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  • 1
    Language: English
    In: Signs January 2011, Vol.36(2), pp.385-410
    Description: Abstract As part of a feminist commitment to collaboration, this article appears as a companion essay to Mimi Thi Nguyen’s “The Biopower of Beauty: Humanitarian Imperialisms and Global Feminisms” and offers a point of departure for thinking about fashion and beauty as processes that produce subjects recruited to, and aligned with, the national interests of the United States in the war on terror. The Muslim woman in the veil and her imagined opposite in the fashionably modern—and implicitly Western—woman become convenient metaphors for articulating geopolitical contests of power as a human rights concern, as a rescue mission, as a beautifying mandate. This article examines newer iterations of this opposition, in the wake of September 11, 2001, in order to demonstrate the critical resonance of a biopolitics on fashion and beauty. In “The Right to Fashion in the Age of Terrorism,” the author examines the relationship between the U.S. war on terror, targeting persons whose sartorial choices are described as terrorist‐looking and oppressive, and the right‐to‐fashion discourse, which promotes fashion’s mass‐market diffusion as a civil liberty. Looking at these multiple invocations of the democratization of fashion, this article argues that the right‐to‐fashion discourse colludes with the war on terror by fabricating a neoliberal consumer‐citizen who is also a couture‐citizen and whose right to fashion reasserts U.S.exceptionalism, which is secured by private property, social mobility, and individualism.
    Keywords: United States–Us ; Fashion ; Terrorism ; Feminism ; Muslims ; Women;
    ISSN: 00979740
    E-ISSN: 15456943
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  • 2
    Language: English
    In: Science, 08/31/2012, Vol.337(6098), pp.1097-1101
    Description: The classical view of DNA posits that DNA must be stiff below the persistence length l〈150 base pairs (bp)], but recent studies addressing this have yielded contradictory results. We developed a fluorescence-based, protein-free assay for studying the cyclization of single DNA molecules in real time. The assay samples the equilibrium population of a sharply bent, transient species that is entirely suppressed in single-molecule mechanical measurements and is biologically more relevant than the annealed species sampled in the traditional ligase-based assay. The looping rate has a weak length dependence between 67 and 106 bp that cannot be described by the worm-like chain model Many biologically important protein-DNA interactions that involve looping and bending of DNA below 100 bp likely use this intrinsic bendability of DNA. 10.1126/science.1224139
    Keywords: Dna -- Physiological Aspects ; Molecular Genetics -- Research ; Assaying -- Research;
    ISSN: 0036-8075
    E-ISSN: 1095-9203
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  • 3
    Language: English
    In: Science, 05/24/2013, Vol.340(6135), pp.991-994
    Description: Cell-cell and cell-matrix mechanical interactions through membrane receptors direct a wide range of cellular functions and orchestrate the development of multicellular organisms. To define the single molecular forces required to activate signaling through a ligand-receptor bond, we developed the tension gauge tether (TGT) approach in which the ligand is immobilized to a surface through a rupturable tether before receptor engagement. TGT serves as an autonomous gauge to restrict the receptor-ligand tension. Using a range of tethers with tunable tension tolerances, we show that cells apply a universal peak tension of about 40 piconewtons (pN) to single integrin-ligand bonds during initial adhesion. We find that less than 12 pN is required to activate Notch receptors. TGT can also provide a defined molecular mechanical cue to regulate cellular functions. 10.1126/science.1231041
    Keywords: Molecular Biology -- Research ; Integrins -- Physiological Aspects ; Integrins -- Health Aspects ; Cell Interactions -- Research;
    ISSN: 0036-8075
    E-ISSN: 1095-9203
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  • 4
    Language: English
    In: Science, 07/25/2014, Vol.345(6195), pp.380-381
    Description: Polymers are ubiquitous and occur in many diverse forms, including cross-linked synthetic polymers (e.g., rubber and plastic) and biopolymers such as DNA and proteins. DNA has long been used as a model system for polymer science because long, chemically well-defined DNA chains can be prepared using its ability to self-replicate, and because it can be analyzed at the single-molecule level. For instance, the relaxation dynamics of a distorted DNA molecule eventually reverting to its lowest-energy configuration have been investigated extensively (1). There has been growing interest in understanding the relaxation of spatially confined polymers. How biopolymers such as DNA and proteins behave under high spatial confinement is important because they often experience such conditions-for example, when DNA passes through a narrow pore during viral packaging or bacterial conjugation. With the advent of nanotechnology (DNA is 2 nm in diameter), it has now become possible to study the relaxation dynamics of DNA confined in one (2) and two (3) dimensions. Berndsen et al. (4) have undertaken the first characterization of DNA relaxation under extreme confinement in three dimensions. Remarkably, they find that DNA relaxation under such circumstances is slowed by a factor of more than 60,000, presenting a daunting challenge for the biological machines that need to compact DNA reliably into tight spaces.
