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  • 1
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    Substrate stiffness-modulated registry phase correlations in cardiomyocytes map structural order to coherent beating (2015)
    Springer Nature
    Details
    Publication Date: 2015-01-21
    Description: Article Cardiomyocyte function depends on the interplay between the intracellular fibrillar organization, contraction strain and substrate stiffness. Here the authors present a model that maps the measured values of the registry striations to those of the beating strain as functions of the substrate rigidity. Nature Communications doi: 10.1038/ncomms7085 Authors: K. Dasbiswas, S. Majkut, D. E. Discher, Samuel A. Safran
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 2
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    Polymersomes: tough vesicles made from diblock copolymers (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-15
    Description: Vesicles were made from amphiphilic diblock copolymers and characterized by micromanipulation. The average molecular weight of the specific polymer studied, polyethyleneoxide-polyethylethylene (EO40-EE37), is several times greater than that of typical phospholipids in natural membranes. Both the membrane bending and area expansion moduli of electroformed polymersomes (polymer-based liposomes) fell within the range of lipid membrane measurements, but the giant polymersomes proved to be almost an order of magnitude tougher and sustained far greater areal strain before rupture. The polymersome membrane was also at least 10 times less permeable to water than common phospholipid bilayers. The results suggest a new class of synthetic thin-shelled capsules based on block copolymer chemistry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Discher, B M -- Won, Y Y -- Ege, D S -- Lee, J C -- Bates, F S -- Discher, D E -- Hammer, D A -- P01-HL18208/HL/NHLBI NIH HHS/ -- R01-HL62352-01/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1999 May 14;284(5417):1143-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Engineering and Applied Science, and Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10325219" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Lipid Bilayers/chemistry ; *Liposomes ; *Membranes, Artificial ; Molecular Weight ; Osmotic Pressure ; Permeability ; Phospholipids/chemistry ; Physicochemical Phenomena ; Polyethylenes/*chemistry ; Polymers/*chemistry ; Surface Tension
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Polymer vesicles (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-10
    Description: Vesicles are microscopic sacs that enclose a volume with a molecularly thin membrane. The membranes are generally self-directed assemblies of amphiphilic molecules with a dual hydrophilic-hydrophobic character. Biological amphiphiles form vesicles central to cell function and are principally lipids of molecular weight less than 1 kilodalton. Block copolymers that mimic lipid amphiphilicity can also self-assemble into vesicles in dilute solution, but polymer molecular weights can be orders of magnitude greater than those of lipids. Structural features of vesicles, as well as properties including stability, fluidity, and intermembrane dynamics, are greatly influenced by characteristics of the polymers. Future applications of polymer vesicles will rely on exploiting unique property-performance relations, but results to date already underscore the fact that biologically derived vesicles are but a small subset of what is physically and chemically possible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Discher, Dennis E -- Eisenberg, Adi -- New York, N.Y. -- Science. 2002 Aug 9;297(5583):967-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Engineering and Applied Science, University of Pennsylvania, Philadelphia, PA 19104-6393, USA. discher@seas.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12169723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane ; Chemistry, Physical ; Hydrophobic and Hydrophilic Interactions ; *Membranes, Artificial ; Micelles ; Molecular Weight ; Physicochemical Phenomena ; *Polymers/chemistry ; Proteins/chemistry ; Solvents ; Surface-Active Agents
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Forced unfolding of proteins within cells (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-08-04
    Description: To identify cytoskeletal proteins that change conformation or assembly within stressed cells, in situ labeling of sterically shielded cysteines with fluorophores was analyzed by fluorescence imaging, quantitative mass spectrometry, and sequential two-dye labeling. Within red blood cells, shotgun labeling showed that shielded cysteines in the two isoforms of the cytoskeletal protein spectrin were increasingly labeled as a function of shear stress and time, indicative of forced unfolding of specific domains. Within mesenchymal stem cells-as a prototypical adherent cell-nonmuscle myosin IIA and vimentin are just two of the cytoskeletal proteins identified that show differential labeling in tensed versus drug-relaxed cells. Cysteine labeling of proteins within live cells can thus be used to fluorescently map out sites of molecular-scale deformation, and the results also suggest means to colocalize signaling events such as phosphorylation with forced unfolding.