicochemical Phenomena ; Stereoisomerism
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  • 28
    Publication Date: 2005-11-19
    Description: Normal tissue cells are generally not viable when suspended in a fluid and are therefore said to be anchorage dependent. Such cells must adhere to a solid, but a solid can be as rigid as glass or softer than a baby's skin. The behavior of some cells on soft materials is characteristic of important phenotypes; for example, cell growth on soft agar gels is used to identify cancer cells. However, an understanding of how tissue cells-including fibroblasts, myocytes, neurons, and other cell types-sense matrix stiffness is just emerging with quantitative studies of cells adhering to gels (or to other cells) with which elasticity can be tuned to approximate that of tissues. Key roles in molecular pathways are played by adhesion complexes and the actinmyosin cytoskeleton, whose contractile forces are transmitted through transcellular structures. The feedback of local matrix stiffness on cell state likely has important implications for development, differentiation, disease, and regeneration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Discher, Dennis E -- Janmey, Paul -- Wang, Yu-Li -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1139-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Engineering and Applied Science and Cell and Molecular Biology Graduate Group, University of Pennsylvania, Philadelphia, PA 19104-6315, USA. discher@seas.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293750" target="_blank"〉PubMed〈/a〉
    Keywords: Biomechanical Phenomena ; Cell Adhesion ; Cell Communication ; *Cell Physiological Phenomena ; Cytoskeleton/physiology ; Elasticity ; Humans ; Muscle Contraction/physiology ; Organogenesis/physiology
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  • 29
    Publication Date: 2005-05-28
    Description: The typical scales for plant and fungal movements vary over many orders of magnitude in time and length, but they are ultimately based on hydraulics and mechanics. We show that quantification of the length and time scales involved in plant and fungal motions leads to a natural classification, whose physical basis can be understood through an analysis of the mechanics of water transport through an elastic tissue. Our study also suggests a design principle for nonmuscular hydraulically actuated structures: Rapid actuation requires either small size or the enhancement of motion on large scales via elastic instabilities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skotheim, Jan M -- Mahadevan, L -- New York, N.Y. -- Science. 2005 May 27;308(5726):1308-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Applied Mathematics and Theoretical Physics, Centre for Mathematical Sciences, University of Cambridge, Cambridge CB3 0WA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15919993" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Wall/physiology ; Droseraceae/anatomy & histology/physiology ; Elasticity ; Euphorbiaceae/anatomy & histology/physiology ; Fungi/cytology/*physiology ; Mathematics ; Movement ; Mucorales/cytology/physiology ; Physical Phenomena ; Physics ; Plant Leaves/*physiology ; *Plant Physiological Phenomena ; Plants/anatomy & histology ; Pressure ; Time Factors ; Viscosity ; Water/*physiology
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  • 30
    Publication Date: 2005-03-26
    Description: Soft tissues are preserved within hindlimb elements of Tyrannosaurus rex (Museum of the Rockies specimen 1125). Removal of the mineral phase reveals transparent, flexible, hollow blood vessels containing small round microstructures that can be expressed from the vessels into solution. Some regions of the demineralized bone matrix are highly fibrous, and the matrix possesses elasticity and resilience. Three populations of microstructures have cell-like morphology. Thus, some dinosaurian soft tissues may retain some of their original flexibility, elasticity, and resilience.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schweitzer, Mary H -- Wittmeyer, Jennifer L -- Horner, John R -- Toporski, Jan K -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1952-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Marine, Earth, Atmospheric Sciences, North Carolina State University, Raleigh, NC 27695, USA. schweitzer@ncsu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790853" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Vessels/*anatomy & histology/cytology ; Bone Demineralization Technique ; Bone Matrix ; Bone and Bones/anatomy & histology/*blood supply/*cytology ; Cell Separation ; DNA/analysis ; Dinosaurs/*anatomy & histology ; Elasticity ; Femur/anatomy & histology/blood supply ; *Fossils ; Microscopy, Electron, Scanning ; Montana ; Osteocytes/*cytology/ultrastructure ; Time
