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  • Polymers
  • energy economics
  • American Association for the Advancement of Science (AAAS)  (63)
  • Cambridge University Press  (2)
  • 1
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    Cambridge University Press
    Publication Date: 2022-08-09
    Description: This book is for researchers, policymakers, and practitioners who want to understand the dynamics and governance of low-carbon transitions. It shows how UK electricity, heat, and mobility systems are being reconfigured and explains the varying speed, depth, and scope of change. Available as Open Access on Cambridge Core.
    Keywords: climate change ; low-carbon energy transitions ; sustainability ; energy ; transport ; energy economics ; energy policy ; renewable energy ; environmental studies
    Language: English
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  • 2
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    Cambridge University Press
    Publication Date: 2022-08-09
    Description: This comprehensive volume focuses on the politics of fossil fuel subsidies and provides insights from numerous case studies, applying a variety of political and economic theoretical approaches. Ideal for researchers, practitioners, and students of political science, international relations, and public policy. This title is also available as Open Access.
    Keywords: energy policy ; energy economics ; environmental policy ; environmental science ; climate change ; bic Book Industry Communication::J Society & social sciences::JP Politics & government::JPS International relations ; bic Book Industry Communication::L Law::LN Laws of Specific jurisdictions::LNK Environment, transport & planning law::LNKJ Environment law ; bic Book Industry Communication::L Law::LN Laws of Specific jurisdictions::LNC Company, commercial & competition law::LNCR Energy & natural resources law ; bic Book Industry Communication::R Earth sciences, geography, environment, planning::RN The environment::RNF Environmental management ; bic Book Industry Communication::R Earth sciences, geography, environment, planning::RN The environment::RNT Social impact of environmental issues
    Language: English
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  • 3
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2016-06-24
    Description: Author: Philip Yeagle
    Keywords: Polymers
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-10-26
    Description: Katanin, a member of the AAA adenosine triphosphatase (ATPase) superfamily, uses nucleotide hydrolysis energy to sever and disassemble microtubules. Many AAA enzymes disassemble stable protein-protein complexes, but their mechanisms are not well understood. A fluorescence resonance energy transfer assay demonstrated that the p60 subunit of katanin oligomerized in an adenosine triphosphate (ATP)- and microtubule-dependent manner. Oligomerization increased the affinity of katanin for microtubules and stimulated its ATPase activity. After hydrolysis of ATP, microtubule-bound katanin oligomers disassembled microtubules and then dissociated into free katanin monomers. Coupling a nucleotide-dependent oligomerization cycle to the disassembly of a target protein complex may be a general feature of ATP-hydrolyzing AAA domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hartman, J J -- Vale, R D -- New York, N.Y. -- Science. 1999 Oct 22;286(5440):782-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Howard Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10531065" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/*metabolism ; Adenosine Triphosphate/analogs & derivatives/*metabolism ; Amino Acid Sequence ; Centrifugation, Density Gradient ; Fluorescence ; Hydrolysis ; Luminescent Proteins ; Microtubules/*metabolism ; Models, Biological ; Molecular Sequence Data ; Polymers ; Recombinant Fusion Proteins/chemistry/metabolism ; Tubulin/metabolism
    Print ISSN: 0036-8075
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-03-30
    Description: Diatoms are encased in an intricately patterned wall that consists of amorphous silica. Species-specific fabrication of this ornate biomineral enables taxonomists to identify thousands of diatom species. The molecular mechanisms that control this nanofabrication and generate the diversity of patterns is not well understood. A simple model is described, in which repeated phase separation events during wall biogenesis are assumed to produce self-similar silica patterns in smaller and smaller scales. On the basis of this single assumption, the apparently complex patterns found in the valves of the diatom genus Coscinodiscus can be predicted. Microscopic analysis of valves in statu nascendi from three different Coscinodiscus species supports the conclusions derived from the model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sumper, Manfred -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl Biochemie I, Universitat Regensburg, 93053 Regensburg, Germany. manfred.sumper@vkl.uni-regensburg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923533" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Wall/*chemistry/metabolism/ultrastructure ; Chemical Precipitation ; Diatoms/*chemistry/classification/metabolism/ultrastructure ; Microscopy, Electron, Scanning ; Models, Biological ; Morphogenesis ; Polyamines/analysis/metabolism ; Polymers ; Silicic Acid/chemistry/metabolism ; Silicon Dioxide/*chemistry/metabolism ; Species Specificity
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  • 6
    Publication Date: 2002-03-02
    Description: We report a method to generate steady coaxial jets of immiscible liquids with diameters in the range of micrometer/nanometer size. This compound jet is generated by the action of electro-hydrodynamic (EHD) forces with a diameter that ranges from tens of nanometers to tens of micrometers. The eventual jet breakup results in an aerosol of monodisperse compound droplets with the outer liquid surrounding or encapsulating the inner one. Following this approach, we have produced monodisperse capsules with diameters varying between 10 and 0.15 micrometers, depending on the running parameters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loscertales, I G -- Barrero, A -- Guerrero, I -- Cortijo, R -- Marquez, M -- Ganan-Calvo, A M -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1695-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Escuela Tecnica Superior de Ingenieros Industriales, Universidad de Malaga, Plaza El Ejido, S/N Malaga 29013, Spain. loscertales@uma.es〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872835" target="_blank"〉PubMed〈/a〉
    Keywords: *Aerosols ; Capsules ; Chemistry, Physical ; Drug Compounding/*methods ; Electric Conductivity ; Electricity ; Emulsions ; *Nanotechnology ; Olive Oil ; Particle Size ; Physicochemical Phenomena ; Plant Oils ; Polymers ; Spectrometry, Mass, Electrospray Ionization ; Water
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  • 7
    Publication Date: 2001-04-17
    Description: We report a method that uses the process of selective withdrawal of one fluid through a second immiscible fluid to coat small particles with polymer films. Fluid is withdrawn through a tube with its orifice slightly above a water-oil interface. Upon increasing the flow rate, there is a transition from a state where only oil is withdrawn to a state where the water, containing the particles to be coated and appropriate prepolymer reagents, is entrained in a thin spout along with the oil. The entrained particles eventually cause the spout interface to break, producing a thin coat of controllable thickness around each particle, which can be subsequently polymerized using chemical reagents, light, or heat. This method allows flexibility in the chemical composition and thickness of the conformal coatings.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, I -- Li, H -- Hougland, J L -- Mrksich, M -- Nagel, S R -- New York, N.Y. -- Science. 2001 Apr 13;292(5515):265-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉James Frank Institute and Department of Physics, Department of Chemistry, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11303097" target="_blank"〉PubMed〈/a〉
    Keywords: *Benzoates ; Chemistry, Physical/*methods ; Deuterium Oxide ; Microscopy, Confocal ; Microspheres ; Mineral Oil ; Papaver ; Plants, Medicinal ; *Pollen ; *Polyethylene Glycols ; Polymers ; Seeds ; Viscosity ; Water ; Zea mays
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  • 8
    Publication Date: 2001-12-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2462-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752554" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacteriophages/genetics ; Crystallization ; *Electric Conductivity ; *Microchemistry ; Miniaturization ; Mutation ; *Nanotechnology ; Polymers ; Pressure ; Selenium Compounds ; Sensitivity and Specificity ; Temperature ; Zinc Compounds
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  • 9
    Publication Date: 2000-07-06