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2741095/" 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/PMC2741095/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, Colin P -- Tang, Hsin-Yao -- Carag, Christine -- Speicher, David W -- Discher, Dennis E -- R01 EB007049/EB/NIBIB NIH HHS/ -- R01 EB007049-01/EB/NIBIB NIH HHS/ -- R01 EB007049-02/EB/NIBIB NIH HHS/ -- R01 EB007049-03/EB/NIBIB NIH HHS/ -- R01 HL062352/HL/NHLBI NIH HHS/ -- R01 HL062352-09A1/HL/NHLBI NIH HHS/ -- R21 AR056128/AR/NIAMS NIH HHS/ -- R21 AR056128-01A1/AR/NIAMS NIH HHS/ -- R21 AR056128-02/AR/NIAMS NIH HHS/ -- S10 RR022575/RR/NCRR NIH HHS/ -- S10 RR022575-01A1/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2007 Aug 3;317(5838):663-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biophysical Engineering Lab, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17673662" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatography, Liquid ; Cysteine/chemistry ; Cytoskeletal Proteins/*chemistry ; Erythrocytes/*chemistry ; Fluorescence ; Fluorescent Antibody Technique ; Fluorescent Dyes ; Heterocyclic Compounds with 4 or More Rings/pharmacology ; Humans ; Mesenchymal Stromal Cells/*chemistry ; Naphthalenesulfonates ; Nonmuscle Myosin Type IIA/chemistry ; *Protein Conformation ; *Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Spectrin/chemistry ; Stress, Mechanical ; Tandem Mass Spectrometry ; Temperature ; Vimentin/chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Growth factors, matrices, and forces combine and control stem cells (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-06-27
    Description: Stem cell fate is influenced by a number of factors and interactions that require robust control for safe and effective regeneration of functional tissue. Coordinated interactions with soluble factors, other cells, and extracellular matrices define a local biochemical and mechanical niche with complex and dynamic regulation that stem cells sense. Decellularized tissue matrices and synthetic polymer niches are being used in the clinic, and they are also beginning to clarify fundamental aspects of how stem cells contribute to homeostasis and repair, for example, at sites of fibrosis. Multifaceted technologies are increasingly required to produce and interrogate cells ex vivo, to build predictive models, and, ultimately, to enhance stem cell integration in vivo for therapeutic benefit.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2847855/" 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/PMC2847855/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Discher, Dennis E -- Mooney, David J -- Zandstra, Peter W -- R37 DE013033/DE/NIDCR NIH HHS/ -- R37 DE013033-12/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 2009 Jun 26;324(5935):1673-7. doi: 10.1126/science.1171643.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biophysical Engineering and Nanobiopolymers Laboratory, School of Engineering and Applied Science, University of Pennsylvania, Philadelphia, PA 19104, USA. discher@seas.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19556500" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Adhesion ; Cell Differentiation ; Cell Proliferation ; Cell Survival ; Extracellular Matrix/*physiology ; Fibrosis ; Humans ; Intercellular Signaling Peptides and Proteins/*metabolism/pharmacology ; Stem Cell Niche/*physiology ; Stem Cell Transplantation ; Stem Cells/*cytology/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Minimal "Self" peptides that inhibit phagocytic clearance and enhance delivery of nanoparticles (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-02-23
    Description: Foreign particles and cells are cleared from the body by phagocytes that must also recognize and avoid clearance of "self" cells. The membrane protein CD47 is reportedly a "marker of self" in mice that impedes phagocytosis of self by signaling through the phagocyte receptor CD172a. Minimal "Self" peptides were computationally designed from human CD47 and then synthesized and attached to virus-size particles for intravenous injection into mice that express a CD172a variant compatible with hCD47. Self peptides delay macrophage-mediated clearance of nanoparticles, which promotes persistent circulation that enhances dye and drug delivery to tumors. Self-peptide affinity for CD172a is near the optimum measured for human CD172a variants, and Self peptide also potently inhibits nanoparticle uptake mediated by the contractile cytoskeleton. The reductionist approach reveals the importance of human Self peptides and their utility in enhancing drug delivery and imaging.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3966479/" 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/PMC3966479/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodriguez, Pia L -- Harada, Takamasa -- Christian, David A -- Pantano, Diego A -- Tsai, Richard K -- Discher, Dennis E -- 8UL1TR000003/TR/NCATS NIH HHS/ -- P01-DK032094/DK/NIDDK NIH HHS/ -- P30-DK090969/DK/NIDDK NIH HHS/ -- R01 EB007049/EB/NIBIB NIH HHS/ -- R01 HL062352/HL/NHLBI NIH HHS/ -- R01-EB007049/EB/NIBIB NIH HHS/ -- R01-HL062352/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2013 Feb 22;339(6122):971-5. doi: 10.1126/science.1229568.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular and Cell Biophysics and NanoBioPolymers Laboratory, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23430657" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD47/chemistry/immunology/metabolism ; Antigens, Differentiation/*metabolism ; Antineoplastic Agents/administration & dosage ; Autoantigens ; Blood Circulation ; Diagnostic Imaging/methods ; Drug Delivery Systems/*methods ; Humans ; Mice ; Mice, Inbred NOD ; Mice, SCID ; *Nanoparticles/administration & dosage/analysis ; Neoplasms/chemistry/diagnosis/drug therapy ; Paclitaxel/administration & dosage ; Particle Size ; Peptide Fragments/chemical synthesis/chemistry/immunology/*metabolism ; Phagocytes/immunology/metabolism ; *Phagocytosis ; Receptors, Immunologic/immunology/*metabolism ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Tissue cells feel and respond to the stiffness of their substrate (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 8