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-19
    Description: In origami, form follows the sequential spatial organization of folds. This requires continuous intervention and raises a natural question: Can origami arise through self-organization? We answer this affirmatively by examining the possible physical origin for the Miura-ori leaf-folding patterns that arise naturally in insect wings, leaves, and other laminae-like organelles. In particular, we point out examples where biaxial compression of an elastically supported thin film, such as that due to differential growth, shrinkage, desiccation, or thermal expansion, spontaneously generates these patterns, and we provide a simple theoretical explanation for their occurrence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahadevan, L -- Rica, S -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1740.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Engineering and Applied Sciences and Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, MA 02138, USA. lm@deas.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774751" target="_blank"〉PubMed〈/a〉
    Keywords: Betulaceae/anatomy & histology/physiology ; Elasticity ; Mathematics ; Plant Leaves/anatomy & histology/*physiology ; Stress, Mechanical
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  • 32
    Publication Date: 2004-05-29
    Description: Networks of cross-linked and bundled actin filaments are ubiquitous in the cellular cytoskeleton, but their elasticity remains poorly understood. We show that these networks exhibit exceptional elastic behavior that reflects the mechanical properties of individual filaments. There are two distinct regimes of elasticity, one reflecting bending of single filaments and a second reflecting stretching of entropic fluctuations of filament length. The mechanical stiffness can vary by several decades with small changes in cross-link concentration, and can increase markedly upon application of external stress. We parameterize the full range of behavior in a state diagram and elucidate its origin with a robust model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardel, M L -- Shin, J H -- MacKintosh, F C -- Mahadevan, L -- Matsudaira, P -- Weitz, D A -- GM52703/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 May 28;304(5675):1301-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166374" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*chemistry/metabolism ; Actins/*chemistry/metabolism ; Biopolymers/chemistry/metabolism ; Elasticity ; Entropy ; Mathematics ; Microfilament Proteins/chemistry/metabolism ; Models, Biological ; Stress, Mechanical
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  • 33
    Publication Date: 2002-11-02
    Description: We present an approach to fabricate solid capsules with precise control of size, permeability, mechanical strength, and compatibility. The capsules are fabricated by the self-assembly of colloidal particles onto the interface of emulsion droplets. After the particles are locked together to form elastic shells, the emulsion droplets are transferred to a fresh continuous-phase fluid that is the same as that inside the droplets. The resultant structures, which we call "colloidosomes," are hollow, elastic shells whose permeability and elasticity can be precisely controlled. The generality and robustness of these structures and their potential for cellular immunoisolation are demonstrated by the use of a variety of solvents, particles, and contents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dinsmore, A D -- Hsu, Ming F -- Nikolaides, M G -- Marquez, Manuel -- Bausch, A R -- Weitz, D A -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):1006-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and DEAS, Harvard University, Cambridge, MA 02138, USA. dinsmore@physics.umass.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411700" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; *Capsules ; Cell Physiological Phenomena ; Cell Survival ; Cells, Cultured ; Chemistry, Physical ; *Colloids ; Diffusion ; Elasticity ; Emulsions ; Fibroblasts/physiology ; Microscopy, Confocal ; Microscopy, Electron, Scanning ; Permeability ; Physicochemical Phenomena ; Polylysine ; Polymethyl Methacrylate ; Surface Properties ; Water
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alper, Joe -- New York, N.Y. -- Science. 2002 Jul 19;297(5580):329-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Chemistry, Physical ; Collagen/chemistry ; Elasticity ; Elastin/chemistry ; *Fibroins ; Insect Proteins/chemistry ; Microfilament Proteins/chemistry ; Physicochemical Phenomena ; Polymers/*chemistry ; *Protein Conformation ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry ; Recombinant Proteins/chemistry ; Repetitive Sequences, Amino Acid ; Stress, Mechanical