    Description: Conducting polymers are excellent materials for actuators that are operated in aqueous media. Microactuators based on polypyrrole-gold bilayers enable large movement of structures attached to these actuators and are of particular interest for the manipulation of biological objects, such as single cells. A fabrication method for creating individually addressable and controllable polypyrrole-gold microactuators was developed. With these individually controlled microactuators, a micrometer-size manipulator, or microrobotic arm, was fabricated. This microrobotic arm can pick up, lift, move, and place micrometer-size objects within an area of about 250 micrometers by 100 micrometers, making the microrobot an excellent tool for single-cell manipulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jager, E W -- Inganas, O -- Lundstrom, I -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2335-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and Measurement Technology, Division of Applied Physics, Linkopings universitet, S-581 83, Linkoping, Sweden. edjag@ifm.liu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875911" target="_blank"〉PubMed〈/a〉
    Keywords: Benzenesulfonates ; Body Fluids ; Cytodiagnosis ; *Cytological Techniques ; Electrochemistry ; Glass ; Gold ; Humans ; Medical Laboratory Science/instrumentation/*methods ; Microelectrodes ; Micromanipulation/instrumentation/*methods ; Microspheres ; Microsurgery ; Miniaturization ; Polycyclic Compounds ; Polymers ; Polyurethanes ; Pyrroles ; *Robotics ; Silicon ; Water
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  • 10
    Publication Date: 2001-02-27
    Description: Traditionally, access to structurally defined complex carbohydrates has been very laborious. Although recent advancements in solid-phase synthesis have made the construction of complex oligosaccharides less tedious, a high level of technical expertise is still necessary to obtain the desired structures. We describe the automated chemical synthesis of several oligosaccharides on a solid-phase synthesizer. A branched dodecasaccharide was synthesized through the use of glycosyl phosphate building blocks and an octenediol functionalized resin. The target oligosaccharide was readily obtained after cleavage from the solid support. Access to certain complex oligosaccharides now has become feasible in a fashion much like the construction of oligopeptides and oligonucleotides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Plante, O J -- Palmacci, E R -- Seeberger, P H -- RR-00995/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2001 Feb 23;291(5508):1523-7. Epub 2001 Feb 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11222853" target="_blank"〉PubMed〈/a〉
    Keywords: Automation ; Carbohydrate Conformation ; Carbohydrate Sequence ; Chemistry, Organic/instrumentation/methods ; Glucans/chemical synthesis/chemistry ; Glycosylation ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Oligosaccharides/*chemical synthesis/*chemistry/isolation & purification ; Polymers ; Resins, Plant ; Temperature
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  • 11
    Publication Date: 1998-07-17
    Description: Recombinant DNA methods were used to create artificial proteins that undergo reversible gelation in response to changes in pH or temperature. The proteins consist of terminal leucine zipper domains flanking a central, flexible, water-soluble polyelectrolyte segment. Formation of coiled-coil aggregates of the terminal domains in near-neutral aqueous solutions triggers formation of a three-dimensional polymer network, with the polyelectrolyte segment retaining solvent and preventing precipitation of the chain. Dissociation of the coiled-coil aggregates through elevation of pH or temperature causes dissolution of the gel and a return to the viscous behavior that is characteristic of polymer solutions. The mild conditions under which gel formation can be controlled (near-neutral pH and near-ambient temperature) suggest that these materials have potential in bioengineering applications requiring encapsulation or controlled release of molecular and cellular species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petka, W A -- Harden, J L -- McGrath, K P -- Wirtz, D -- Tirrell, D A -- New York, N.Y. -- Science. 1998 Jul 17;281(5375):389-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA 01003, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9665877" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carrier Proteins/*chemistry/isolation & purification ; Chemistry, Physical ; Circular Dichroism ; Dimerization ; Electrolytes ; *Gels ; Genes, Synthetic ; Hydrogel ; Hydrogen-Ion Concentration ; Leucine Zippers ; Molecular Sequence Data ; Physicochemical Phenomena ; Polyethylene Glycols/*chemistry/isolation & purification ; Polymers ; *Protein Engineering ; Protein Folding ; *Protein Structure, Secondary ; Recombinant Proteins/*chemistry/isolation & purification ; Temperature ; Viscosity
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-12-06
    Description: Efficient synthetic methods required to assemble complex molecular arrays include reactions that are both selective (chemo-, regio-, diastereo-, and enantio-) and economical in atom count (maximum number of atoms of reactants appearing in the products). Methods that involve simply combining two or more building blocks with any other reactant needed only catalytically constitute the highest degree of atom economy. Transition metal-catalyzed methods that are both selective and economical for formation of cyclic structures, of great interest for biological purposes, represent an important starting point for this long-term goal. The limited availability of raw materials, combined with environmental concerns, require the highlighting of these goals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trost, B M -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1471-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, CA 94305-5080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962206" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; *Chemistry ; Isomerism ; Methylation ; Polymers
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  • 13
    Publication Date: 1990-03-30
    Description: Profilin is generally thought to regulate actin polymerization, but the observation that acidic phospholipids dissociate the complex of profilin and actin raised the possibility that profilin might also regulate lipid metabolism. Profilin isolated from platelets binds with high affinity to small clusters of phosphatidylinositol 4,5-bisphosphate (PIP2) molecules in micelles and also in bilayers with other phospholipids. The molar ratio of the complex of profilin with PIP2 is 1:7 in micelles of pure PIP2 and 1:5 in bilayers composed largely of other phospholipids. Profilin competes efficiently with platelet cytosolic phosphoinositide-specific phospholipase C for interaction with the PIP2 substrate and thereby inhibits PIP2 hydrolysis by this enzyme. The cellular concentrations and binding characteristics of these molecules are consistent with profilin being a negative regulator of the phosphoinositide signaling pathway in addition to its established function as an inhibitor of actin polymerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldschmidt-Clermont, P J -- Machesky, L M -- Baldassare, J J -- Pollard, T D -- GM 26338/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 30;247(4950):1575-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2157283" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Chromatography, Gel ; *Contractile Proteins ; Humans ; Hydrolysis ; Micelles ; Microfilament Proteins/*metabolism ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/*metabolism ; Polymers ; Profilins ; Type C Phospholipases/*antagonists & inhibitors/metabolism
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  • 14
    Publication Date: 1990-04-06
    Description: The ion distribution in an electrolyte solution in contact with a charged polymerized phospholipid membrane was directly measured with long-period x-ray standing waves. The 27-angstrom-thick lipid monolayer was supported on a tungsten/silicon mirror. X-ray standing waves were generated above the mirror surface by total external reflection of a 9.8-kiloelectron volt x-ray beam from a synchrotron undulator. The membrane surface, which contained negatively charged phosphate headgroups, was bathed in a dilute ZnCl2 solution. The concentration of Zn2+ in the condensed layer at the membrane surface and the Zn2+ distribution in the diffuse layer were measured as a function of headgroup charge. The Debye length of the diffuse layer varied between 3 and 58 angstroms. The results qualitatively agree with the Gouy-Chapman-Stern model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bedzyk, M J -- Bommarito, G M -- Caffrey, M -- Penner, T L -- DK-36849/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 6;248(4951):52-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2321026" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; *Electrochemistry ; Electrolytes ; Hydrogen-Ion Concentration ; *Membranes, Artificial ; Particle Accelerators ; Phospholipids ; Physicochemical Phenomena ; Polymers ; Solutions ; Water ; X-Rays ; Zinc/analysis
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-03-29
    Description: The dynamic process of electronic energy transfer is shown to be an important tool for probing the microstructure of molecular systems, particularly those in which donors and acceptors occupy specifically labeled sites of spatially confining host matrices. Special attention is given to analyzing the temporal behavior of the direct energy transfer reaction for systems in which the dipolar coupling is between a donor and randomly distributed acceptors. This dynamic process is dependent on two competing lengths when the donor and acceptor distribution is determined by the microstructure of the confining system: Rp, the dominant length characterizing the size of the confinement, and R0, which scales the strength of the dipolar coupling. When energy transfer processes are viewed in the context of these two competing lengths, a picture emerges of the microstructure of the confinement that is consistent with and corroborated by other structural probes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drake, J M -- Klafter, J -- Levitz, P -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1574-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Exxon Research and Engineering Company, Clinton Township, Annandale, NJ 08801.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2011737" target="_blank"〉PubMed〈/a〉