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    Materials science: Bubble wrap of cell-like aggregates (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-03-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harada, Takamasa -- Discher, Dennis E -- England -- Nature. 2011 Mar 10;471(7337):172-3. doi: 10.1038/471172a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21390121" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Artificial Cells/*chemistry ; Biomimetics/methods ; Capsules/chemical synthesis/chemistry ; Cell Adhesion ; Chloroform/chemistry ; Emulsions/*chemistry ; Hexanes/chemistry ; Hydrophobic and Hydrophilic Interactions ; Microfluidic Analytical Techniques ; Oils/chemistry ; Polymerization ; Solubility ; Solvents/chemistry ; Surface-Active Agents/chemistry ; Water/chemistry
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 9
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    Molecular maps of red cell deformation: hidden elasticity and in situ connectivity (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-11
    Description: Fluorescence-imaged micropipette aspiration was used to map redistribution of the proteins and lipids in highly extended human red blood cell membranes. Whereas the fluid bilayer distributed uniformly (+/- 10 percent), the underlying, solidlike cytoskeleton of spectrin, actin, and protein 4.1 exhibited a steep gradient in density along the aspirated projection, which was reversible on release from deformation. Quantitation of the cytoskeletal protein density gradients showed that skeletal elasticity is well represented by a grafted polymer network with a ratio of surface dilation modulus to shear modulus of approximately 2:1. Fractionally mobile integral proteins, such as band 3, and highly mobile receptors, such as CD59 as well as glycophorin C in protein 4.1-deficient cells, appeared to be squeezed out of areas dense in the underlying network and enriched in areas of network dilation. This complementary segregation demonstrates patterning of cell surface components by cytoskeletal dilation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Discher, D E -- Mohandas, N -- Evans, E A -- P01 DK32094-09/DK/NIDDK NIH HHS/ -- R01 DK26263-15/DK/NIDDK NIH HHS/ -- R01 HL31579-13/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1032-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Joint Graduate Group in Bioengineering, University of California, Berkeley, San Francisco 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973655" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/blood ; Anion Exchange Protein 1, Erythrocyte/analysis ; Blood Proteins/*analysis ; *Cytoskeletal Proteins ; Cytoskeleton/chemistry/*physiology ; Elasticity ; *Erythrocyte Deformability ; Erythrocyte Membrane/*chemistry/physiology ; Erythrocytes/chemistry/cytology/*physiology ; Glycophorin/analysis ; Glycosylphosphatidylinositols/blood ; Humans ; Lipid Bilayers ; Membrane Lipids/*blood ; Membrane Proteins/analysis ; Microscopy, Fluorescence ; *Neuropeptides ; Spectrin/analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Multiscale mechanics of fibrin polymer: gel stretching with protein unfolding and loss of water (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-08
    Description: Blood clots and thrombi consist primarily of a mesh of branched fibers made of the protein fibrin. We propose a molecular basis for the marked extensibility and negative compressibility of fibrin gels based on the structural and mechanical properties of clots at the network, fiber, and molecular levels. The force required to stretch a clot initially rises linearly and is accompanied by a dramatic decrease in clot volume and a peak in compressibility. These macroscopic transitions are accompanied by fiber alignment and bundling after forced protein unfolding. Constitutive models are developed to integrate observations at spatial scales that span six orders of magnitude and indicate that gel extensibility and expulsion of water are both manifestations of protein unfolding, which is not apparent in other matrix proteins such as collagen.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2846107/" 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/PMC2846107/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, Andre E X -- Litvinov, Rustem I -- Discher, Dennis E -- Purohit, Prashant K -- Weisel, John W -- HL090774/HL/NHLBI NIH HHS/ -- HL30954/HL/NHLBI NIH HHS/ -- HL62352/HL/NHLBI NIH HHS/ -- R01 HL030954/HL/NHLBI NIH HHS/ -- R01 HL030954-24/HL/NHLBI NIH HHS/ -- R01 HL090774/HL/NHLBI NIH HHS/ -- R01 HL090774-01A2/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2009 Aug 7;325(5941):741-4. doi: 10.1126/science.1172484.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19661428" target="_blank"〉PubMed〈/a〉
    Keywords: Biopolymers/chemistry ; *Blood Coagulation ; Fibrin/*chemistry ; Fibrinogen/chemistry ; Gels ; Humans ; Mechanical Phenomena ; Microscopy, Electron ; Models, Molecular ; Protein Folding ; Stress, Mechanical ; Water/chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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