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  • 35
    Publication Date: 2002-04-27
    Description: The introduction of biodegradable implant materials as well as minimally invasive surgical procedures in medicine has substantially improved health care within the past few decades. This report describes a group of degradable thermoplastic polymers that are able to change their shape after an increase in temperature. Their shape-memory capability enables bulky implants to be placed in the body through small incisions or to perform complex mechanical deformations automatically. A smart degradable suture was created to illustrate the potential of these shape-memory thermoplastics in biomedical applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lendlein, Andreas -- Langer, Robert -- New York, N.Y. -- Science. 2002 May 31;296(5573):1673-6. Epub 2002 Apr 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉mnemoScience GmbH, Pauwelsstrabetae 19, D-52074 Aachen, Germany. a.lendlein@mnemoscience.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976407" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biocompatible Materials/chemical synthesis/chemistry ; Chemistry, Physical ; Dioxanes/chemistry ; Elasticity ; Elastomers ; Isocyanates/chemistry ; Mechanics ; Physicochemical Phenomena ; Polyesters/chemistry ; *Polymers/chemical synthesis/chemistry ; *Prostheses and Implants ; Rats ; Stress, Mechanical ; *Sutures ; Temperature ; Thermodynamics
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  • 36
    Publication Date: 2002-01-19
    Description: Spider silks are protein-based "biopolymer" filaments or threads secreted by specialized epithelial cells as concentrated soluble precursors of highly repetitive primary sequences. Spider dragline silk is a flexible, lightweight fiber of extraordinary strength and toughness comparable to that of synthetic high-performance fibers. We sought to "biomimic" the process of spider silk production by expressing in mammalian cells the dragline silk genes (ADF-3/MaSpII and MaSpI) of two spider species. We produced soluble recombinant (rc)-dragline silk proteins with molecular masses of 60 to 140 kilodaltons. We demonstrated the wet spinning of silk monofilaments spun from a concentrated aqueous solution of soluble rc-spider silk protein (ADF-3; 60 kilodaltons) under modest shear and coagulation conditions. The spun fibers were water insoluble with a fine diameter (10 to 40 micrometers) and exhibited toughness and modulus values comparable to those of native dragline silks but with lower tenacity. Dope solutions with rc-silk protein concentrations 〉20% and postspinning draw were necessary to achieve improved mechanical properties of the spun fibers. Fiber properties correlated with finer fiber diameter and increased birefringence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lazaris, Anthoula -- Arcidiacono, Steven -- Huang, Yue -- Zhou, Jiang-Feng -- Duguay, Francois -- Chretien, Nathalie -- Welsh, Elizabeth A -- Soares, Jason W -- Karatzas, Costas N -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):472-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nexia Biotechnologies, Vaudreuil-Dorion, Quebec J7V 8P5, Canada. alazaris@nexiabiotech.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799236" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Biopolymers ; Birefringence ; Cattle ; Cell Line ; Cloning, Molecular ; Cricetinae ; Culture Media, Conditioned ; DNA, Complementary ; Elasticity ; Epithelial Cells/metabolism ; *Fibroins ; Materials Testing ; Mechanics ; Molecular Sequence Data ; Molecular Weight ; *Protein Biosynthesis ; Protein Structure, Secondary ; Proteins/chemistry/*genetics/isolation & purification ; Recombinant Proteins/biosynthesis/chemistry/isolation & purification ; Solubility ; Spiders/*genetics/metabolism ; Stress, Mechanical ; Tensile Strength ; Water
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiss, G -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1753-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11546850" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cooking ; Elasticity ; Fats/metabolism ; *Food ; Food Analysis ; *Food Preferences/physiology/psychology ; Hot Temperature ; Humans ; Perception ; *Research ; *Sensation ; Smell ; Taste ; Viscosity
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez, J M -- Chu, S -- Oberhauser, A F -- New York, N.Y. -- Science. 2001 Apr 27;292(5517):653-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, Mayo Foundation, Rochester, MN 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11330326" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Elasticity ; Ion Channels/chemistry ; Kinetics ; *Nucleic Acid Conformation ; Physicochemical Phenomena ; RNA/*chemistry ; RNA Stability ; RNA, Catalytic/*chemistry ; Stress, Mechanical ; Thermodynamics