    Keywords: *Energy Transfer ; Mathematics ; Models, Biological ; *Models, Theoretical ; Polymers ; Probability
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-03-01
    Description: The challenge presented by myofibril assembly in striated muscle is to understand the molecular mechanisms by which its protein components are arranged at each level of organization. Recent advances in the genetics and cell biology of muscle development have shown that in vivo assembly of the myofilaments requires a complex array of structural and associated proteins and that organization of whole sarcomeres occurs initially at the cell membrane. These studies have been complemented by in vitro analyses of the renaturation, polymerization, and three-dimensional structure of the purified proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Epstein, H F -- Fischman, D A -- AR-32147/AR/NIAMS NIH HHS/ -- GM-33223/GM/NIGMS NIH HHS/ -- HL-42267/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1039-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1998120" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/physiology ; Amino Acid Sequence ; Animals ; Macromolecular Substances ; Molecular Sequence Data ; Morphogenesis ; Muscle Contraction ; *Muscle Development ; Muscle Proteins/*physiology ; Myofibrils/*physiology ; Myosins/physiology ; Polymers ; Sarcolemma/physiology
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-02-22
    Description: Well-defined, monodisperse, homologous series of oligonucleotides and DNA restriction fragments may now be produced and used as models of rigid and semirigid rodlike molecules in solution. Information from optical experiments on these model systems aids in the formulation and testing of theories of macromolecular dynamics in both dilute and concentrated solution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pecora, R -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):893-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stanford University, CA 94305-5080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2000490" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry ; *Models, Chemical ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/*chemistry ; Plasmids ; Polymers ; Restriction Mapping
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1319.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17823329" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biogenic Amines/*analysis ; Copper/chemistry ; *Fishes/microbiology ; *Food ; Food Contamination ; Food Microbiology ; Food Technology/*methods ; Humans ; Polymers
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  • 19
    Publication Date: 2010-07-10
    Description: Self-organization of nanoparticles is an efficient strategy for producing nanostructures with complex, hierarchical architectures. The past decade has witnessed great progress in nanoparticle self-assembly, yet the quantitative prediction of the architecture of nanoparticle ensembles and of the kinetics of their formation remains a challenge. We report on the marked similarity between the self-assembly of metal nanoparticles and reaction-controlled step-growth polymerization. The nanoparticles act as multifunctional monomer units, which form reversible, noncovalent bonds at specific bond angles and organize themselves into a colloidal polymer. We show that the kinetics and statistics of step-growth polymerization enable a quantitative prediction of the architecture of linear, branched, and cyclic self-assembled nanostructures; their aggregation numbers and size distribution; and the formation of structural isomers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Kun -- Nie, Zhihong -- Zhao, Nana -- Li, Wei -- Rubinstein, Michael -- Kumacheva, Eugenia -- 1-R01-HL077546-03A2/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2010 Jul 9;329(5988):197-200. doi: 10.1126/science.1189457.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Toronto, 80 Saint George Street, Toronto, Ontario M5S 3H6, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20616274" target="_blank"〉PubMed〈/a〉
    Keywords: Cetrimonium Compounds/chemistry ; Colloids ; Cyclization ; Gold ; Isomerism ; Kinetics ; Metal Nanoparticles/*chemistry ; Microscopy, Electron, Transmission ; Nanotechnology/methods ; Physicochemical Processes ; Polymers ; Polystyrenes/chemistry
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  • 20
    Publication Date: 2010-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2010 Oct 15;330(6002):314-5. doi: 10.1126/science.330.6002.314.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20947742" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/*administration & dosage ; Clinical Trials as Topic ; *Drug Carriers ; Humans ; Nanomedicine/methods ; *Nanoparticles ; Neoplasms/diagnosis/*drug therapy ; Polymers ; RNA, Antisense/administration & dosage ; Vaccines/administration & dosage
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  • 21
    Publication Date: 2014-02-22
    Description: The high cost of powerful, large-stroke, high-stress artificial muscles has combined with performance limitations such as low cycle life, hysteresis, and low efficiency to restrict applications. We demonstrated that inexpensive high-strength polymer fibers used for fishing line and sewing thread can be easily transformed by twist insertion to provide fast, scalable, nonhysteretic, long-life tensile and torsional muscles. Extreme twisting produces coiled muscles that can contract by 49%, lift loads over 100 times heavier than can human muscle of the same length and weight, and generate 5.3 kilowatts of mechanical work per kilogram of muscle weight, similar to that produced by a jet engine. Woven textiles that change porosity in response to temperature and actuating window shutters that could help conserve energy were also demonstrated. Large-stroke tensile actuation was theoretically and experimentally shown to result from torsional actuation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haines, Carter S -- Lima, Marcio D -- Li, Na -- Spinks, Geoffrey M -- Foroughi, Javad -- Madden, John D W -- Kim, Shi Hyeong -- Fang, Shaoli -- Jung de Andrade, Monica -- Goktepe, Fatma -- Goktepe, Ozer -- Mirvakili, Seyed M -- Naficy, Sina -- Lepro, Xavier -- Oh, Jiyoung -- Kozlov, Mikhail E -- Kim, Seon Jeong -- Xu, Xiuru -- Swedlove, Benjamin J -- Wallace, Gordon G -- Baughman, Ray H -- New York, N.Y. -- Science. 2014 Feb 21;343(6173):868-72. doi: 10.1126/science.1246906.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The 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/24558156" target="_blank"〉PubMed〈/a〉
    Keywords: *Cotton Fiber ; Humans ; Muscles/chemistry/ultrastructure ; *Nylons ; Polymers ; Porosity ; *Tensile Strength ; *Torsion, Mechanical
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-01-10
    Description: In vivo, cytoplasmic microtubules are nucleated and anchored by their minus ends at the centrosome and are believed to turn over by a mechanism termed dynamic instability: depolymerization and repolymerization at their plus ends. In cytoplasmic fragments of fish melanophores, microtubules were shown to detach from their nucleation site and depolymerize from their minus ends. Free microtubules moved toward the periphery by treadmilling-growth at one end and shortening from the opposite end. Frequent release from nucleation sites may be a general property of centrosomes and permit a minus-end mechanism of microtubule turnover and treadmilling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodionov, V I -- Borisy, G G -- GM25062/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 10;275(5297):215-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, University of Wisconsin, Madison, WI 53706, USA. ggborisy@facstaf.wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8985015" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/metabolism ; Cells, Cultured ; Centrosome/metabolism ; Cytoplasm/metabolism/ultrastructure ; Fishes ; Kinetics ; Melanophores/ultrastructure ; Microtubules/metabolism/*physiology/ultrastructure ; Movement ; Pigments, Biological/metabolism ; Polymers
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-10-06
    Description: Ste5 is a scaffold for the mitogen-activated protein kinase (MAPK) cascade components in a yeast pheromone response pathway. Ste5 also associates with Ste4, the beta subunit of a heterotrimeric guanine nucleotide-binding protein, potentially linking receptor activation to stimulation of the MAPK cascade. A RING-H2 motif at the Ste5 amino terminus is apparently essential for function because Ste5(C177S) and Ste5(C177A C180A) mutants did not rescue the mating defect of a ste5Delta cell. In vitro Ste5(C177A C180A) bound each component of the MAPK cascade, but not Ste4. Unlike wild-type Ste5, the mutant did not appear to oligomerize; however, when fused to a heterologous dimerization domain (glutathione S-transferase), the chimeric protein restored mating in an ste5Delta cell and an ste4Delta ste5Delta double mutant. Thus, the RING-H2 domain mediates Ste4-Ste5 interaction, which is a prerequisite for Ste5-Ste5 self-association and signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye, C -- Dhillon, N -- Thorner, J -- CA09041/CA/NCI NIH HHS/ -- GM21841/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, Division of Biochemistry and Molecular Biology, University of California, Berkeley, CA 94720-3202, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311911" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Carrier Proteins ; Dimerization ; Fungal Proteins/*chemistry/genetics/*metabolism ; *GTP-Binding Protein beta Subunits ; GTP-Binding Proteins/*metabolism ; Genetic Complementation Test ; Glutathione Transferase/chemistry ; *Heterotrimeric GTP-Binding Proteins ; Molecular Sequence Data ; Peptides/*physiology ; Pheromones/physiology ; Point Mutation ; Polymers ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/chemistry/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; *Signal Transduction ; Transformation, Genetic
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1997 May 23;276(5316):1195-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9182328" target="_blank"〉PubMed〈/a〉
    Keywords: Carotenoids/*chemistry ; Molecular Structure ; Optics and Photonics ; Photochemistry ; Polymers ; Spectrum Analysis
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  • 25
    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonner, R F -- Emmert-Buck, M -- Cole, K -- Pohida, T -- Chuaqui, R -- Goldstein, S -- Liotta, L A -- New York, N.Y. -- Science. 1997 Nov 21;278(5342):1481,1483.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Integrative and Medical Biophysics, National Institute of Child Health and Human Development, Bethesda, MD 20852, USA. bonner@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411767" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Separation/instrumentation/*methods ; DNA/analysis ; Gene Expression ; *Histological Techniques/instrumentation ; Humans ; *Lasers ; Microscopy ; Neoplasms/genetics ; Plastics ; Polymerase Chain Reaction ; Polymers ; Proteins/analysis ; RNA/analysis ; Software
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  • 26
    Publication Date: 1998-01-24
    Description: The electromechanical properties of a monomolecular film of poly-gamma-benzyl-L-glutamate (PBLG) 15 nanometers thick grafted at the carboxyl-terminal end to a flat aluminum surface were measured. The field-induced change in film thickness, dominated by a large inverse-piezoelectric effect, demonstrates that the "grafting-from" technique forces the chains into a parallel arrangement. The mechanical plate modulus of the film as determined by electrostriction agrees with the theoretical prediction for a single PBLG molecule along the chain axis. The experiments show that ultrathin polypeptide layers with large persistent polarization can be fabricated by the grafting approach.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaworek, T -- Neher, D -- Wegner, G -- Wieringa, R H -- Schouten, A J -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):57-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Polymerforschung, Ackermannweg 10, 55128 Mainz, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417021" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum ; Electrochemistry ; Electrodes ; Polyglutamic Acid/*analogs & derivatives/chemistry ; Polymers ; *Protein Structure, Secondary ; Spectrophotometry, Infrared
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  • 27
    Publication Date: 2002-05-11
    Description: Light-powered molecular machines are conjectured to be essential constituents of future nanoscale devices. As a model for such systems, we have synthesized a polymer of bistable photosensitive azobenzenes. Individual polymers were investigated by single-molecule force spectroscopy in combination with optical excitation in total internal reflection. We were able to optically lengthen and contract individual polymers by switching the azo groups between their trans and cis configurations. The polymer was found to contract against an external force acting along the polymer backbone, thus delivering mechanical work. As a proof of principle, the polymer was operated in a periodic mode, demonstrating for the first time optomechanical energy conversion in a single-molecule device.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hugel, Thorsten -- Holland, Nolan B -- Cattani, Anna -- Moroder, Luis -- Seitz, Markus -- Gaub, Hermann E -- New York, N.Y. -- Science. 2002 May 10;296(5570):1103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl fur Angewandte Physik & Center for Nanoscience, Ludwig-Maximilians Universitat, Amalienstrasse 54, 80799 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004125" target="_blank"〉PubMed〈/a〉
    Keywords: Azo Compounds/*chemistry ; Chemistry, Physical ; Dimethyl Sulfoxide ; *Light ; Mechanics ; Microscopy, Atomic Force ; Molecular Conformation ; Nanotechnology ; Optics and Photonics ; Peptides/*chemistry ; Photochemistry ; Physicochemical Phenomena ; Polymers ; Protein Conformation ; Software ; Spectrum Analysis ; Temperature
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  • 28
    Publication Date: 2005-10-08
    Description: A nondestructive imaging method, scanning near-field ultrasound holography (SNFUH), has been developed that provides depth information as well as spatial resolution at the 10- to 100-nanometer scale. In SNFUH, the phase and amplitude of the scattered specimen ultrasound wave, reflected in perturbation to the surface acoustic standing wave, are mapped with a scanning probe microscopy platform to provide nanoscale-resolution images of the internal substructure of diverse materials. We have used SNFUH to image buried nanostructures, to perform subsurface metrology in microelectronic structures, and to image malaria parasites in red blood cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shekhawat, Gajendra S -- Dravid, Vinayak P -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):89-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Nanotechnology.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210534" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Erythrocytes/parasitology/ultrastructure ; Holography/*methods ; Microscopy, Atomic Force/*instrumentation ; Microscopy, Scanning Probe ; *Nanostructures ; *Nanotechnology ; Plasmodium/ultrastructure ; Polymers ; *Ultrasonography
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  • 29
    Publication Date: 2004-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moghimi, S M -- Hunter, A C -- Murray, J C -- Szewczyk, A -- New York, N.Y. -- Science. 2004 Jan 30;303(5658):626-8; author reply 626-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14752144" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Azides/*chemistry ; Cations ; Drug Carriers/*metabolism ; Endocytosis ; Ethylene Oxide/chemistry/metabolism ; Hydrogen-Ion Concentration ; Lactones/chemistry/metabolism ; Lysosomes/metabolism ; *Micelles ; Nanotechnology ; Organelles/*metabolism ; PC12 Cells ; Polymers ; Rats ; Rhodamines/*chemistry ; Solubility ; Surface-Active Agents
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-10-08
    Description: Every new microscopic imaging technique reveals hidden features but also new challenges. To capture information about substructure features, especially defects and voids, in the next generation of integrated circuits, higher resolution methods of surface imaging will be required. In his Perspective, Diebold discusses results reported in the same issue by Shekhawat and Dravid in which an acoustic scanning holographic imaging technique has been extended to unprecedented spatial resolution. The method has also been used on biological cells, and the hope is that it can be developed further to obtain detailed information about the depth and elastic properties of buried features.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diebold, Alain C -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):61-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉SEMATECH, Austin, TX 78741, USA. .diebold@sematech.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210522" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Copper ; Fibroblasts/ultrastructure ; Holography/*methods ; Mice ; Microscopy, Acoustic ; Microscopy, Atomic Force/*instrumentation ; *Nanostructures ; *Nanotechnology ; Polymers ; *Ultrasonography
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  • 31
    Publication Date: 2005-09-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1810.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166496" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caprylates/blood/*chemistry/toxicity ; Carcinogens ; Fluorocarbons/blood/*chemistry/toxicity ; Humans ; Hydrocarbons ; Hydrocarbons, Fluorinated/*chemical synthesis/*chemistry/metabolism ; Methane/analogs & derivatives/chemistry ; Polymers ; Solvents ; *Textiles
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2003-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsumoto, Gary -- New York, N.Y. -- Science. 2003 Nov 28;302(5650):1492-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14645823" target="_blank"〉PubMed〈/a〉
    Keywords: Aerosols ; *Anthrax ; *Bacillus anthracis ; *Bioterrorism ; Glass ; Nanotechnology ; Particle Size ; Polymers ; Powders ; Silanes ; Silicon Dioxide ; Siloxanes ; *Spores, Bacterial ; Static Electricity ; Surface Properties ; United States