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  • 39
    Publication Date: 2001-02-07
    Description: Soft lithography is an alternative to silicon-based micromachining that uses replica molding of nontraditional elastomeric materials to fabricate stamps and microfluidic channels. We describe here an extension to the soft lithography paradigm, multilayer soft lithography, with which devices consisting of multiple layers may be fabricated from soft materials. We used this technique to build active microfluidic systems containing on-off valves, switching valves, and pumps entirely out of elastomer. The softness of these materials allows the device areas to be reduced by more than two orders of magnitude compared with silicon-based devices. The other advantages of soft lithography, such as rapid prototyping, ease of fabrication, and biocompatibility, are retained.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Unger, M A -- Chou, H P -- Thorsen, T -- Scherer, A -- Quake, S R -- DA-9121/DA/NIDA NIH HHS/ -- NS-11756/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):113-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Applied Physics, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10753110" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesiveness ; *Biocompatible Materials ; Elasticity ; Materials Testing ; Pressure ; *Prostheses and Implants ; *Silicone Elastomers
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  • 40
    Publication Date: 2001-02-07
    Description: The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5'-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5'-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaguchi, K -- Ishiwata, S -- New York, N.Y. -- Science. 2001 Jan 26;291(5504):667-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, School of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11158681" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/*metabolism ; Adenosine Triphosphate/metabolism ; Adenylyl Imidodiphosphate/*metabolism ; Animals ; Cattle ; Elasticity ; Kinesin/*metabolism ; Kinetics ; Microtubules/metabolism ; Models, Biological ; Swine
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-11-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engel, J -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1785-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biphysical Chemistry, Biozentrum of the University, CH 4056 Basel, Switzerland. engel@ubaclu.unibas.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9324767" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Annelida/chemistry ; Bivalvia/chemistry ; Collagen/*chemistry/*physiology ; Elasticity ; Glycine/chemistry ; Glycosylation ; Hydra/chemistry ; Invertebrates/*chemistry/physiology ; Proline/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Tensile Strength
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-09-20
    Description: To adhere to solid surfaces, marine mussels produce byssal threads, each of which is a stiff tether at one end and a shock absorber with 160 percent extensibility at the other end. The elastic extensibility of proximal byssus is extraordinary given its construction of collagen and the limited extension (less than 10 percent) of most collagenous materials. From the complementary DNA, we deduced that the primary structure of a collagenous protein (preCol-P) predominating in the extensible proximal portion of the threads encodes an unprecedented natural block copolymer with three major domain types: a central collagen domain, flanking elastic domains, and histidine-rich terminal domains. The elastic domains have sequence motifs that strongly resemble those of elastin and the amorphous glycine-rich regions of spider silk fibroins. Byssal thread extensibility may be imparted by the elastic domains of preCol-P.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coyne, K J -- Qin, X X -- Waite, J H -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1830-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College of Marine Studies and Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9295275" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/chemistry ; Amino Acid Sequence ; Animals ; Base Sequence ; Biopolymers/chemistry ; Bivalvia/*chemistry/genetics ; Collagen/*chemistry/genetics ; DNA, Complementary ; Elasticity ; Elastin/chemistry/genetics ; Fibroins/chemistry ; Glycine/chemistry ; Histidine/chemistry ; Molecular Sequence Data ; Proline/chemistry ; Protein Conformation ; Protein Precursors/*chemistry/genetics ; Protein Structure, Secondary ; Sequence Alignment ; Serine/chemistry