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-03-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fortin, Danielle -- New York, N.Y. -- Science. 2004 Mar 12;303(5664):1618-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, University of Ottawa, 140 Louis Pasteur, Ottawa, Ontario K1N 6N5, Canada. dfortin@uottawa.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15016984" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/chemistry/*metabolism/ultrastructure ; *Biofilms ; Cell Membrane/metabolism ; Cell Wall/metabolism ; Crystallization ; Ferric Compounds/analysis/*metabolism ; Ferritins/*chemistry/metabolism ; Ferrous Compounds/metabolism ; Geologic Sediments/*microbiology ; Hydrogen-Ion Concentration ; Microscopy, Electron ; Mining ; Oxidation-Reduction ; Polymers ; Polysaccharides, Bacterial/*chemistry/*metabolism ; Proton-Motive Force ; Spectrometry, X-Ray Emission
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  • 34
    Publication Date: 2004-03-16
    Description: Biological systems can produce extraordinary inorganic structures and morphologies. The mechanisms of synthesis are poorly understood but are of great interest for engineering novel materials. We use spectromicroscopy to show that microbially generated submicrometer-diameter iron oxyhydroxide (FeOOH) filaments contain polysaccharides, providing an explanation for the formation of akaganeite pseudo-single crystals with aspect ratios of approximately 1000:1. We infer that the cells extrude the polysaccharide strands to localize FeOOH precipitation in proximity to the cell membrane to harness the proton gradient for energy generation. Characterization of organic compounds with high spatial resolution, correlated with mineralogical information, should improve our understanding of biomineralization mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, Clara S -- De Stasio, Gelsomina -- Welch, Susan A -- Girasole, Marco -- Frazer, Bradley H -- Nesterova, Maria V -- Fakra, Sirine -- Banfield, Jillian F -- New York, N.Y. -- Science. 2004 Mar 12;303(5664):1656-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth and Planetary Science, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15016997" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/chemistry/*metabolism/ultrastructure ; *Biofilms ; Cell Membrane/metabolism ; Crystallization ; Ferric Compounds/*chemistry ; Ferritins/*chemistry/metabolism ; Ferrous Compounds/chemistry/metabolism ; Gallionellaceae/ultrastructure ; Geologic Sediments/*microbiology ; Hydrogen-Ion Concentration ; Leptothrix/ultrastructure ; Microscopy, Electron ; Mining ; Oxidation-Reduction ; Polymers ; Polysaccharides, Bacterial/*chemistry/*metabolism ; Proton-Motive Force ; Spectrometry, X-Ray Emission ; Water Microbiology
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  • 35
    Publication Date: 2003-12-03
    Description: An array of aligned carbon nanotubes (CNTs) was incorporated across a polymer film to form a well-ordered nanoporous membrane structure. This membrane structure was confirmed by electron microscopy, anisotropic electrical conductivity, gas flow, and ionic transport studies. The measured nitrogen permeance was consistent with the flux calculated by Knudsen diffusion through nanometer-scale tubes of the observed microstructure. Data on Ru(NH3)6(3+) transport across the membrane in aqueous solution also indicated transport through aligned CNT cores of the observed microstructure. The lengths of the nanotubes within the polymer film were reduced by selective electrochemical oxidation, allowing for tunable pore lengths. Oxidative trimming processes resulted in carboxylate end groups that were readily functionalized at the entrance to each CNT inner core. Membranes with CNT tips that were functionalized with biotin showed a reduction in Ru(NH3)6(3+) flux by a factor of 15 when bound with streptavidin, thereby demonstrating the ability to gate molecular transport through CNT cores for potential applications in chemical separations and sensing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hinds, Bruce J -- Chopra, Nitin -- Rantell, Terry -- Andrews, Rodney -- Gavalas, Vasilis -- Bachas, Leonidas G -- New York, N.Y. -- Science. 2004 Jan 2;303(5654):62-5. Epub 2003 Nov 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical and Materials Engineering, University of Kentucky, Lexington KY 40506, USA. bjhinds@engr.uky.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14645855" target="_blank"〉PubMed〈/a〉
    Keywords: Biotin/chemistry ; Diffusion ; Electric Conductivity ; Electrochemistry ; Ions/chemistry ; *Membranes, Artificial ; Microscopy, Electron ; Microscopy, Electron, Scanning ; *Nanotubes, Carbon ; Nitrogen/chemistry ; Oxidation-Reduction ; Polymers ; Ruthenium Compounds/chemistry ; Streptavidin/chemistry
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  • 36
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2016-04-22
    Description: Author: Phil Szuromi
    Keywords: Polymers
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  • 37
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2016-04-01
    Description: Author: Phil Szuromi
    Keywords: Polymers
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  • 38
    Publication Date: 2006-01-28
    Description: Biomass represents an abundant carbon-neutral renewable resource for the production of bioenergy and biomaterials, and its enhanced use would address several societal needs. Advances in genetics, biotechnology, process chemistry, and engineering are leading to a new manufacturing concept for converting renewable biomass to valuable fuels and products, generally referred to as the biorefinery. The integration of agroenergy crops and biorefinery manufacturing technologies offers the potential for the development of sustainable biopower and biomaterials that will lead to a new manufacturing paradigm.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ragauskas, Arthur J -- Williams, Charlotte K -- Davison, Brian H -- Britovsek, George -- Cairney, John -- Eckert, Charles A -- Frederick, William J Jr -- Hallett, Jason P -- Leak, David J -- Liotta, Charles L -- Mielenz, Jonathan R -- Murphy, Richard -- Templer, Richard -- Tschaplinski, Timothy -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):484-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA. arthur.ragauskas@chemistry.gatech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439654" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomass ; *Biotechnology ; Carbohydrate Metabolism ; *Energy-Generating Resources ; Fermentation ; Photosynthesis ; Plant Development ; Plants/genetics/*metabolism ; Polymers ; Public Policy
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-04-29
    Description: This work presents the fabrication of biologically inspired artificial compound eyes. The artificial ommatidium, like that of an insect's compound eyes, consists of a refractive polymer microlens, a light-guiding polymer cone, and a self-aligned waveguide to collect light with a small angular acceptance. The ommatidia are omnidirectionally arranged along a hemispherical polymer dome such that they provide a wide field of view similar to that of a natural compound eye. The spherical configuration of the microlenses is accomplished by reconfigurable microtemplating, that is, polymer replication using the deformed elastomer membrane with microlens patterns. The formation of polymer waveguides self-aligned with microlenses is also realized by a self-writing process in a photosensitive polymer resin. The angular acceptance is directly measured by three-dimensional optical sectioning with a confocal microscope, and the detailed optical characteristics are studied in comparison with a natural compound eye.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeong, Ki-Hun -- Kim, Jaeyoun -- Lee, Luke P -- New York, N.Y. -- Science. 2006 Apr 28;312(5773):557-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomolecular Nanotechnology Center, Berkeley Sensor and Actuator Center, Department of Bioengineering, 485 Evans Hall No. 1762, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16645090" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bees ; *Biomimetic Materials ; Dimethylpolysiloxanes ; Elastomers ; Epoxy Resins ; *Eye, Artificial ; Lens, Crystalline ; *Lenses ; Microscopy, Confocal ; *Optics and Photonics ; *Photoreceptor Cells, Invertebrate ; Polymers ; Resins, Synthetic ; Silicones ; Ultraviolet Rays ; Visual Fields
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Belotserkovskii, B P -- Johnston, B H -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):222-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539626" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry/metabolism ; High Mobility Group Proteins/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; *Nucleic Acid Denaturation ; Polymers ; Polypropylenes/*chemistry ; Repetitive Sequences, Nucleic Acid ; Surface Properties
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1339-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660115" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Inflammatory Agents/*chemical synthesis ; Catalysis ; Chemistry, Pharmaceutical/*methods ; *Drug Design ; Polymers ; Thalidomide/*analogs & derivatives/chemical synthesis/pharmacology ; Tumor Necrosis Factor-alpha/biosynthesis
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-05
    Description: Scientific and practical applications of supported lipid-protein bilayers are described. Membranes can be covalently coupled to or separated from solids by ultrathin layers of water or soft polymer cushions. The latter systems maintain the structural and dynamic properties of free bilayers, forming a class of models of biomembranes that allow the application of a manifold of surface-sensitive techniques. They form versatile models of low-dimensionality complex fluids, which can be used to study interfacial forces and wetting phenomena, and enable the design of phantom cells to explore the interplay of lock-and-key forces (such as receptor-ligand binding) and universal forces for cell adhesion. Practical applications are the design of (highly selective) receptor surfaces of biosensors on electrooptical devices or the biofunctionalization of inorganic solids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sackmann, E -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):43-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Physik Department E22 (Biophysics Laboratory) Technische Universitat Munchen, Garching, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539599" target="_blank"〉PubMed〈/a〉
    Keywords: Biosensing Techniques ; Cell Adhesion ; Diffusion ; Electrochemistry ; Ligands ; *Lipid Bilayers ; *Membranes, Artificial ; Polymers ; Proteins/*chemistry ; Receptors, Cell Surface/metabolism ; Surface Properties ; Thermodynamics
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  • 43
    Publication Date: 1993-11-12
    Description: Dimerization and oligomerization are general biological control mechanisms contributing to the activation of cell membrane receptors, transcription factors, vesicle fusion proteins, and other classes of intra- and extracellular proteins. Cell permeable, synthetic ligands were devised that can be used to control the intracellular oligomerization of specific proteins. To demonstrate their utility, these ligands were used to induce intracellular oligomerization of cell surface receptors that lacked their transmembrane and extracellular regions but contained intracellular signaling domains. Addition of these ligands to cells in culture resulted in signal transmission and specific target gene activation. Monomeric forms of the ligands blocked the pathway. This method of ligand-regulated activation and termination of signaling pathways has the potential to be applied wherever precise control of a signal transduction pathway is desired.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spencer, D M -- Wandless, T J -- Schreiber, S L -- Crabtree, G R -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1019-24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7694365" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Carrier Proteins/*metabolism ; Cross-Linking Reagents ; Gene Expression Regulation ; Heat-Shock Proteins/*metabolism ; Ligands ; Membrane Proteins/*metabolism ; Models, Biological ; Molecular Sequence Data ; Polymers ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/*metabolism ; Tacrolimus/*analogs & derivatives/chemical synthesis/chemistry/metabolism ; Tacrolimus Binding Proteins ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured
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  • 44
    Publication Date: 1994-03-18
    Description: Injectable nanoparticulate carriers have important potential applications such as site-specific drug delivery or medical imaging. Conventional carriers, however, cannot generally be used because they are eliminated by the reticulo-endothelial system within seconds or minutes after intravenous injection. To address these limitations, monodisperse biodegradable nanospheres were developed from amphiphilic copolymers composed of two biocompatible blocks. The nanospheres exhibited dramatically increased blood circulation times and reduced liver accumulation in mice. Furthermore, they entrapped up to 45 percent by weight of the drug in the dense core in a one-step procedure and could be freeze-dried and easily redispersed without additives in aqueous solutions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gref, R -- Minamitake, Y -- Peracchia, M T -- Trubetskoy, V -- Torchilin, V -- Langer, R -- GM 26698/GM/NIGMS NIH HHS/ -- U01 CA52857/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 18;263(5153):1600-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128245" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biocompatible Materials ; Biodegradation, Environmental ; *Drug Carriers/pharmacokinetics ; *Drug Compounding ; Freeze Drying ; *Lactic Acid ; Lidocaine/administration & dosage/pharmacokinetics ; Mice ; Mice, Inbred BALB C ; *Microspheres ; Polyesters ; Polyethylene Glycols ; *Polyglycolic Acid ; Polymers
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  • 45
    Publication Date: 1994-09-16
    Description: Interleukin-4 (IL-4) is an immunomodulatory cytokine secreted by activated T lymphocytes, basophils, and mast cells. It plays an important role in modulating the balance of T helper (Th) cell subsets, favoring expansion of the Th2 lineage relative to Th1. Imbalance of these T lymphocyte subsets has been implicated in immunological diseases including allergy, inflammation, and autoimmune disease. IL-4 may mediate its biological effects, at least in part, by activating a tyrosine-phosphorylated DNA binding protein. This protein has now been purified and its encoding gene cloned. Examination of the primary amino acid sequence of this protein indicates that it is a member of the signal transducers and activators of transcription (Stat) family of DNA binding proteins, hereby designated IL-4 Stat. Study of the inhibitory activities of phosphotyrosine-containing peptides derived from the intracellular domain of the IL-4 receptor provided evidence for direct coupling of receptor and transcription factor during the IL-4 Stat activation cycle. Such observations indicate that IL-4 Stat has the same functional domain for both receptor coupling and dimerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hou, J -- Schindler, U -- Henzel, W J -- Ho, T C -- Brasseur, M -- McKnight, S L -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1701-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8085155" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cloning, Molecular ; Cross-Linking Reagents ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; Humans ; Interleukin-4/*pharmacology ; Interleukin-4 Receptor alpha Subunit ; Models, Biological ; Molecular Sequence Data ; Monocytes/metabolism ; Phosphopeptides/metabolism/pharmacology ; Phosphorylation ; Polymers ; Receptors, Cell Surface ; Receptors, Interleukin-4 ; Receptors, Mitogen/*metabolism ; STAT6 Transcription Factor ; Trans-Activators/chemistry/genetics/isolation & purification/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-10-15
    Description: The Tax protein of human T cell leukemia virus type-1 (HTLV-I) transcriptionally activates the HTLV-I promoter. This activation requires binding sites for activating transcription factor (ATF) proteins, a family of cellular proteins that contain basic region-leucine zipper (bZIP) DNA binding domains. Data are presented showing that Tax increases the in vitro DNA binding activity of multiple ATF proteins. Tax also stimulated DNA binding by other bZIP proteins, but did not affect DNA binding proteins that lack a bZIP domain. The increase in DNA binding occurred because Tax promotes dimerization of the bZIP domain in the absence of DNA, and the elevated concentration of the bZIP homodimer then facilitates the DNA binding reaction. These results help explain how Tax activates viral transcription and transforms cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagner, S -- Green, M R -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):395-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211160" target="_blank"〉PubMed〈/a〉
    Keywords: Activating Transcription Factor 1 ; Activating Transcription Factor 2 ; Base Sequence ; Basic-Leucine Zipper Transcription Factors ; Binding Sites ; Cell Line ; Cell Transformation, Viral ; Cyclic AMP Response Element-Binding Protein/metabolism ; DNA/*metabolism ; DNA-Binding Proteins ; G-Box Binding Factors ; Gene Products, tax/*metabolism ; Leucine Zippers ; Molecular Sequence Data ; Oligodeoxyribonucleotides/*metabolism ; Plant Proteins ; Polymers ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/*metabolism
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-03-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1994 Mar 25;263(5154):1698-733.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8134833" target="_blank"〉PubMed〈/a〉
    Keywords: *Chemical Engineering ; *Chemistry, Physical ; *Materials Testing ; Metals ; Polymers ; Transistors, Electronic ; Zeolites
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lansbury, P T -- New York, N.Y. -- Science. 1994 Sep 9;265(5178):1510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8079159" target="_blank"〉PubMed〈/a〉
    Keywords: Polymers ; Prions/biosynthesis/*chemistry ; Protein Folding
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-10-30
    Description: A thousandfold miniaturization of immobilized optical fiber sensors, a millionfold or more sample reduction, and at least a hundredfold shorter response time, all simultaneously, were achieved by combining nanofabricated optical fiber tips with near-field photopolymerization. Specifically, pH optical fiber sensors were prepared with internal calibration, making use of the differences in both fluorescence and absorption of the acidic and basic dye species. The submicrometer sensors have excellent detection limits, as well as photostability, reversibility, and millisecond response times. Successful applications include intracellular and intraembryonic measurements. Potential applications include spatially and temporally resolved chemical analysis and kinetics inside single biological cells and their substructures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tan, W -- Shi, Z Y -- Smith, S -- Birnbaum, D -- Kopelman, R -- New York, N.Y. -- Science. 1992 Oct 30;258(5083):778-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439785" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum ; Animals ; *Biosensing Techniques ; Embryo, Mammalian ; *Fiber Optic Technology ; Hydrogen-Ion Concentration ; Microscopy/instrumentation/methods ; Miniaturization ; Optical Fibers ; Photochemistry ; Polymers ; Rats ; Spectrometry, Fluorescence ; Spectrophotometry