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-06-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Potera, C -- New York, N.Y. -- Science. 1997 Jun 6;276(5318):1499-500.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9190686" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/*cytology/genetics ; *Biomechanical Phenomena ; Elasticity ; Hydrogels ; Magnetics ; Materials Testing ; Models, Theoretical ; Mutation ; Polyhydroxyethyl Methacrylate/analogs & derivatives/chemistry ; Silicon Dioxide/chemistry ; Solar System
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, H P -- New York, N.Y. -- Science. 1997 May 16;276(5315):1090-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, UDA. H.Erickson@cellbio.duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9173540" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Connectin ; Elasticity ; Entropy ; Immunoglobulins/chemistry ; Muscle Proteins/*chemistry/physiology ; Muscle Relaxation ; Muscle, Skeletal/chemistry/physiology ; *Protein Folding ; Protein Kinases/*chemistry/physiology ; Sarcomeres/chemistry ; Stress, Mechanical
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  • 45
    Publication Date: 1997-05-16
    Description: Titin, a giant filamentous polypeptide, is believed to play a fundamental role in maintaining sarcomeric structural integrity and developing what is known as passive force in muscle. Measurements of the force required to stretch a single molecule revealed that titin behaves as a highly nonlinear entropic spring. The molecule unfolds in a high-force transition beginning at 20 to 30 piconewtons and refolds in a low-force transition at approximately 2.5 piconewtons. A fraction of the molecule (5 to 40 percent) remains permanently unfolded, behaving as a wormlike chain with a persistence length (a measure of the chain's bending rigidity) of 20 angstroms. Force hysteresis arises from a difference between the unfolding and refolding kinetics of the molecule relative to the stretch and release rates in the experiments, respectively. Scaling the molecular data up to sarcomeric dimensions reproduced many features of the passive force versus extension curve of muscle fibers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kellermayer, M S -- Smith, S B -- Granzier, H L -- Bustamante, C -- AR-42652/AR/NIAMS NIH HHS/ -- GM-32543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 May 16;276(5315):1112-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Veterinary Comparative Anatomy, Pharmacology, and Physiology, Washington State University, Pullman, WA 99164-6520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148805" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Connectin ; Elasticity ; Entropy ; Immunoglobulins/chemistry ; Lasers ; Models, Chemical ; Muscle Contraction ; Muscle Proteins/*chemistry ; Muscle Relaxation ; Muscle, Skeletal/chemistry/physiology ; Protein Denaturation ; *Protein Folding ; Protein Kinases/*chemistry ; Stress, Mechanical
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 46
    Publication Date: 1997-05-16
    Description: Single-molecule atomic force microscopy (AFM) was used to investigate the mechanical properties of titin, the giant sarcomeric protein of striated muscle. Individual titin molecules were repeatedly stretched, and the applied force was recorded as a function of the elongation. At large extensions, the restoring force exhibited a sawtoothlike pattern, with a periodicity that varied between 25 and 28 nanometers. Measurements of recombinant titin immunoglobulin segments of two different lengths exhibited the same pattern and allowed attribution of the discontinuities to the unfolding of individual immunoglobulin domains. The forces required to unfold individual domains ranged from 150 to 300 piconewtons and depended on the pulling speed. Upon relaxation, refolding of immunoglobulin domains was observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rief, M -- Gautel, M -- Oesterhelt, F -- Fernandez, J M -- Gaub, H E -- New York, N.Y. -- Science. 1997 May 16;276(5315):1109-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl fur Angewandte Physik, Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148804" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Connectin ; Elasticity ; Entropy ; Immunoglobulins/*chemistry ; Microscopy, Atomic Force ; Monte Carlo Method ; Muscle Proteins/*chemistry ; *Protein Folding ; Protein Kinases/*chemistry ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Stress, Mechanical ; Thermodynamics
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  • 47
    Publication Date: 1996-03-29