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  • 50
    Publication Date: 2006-01-21
    Description: Nonwoven fibrous membranes were formed from electrospinning lecithin solutions in a single processing step. As the concentration of lecithin increased, the micellar morphology evolved from spherical to cylindrical, and at higher concentrations the cylindrical micelles overlapped and entangled in a fashion similar to polymers in semi-dilute or concentrated solutions. At concentrations above the onset of entanglements of the wormlike micelles, electrospun fibers were fabricated with diameters on the order of 1 to 5 micrometers. The electrospun phospholipid fibers offer the potential for direct fabrication of biologically based, high-surface-area membranes without the use of multiple synthetic steps, complicated electrospinning designs, or postprocessing surface treatments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKee, Matthew G -- Layman, John M -- Cashion, Matthew P -- Long, Timothy E -- New York, N.Y. -- Science. 2006 Jan 20;311(5759):353-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Macromolecules and Interfaces Institute (MII), Virginia Tech, Blacksburg, VA 24061, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16424332" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Hydrogen Bonding ; *Membranes, Artificial ; *Micelles ; Phosphatidylcholines/*chemistry ; Physicochemical Phenomena ; Polymers ; Solutions ; *Static Electricity
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  • 51
    Publication Date: 2008-12-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2008 Dec 5;322(5907):1460-1. doi: 10.1126/science.322.5907.1460.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19056952" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biocompatible Materials ; Cartilage, Articular/*growth & development/transplantation ; *Chondrocytes/cytology ; Heart Diseases/therapy ; Humans ; Joint Diseases/therapy ; Ligaments ; Myocardium ; Myocytes, Cardiac/cytology/physiology ; Polymers ; *Tissue Engineering ; *Tissue Scaffolds
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2009-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perry, Joseph W -- New York, N.Y. -- Science. 2009 May 15;324(5929):892-3. doi: 10.1126/science.1174224.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Chemistry and Biochemistry and Center for Organic Photonics and Electronics, Georgia Institute of Technology, Atlanta, GA 30332, USA. joe.perry@gatech.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19443774" target="_blank"〉PubMed〈/a〉
    Keywords: *Light ; Nanotechnology/*methods ; Optics and Photonics/*methods ; *Photochemical Processes ; Photons ; Polymers
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  • 53
    Publication Date: 2012-06-23
    Description: The quantitatively minor phospholipid phosphatidylinositol (4,5)-bisphosphate [PI(4,5)P(2)] fulfills many cellular functions in the plasma membrane (PM), whereas its synthetic precursor, phosphatidylinositol 4-phosphate (PI4P), has no assigned PM roles apart from PI(4,5)P(2) synthesis. We used a combination of pharmacological and chemical genetic approaches to probe the function of PM PI4P, most of which was not required for the synthesis or functions of PI(4,5)P(2). However, depletion of both lipids was required to prevent PM targeting of proteins that interact with acidic lipids or activation of the transient receptor potential vanilloid 1 cation channel. Therefore, PI4P contributes to the pool of polyanionic lipids that define plasma membrane identity and to some functions previously attributed specifically to PI(4,5)P(2), which may be fulfilled by a more general polyanionic lipid requirement.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3646512/" 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/PMC3646512/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammond, Gerald R V -- Fischer, Michael J -- Anderson, Karen E -- Holdich, Jon -- Koteci, Ardita -- Balla, Tamas -- Irvine, Robin F -- ZIA HD000196-12/Intramural NIH HHS/ -- Biotechnology and Biological Sciences Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2012 Aug 10;337(6095):727-30. doi: 10.1126/science.1222483. Epub 2012 Jun 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK. gerald.hammond@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22722250" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Cell Membrane/*metabolism ; Cercopithecus aethiops ; Endocytosis ; HEK293 Cells ; Humans ; Membrane Proteins/metabolism ; Peptide Fragments/metabolism ; Phosphatidylinositol 4,5-Diphosphate/antagonists & ; inhibitors/biosynthesis/*metabolism ; Phosphatidylinositol Phosphates/*metabolism ; Phosphoric Monoester Hydrolases/genetics/metabolism ; Polymers ; Receptor, Muscarinic M1/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Signal Transduction ; Static Electricity ; TRPV Cation Channels/antagonists & inhibitors/metabolism
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2015-01-17
    Description: In optical microscopy, fine structural details are resolved by using refraction to magnify images of a specimen. We discovered that by synthesizing a swellable polymer network within a specimen, it can be physically expanded, resulting in physical magnification. By covalently anchoring specific labels located within the specimen directly to the polymer network, labels spaced closer than the optical diffraction limit can be isotropically separated and optically resolved, a process we call expansion microscopy (ExM). Thus, this process can be used to perform scalable superresolution microscopy with diffraction-limited microscopes. We demonstrate ExM with apparent ~70-nanometer lateral resolution in both cultured cells and brain tissue, performing three-color superresolution imaging of ~10(7) cubic micrometers of the mouse hippocampus with a conventional confocal microscope.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4312537/" 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/PMC4312537/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Fei -- Tillberg, Paul W -- Boyden, Edward S -- 1DP1NS087724/DP/NCCDPHP CDC HHS/ -- 1R01MH103910-01/MH/NIMH NIH HHS/ -- DP1 NS087724/NS/NINDS NIH HHS/ -- R01 MH103910/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2015 Jan 30;347(6221):543-8. doi: 10.1126/science.1260088. Epub 2015 Jan 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Engineering, Massachussetts Institute of Technology (MIT), Cambridge, MA, USA. ; Department of Electrical Engineering and Computer Science, MIT, Cambridge, MA, USA. ; Department of Biological Engineering, Massachussetts Institute of Technology (MIT), Cambridge, MA, USA. Media Lab, MIT, Cambridge, MA, USA. McGovern Institute, MIT, Cambridge, MA, USA. Department of Brain and Cognitive Sciences, MIT, Cambridge, MA, USA. Center for Neurobiological Engineering, MIT, Cambridge, MA, USA. esb@media.mit.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25592419" target="_blank"〉PubMed〈/a〉
    Keywords: Acrylamide ; Acrylamides ; Acrylates ; Animals ; Coated Pits, Cell-Membrane/*ultrastructure ; Fluorescent Dyes ; Gels ; HEK293 Cells ; Hippocampus/*ultrastructure ; Humans ; Mice, Inbred C57BL ; Mice, Transgenic ; Microscopy/*methods ; Microscopy, Confocal/methods ; Microscopy, Fluorescence/methods ; Microtubules/*ultrastructure ; Optical Imaging/*methods ; Polymers ; Tissue Fixation
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  • 55
    Publication Date: 1983-12-09
    Description: A synthetic heptapeptide from the amino terminus of the beta chain in human fibrin was used as an antigen to produce monoclonal antibodies that bind to fibrin even in the presence of human fibrinogen at the concentration found in plasma. As expected, the antifibrin activity was inhibited by the peptide antigen but not by a control heptapeptide. In a chicken ex vivo circulatory model for fibrin detection, intravenously administered monoclonal antibodies bound to human fibrin-coated disks placed in an extracorporeal chamber. These findings may lead to better methods for identifying deep vein and coronary artery thrombi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hui, K Y -- Haber, E -- Matsueda, G R -- HL28015/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1983 Dec 9;222(4628):1129-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6648524" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/*immunology ; Antibody Specificity ; Fibrin/*immunology ; Fibrinogen/*immunology ; Humans ; Peptide Fragments/chemical synthesis/immunology ; Polymers
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  • 56
    Publication Date: 1984-10-19
    Description: Pyrolysis mass spectrometry in combination with computerized multivariate statistical analysis enables qualitative and quantitative analysis of nonvolatile organic materials containing molecular assemblies of a complexity and size far beyond the capabilities of direct mass spectrometry. The state of the art in pyrolysis mass spectrometry techniques is illustrated through specific applications, including structural determination and quality control of synthetic polymers, quantitative analysis of polymer mixtures, classification and structural characterization of fossil organic matter, and nonsupervised numerical extraction of component patterns from complex biological samples.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meuzelaar, H L -- Windig, W -- Harper, A M -- Huff, S M -- McClennen, W H -- Richards, J M -- New York, N.Y. -- Science. 1984 Oct 19;226(4672):268-74.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6484572" target="_blank"〉PubMed〈/a〉
    Keywords: Biochemical Phenomena ; Biochemistry ; Chemical Phenomena ; Chemistry ; Coal ; Enterobacteriaceae/analysis/isolation & purification ; Hot Temperature ; Mass Spectrometry/*methods ; Polymers
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-01-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1982 Jan 22;215(4531):388-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7058323" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*blood ; *Hemoglobin, Sickle ; Humans ; Oxygen/blood ; Polymers
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 58
    Publication Date: 1982-08-06
    Description: Synthetic dopa melanin and cysteinyldopa melanin have different electron spin resonance spectra. Data are reported for mixtures of these melanins and for dopa-cysteinyldopa copolymers, which are spectroscopically similar. A simple parameterization of the spectra allows estimation of the relative amounts of (i) dopa melanin and cysteinyldopa melanin in mixtures and of (ii) dopa and cysteinyldopa incorporated into copolymers. Several natural eumelanins and pheomelanins have been characterized and shown to be copolymers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sealy, R C -- Hyde, J S -- Felix, C C -- Menon, I A -- Prota, G -- RR-01008/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 6;217(4559):545-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283638" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cysteinyldopa/metabolism ; Dihydroxyphenylalanine/metabolism ; Electron Spin Resonance Spectroscopy/*methods ; Melanins/*analysis/metabolism ; Polymers
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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hench, L L -- New York, N.Y. -- Science. 1980 May 23;208(4446):826-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6246576" target="_blank"〉PubMed〈/a〉
    Keywords: Alloys ; Animals ; *Biocompatible Materials ; Blood Vessels/anatomy & histology ; Bone and Bones/anatomy & histology ; Ceramics ; Humans ; Lactates ; *Lactic Acid ; Methylmethacrylates ; Polyglycolic Acid ; Polymers ; Prostheses and Implants ; Stress, Mechanical
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  • 60
    Publication Date: 1986-09-05
    Description: The oral administration of peptide drugs is well known to be precluded by their digestion in the stomach and small intestine. As a new approach to oral delivery, peptide drugs were coated with polymers cross-linked with azoaromatic groups to form an impervious film to protect orally administered drugs from digestion in the stomach and small intestine. When the azopolymer-coated drug reached the large intestine, the indigenous microflora reduced the azo bonds, broke the cross-links, and degraded the polymer film, thereby releasing the drug into the lumen of the colon for local action or for absorption. The ability of the azopolymer coating to protect and deliver orally administered peptide drugs was demonstrated in rats with the peptide hormones vasopressin and insulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saffran, M -- Kumar, G S -- Savariar, C -- Burnham, J C -- Williams, F -- Neckers, D C -- AI 18710/AI/NIAID NIH HHS/ -- SO-7-RR05700-15/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1081-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526553" target="_blank"〉PubMed〈/a〉
    Keywords: Administration, Oral ; Animals ; Azo Compounds ; Blood Glucose/metabolism ; Diabetes Mellitus, Experimental/drug therapy ; Enterobacteriaceae/metabolism ; Insulin/*administration & dosage ; Lypressin/administration & dosage ; Peptides/*administration & dosage ; Polymers ; Rats ; *Tablets, Enteric-Coated
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-09-25
    Description: Biomaterials are being used with increasing frequency for tissue substitution. Complex devices such as total joint replacements and the total artificial heart represent combinations of polymers and metal alloys for system and organ replacement. The major barriers to the extended use of these devices are the possibility of bacterial adhesion to biomaterials, which causes biomaterial-centered infection, and the lack of successful tissue integration or compatibility with biomaterial surfaces. Interactions of biomaterials with bacteria and tissue cells are directed not only by specific receptors and outer membrane molecules on the cell surface, but also by the atomic geometry and electronic state of the biomaterial surface. An understanding of these mechanisms is important to all fields of medicine and is derived from and relevant to studies in microbiology, biochemistry, and physics. Modifications to biomaterial surfaces at an atomic level will allow the programming of cell-to-substratum events, thereby diminishing infection by enhancing tissue compatibility or integration, or by directly inhibiting bacterial adhesion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gristina, A G -- R01AM26957-05/AM/NIADDK NIH HHS/ -- R01GM35939-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Sep 25;237(4822):1588-95.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3629258" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Adhesion ; Bacterial Infections/*microbiology ; *Biocompatible Materials ; *Cell Adhesion ; Ceramics ; Chemistry, Physical ; Glass ; Glycoproteins ; Humans ; Ions ; Physicochemical Phenomena ; Polymers ; Solubility
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-30
    Description: F-actin is the major component of muscle thin filaments and, more generally, of the microfilaments of the dynamic, multifunctional cytoskeletal systems of nonmuscle eukaryotic cells. Polymeric F-actin is formed by reversible noncovalent self-association of monomeric G-actin. To understand the dynamics of microfilament systems in cells, the dynamics of polymerization of pure actin must be understood. The following model has emerged from recent work. During the polymerization process, adenosine 5'-triphosphate (ATP) that is bound to G-actin is hydrolyzed to adenosine 5'-diphosphate (ADP) that is bound to F-actin. The hydrolysis reaction occurs on the F-actin subsequent to the polymerization reaction in two steps: cleavage of ATP followed by the slower release of inorganic phosphate (Pi). As a result, at high rates of filament growth a transient cap of ATP-actin subunits exists at the ends of elongating filaments, and at steady state a stabilizing cap of ADP.Pi-actin subunits exists at the barbed ends of filaments. Cleavage of ATP results in a highly stable filament with bound ADP.Pi, and release of Pi destabilizes the filament. Thus these two steps of the hydrolytic reaction provide potential mechanisms for regulating the monomer-polymer transition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korn, E D -- Carlier, M F -- Pantaloni, D -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):638-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3672117" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*physiology ; Actins/*physiology ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/*metabolism ; Animals ; Cytoskeleton/*physiology ; Humans ; Hydrolysis ; Kinetics ; Polymers ; Protein Binding
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-09-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1985 Sep 13;229(4718):1109-13.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4035352" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallography ; DNA, Superhelical/analysis ; *Histones ; Models, Structural ; Nucleic Acid Conformation ; *Nucleosomes ; Polymers ; X-Ray Diffraction
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  • 64
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2017-02-24
    Description: Author: Marc S. Lavine
    Keywords: Polymers
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    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 65
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2017-02-24
    Description: Polymers made of even slightly different repeat units are usually immiscible and form materials with two separate phases, like oil and water. Not only do different polymers not mix, but the interfaces between them are very sharp and mechanically weak. This lack of interfacial strength poses a very serious challenge to the recycling of blends of different polymers and, notably, polyethylene (PE) and isotactic polypropylene (iPP), the two polymers most commonly found in the industrial and domestic waste that come from packaging. If these two tough polymers are simply blended together, the resulting material is brittle and cannot be used. On page 814 of this issue, Eagan et al. (1) report that adding just 1% of a suitable block copolymer—a chain of PE connected to a chain of iPP—can create molecular stitches between the two phases and make the resulting blend as tough as iPP and PE themselves. Author: Costantino Creton
    Keywords: Polymers
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