    Description: Single linear DNA molecules were bound at multiple sites at one extremity to a treated glass cover slip and at the other to a magnetic bead. The DNA was therefore torsionally constrained. A magnetic field was used to rotate the beads and thus to coil and pull the DNA. The stretching force was determined by analysis of the Brownian fluctuations of the bead. Here the elastic behavior of individual lambda DNA molecules over- and underwound by up to 500 turns was studied. A sharp transition was discovered from a low to a high extension state at a force of approximately 0.45 piconewtons for underwound molecules and at a force of approximately 3 piconewtons for overwound ones. These transitions, probably reflecting the formation of alternative structures in stretched coiled DNA molecules, might be relevant for DNA transcription and replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strick, T R -- Allemand, J F -- Bensimon, D -- Bensimon, A -- Croquette, V -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1835-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Physique Statistique de l'ENS, associe aux universites Paris VI et VII, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596951" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda/genetics ; DNA, Superhelical/*chemistry ; DNA, Viral/chemistry ; Elasticity ; Magnetics ; *Nucleic Acid Conformation ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 48
    Publication Date: 1996-02-09
    Description: Single molecules of double-stranded DNA (dsDNA) were stretched with force-measuring laser tweezers. Under a longitudinal stress of approximately 65 piconewtons (pN), dsDNA molecules in aqueous buffer undergo a highly cooperative transition into a stable form with 5.8 angstroms rise per base pair, that is, 70% longer than B form dsDNA. When the stress was relaxed below 65 pN, the molecules rapidly and reversibly contracted to their normal contour lengths. This transition was affected by changes in the ionic strength of the medium and the water activity or by cross-linking of the two strands of dsDNA. Individual molecules of single-stranded DNA were also stretched giving a persistence length of 7.5 angstroms and a stretch modulus of 800 pN. The overstretched form may play a significant role in the energetics of DNA recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, S B -- Cui, Y -- Bustamante, C -- GM-32543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):795-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628994" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Chemistry, Physical ; DNA/*chemistry ; DNA, Single-Stranded/*chemistry ; Elasticity ; *Nucleic Acid Conformation ; Osmolar Concentration ; Physicochemical Phenomena ; Thermodynamics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):236.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569971" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/chemistry/physiology ; Amino Acid Sequence ; Connectin ; Elasticity ; Humans ; Molecular Sequence Data ; Molecular Weight ; Muscle Contraction ; Muscle Proteins/*chemistry/physiology ; Protein Kinases/*chemistry/physiology ; Sarcomeres/chemistry/physiology/ultrastructure ; *Sequence Analysis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 50
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-13
    Description: In addition to thick and thin filaments, vertebrate striated muscle contains a third filament system formed by the giant protein titin. Single titin molecules extend from Z discs to M lines and are longer than 1 micrometer. The titin filament contributes to muscle assembly and resting tension, but more details are not known because of the large size of the protein. The complete complementary DNA sequence of human cardiac titin was determined. The 82-kilobase complementary DNA predicts a 3-megadalton protein composed of 244 copies of immunoglobulin and fibronectin type III (FN3) domains. The architecture of sequences in the A band region of titin suggests why thick filament structure is conserved among vertebrates. In the I band region, comparison of titin sequences from muscles of different passive tension identifies two elements that correlate with tissue stiffness. This suggests that titin may act as two springs in series. The differential expression of the springs provides a molecular explanation for the diversity of sarcomere length and resting tension in vertebrate striated muscles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Labeit, S -- Kolmerer, B -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):293-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569978" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/chemistry/*ultrastructure ; Amino Acid Sequence ; Animals ; Connectin ; DNA, Complementary ; Elasticity ; Fibronectins/chemistry ; Humans ; Immunoglobulins/chemistry ; Molecular Sequence Data ; Muscle Contraction ; Muscle Proteins/*chemistry/physiology ; Muscle, Skeletal/*chemistry/ultrastructure ; Myocardium/*chemistry/ultrastructure ; Protein Kinases/*chemistry/physiology ; Rabbits ; Repetitive Sequences, Nucleic Acid ; Sarcomeres/chemistry/*ultrastructure
    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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