    Keywords: Pores ; Biopolymers ; DNA ; Rubber ; Plastics ; Nanotechnology ; Miscellaneous;
    ISSN: 0036-8075
    E-ISSN: 1095-9203
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  • 5
    Language: English
    In: Proceedings of the National Academy of Sciences, 10/11/2011, Vol.108(41), pp.16865-16866
    Description: Author contributions: T.H. and S.M. wrote the paper.
    Keywords: Sciences (General);
    ISSN: 0027-8424
    E-ISSN: 1091-6490
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  • 6
    Language: English
    In: Proceedings of the National Academy of Sciences, 10/22/2013, Vol.110(43), pp.17173-17174
    Description: Author contributions: J.F. and T.H. wrote the paper.
    Keywords: Sciences (General);
    ISSN: 0027-8424
    E-ISSN: 1091-6490
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  • 7
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 2012, Vol.109(42), pp.17022-17027
    Description: Enzyme replacement therapy has been used successfully in many lysosomal storage diseases. However, correction of brain storage has been limited by the inability of infused enzyme to cross the blood–brain barrier (BBB). We recently reported that PerT-GUS, a form of β-glucuronidase (GUS) chemically modified to eliminate its uptake and clearance by carbohydrate-dependent receptors, crossed the BBB and cleared neuronal storage in an immunotolerant model of murine mucopolysaccharidosis (MPS) type VII. In this respect, the chemically modified enzyme was superior to native β-glucuronidase. Chemically modified enzyme was also delivered more effectively to heart, kidney, and muscle. However, liver and spleen, which express high levels of carbohydrate receptors, received nearly fourfold lower levels of PerT-GUS compared with native GUS. A recent report on PerT-treated sulfamidase in murine MPS IIIA confirmed enhanced delivery to other tissues but failed to observe clearance of storage in neurons. To confirm and extend our original observations, we compared the efficacy of 12 weekly i.v. infusions of PerT-GUS versus native GUS on (i) delivery of enzyme to brain; (ii) improvement in histopathology; and (iii) correction of secondary elevations of other lysosomal enzymes. Such correction is a recognized biomarker for correction of neuronal storage. PerT-GUS was superior to native GUS in all three categories. These results provide additional evidence that long-circulating enzyme, chemically modified to escape carbohydrate-mediated clearance, may offer advantages in treating MPS VII. The relevance of this approach to treat other lysosomal storage diseases that affect brain awaits confirmation. ; p. 17022-17027.
    Keywords: Therapeutics ; Heart ; Mucopolysaccharidosis ; Animal Models ; Histopathology ; Receptors ; Biomarkers ; Beta-Glucuronidase ; Mice ; Blood-Brain Barrier ; Kidneys ; Muscles ; Liver ; Spleen ; Neurons ; Brain ; Tissues
    ISSN: 0027-8424
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  • 8
    Language: English
    In: Science, 06/29/2012, Vol.336(6089), pp.1726-1729
    Description: Rrp44 (Dis3) is a key catalytic subunit of the yeast exosome complex and can processively digest structured RNA one nucleotide at a time in the 3' to 5' direction. Its motor function is powered by the energy released from the hydrolytic nuclease reaction instead of adenosine triphosphate hydrolysis as in conventional helicases. Single-molecule fluorescence analysis revealed that instead of unwinding RNA in single base pair steps, Rrp44 accumulates the energy released by multiple single nucleotide step hydrolysis reactions until about four base pairs are unwound in a burst. Kinetic analyses showed that RNA unwinding, not cleavage or strand release, determines the overall RNA degradation rate and that the unwinding step size is determined by the nonlinear elasticity of the Rrp44/RNA complex, but not by duplex stability. doi: 10.1126/science.1216848
    Keywords: Rna -- Physiological Aspects ; Ribonuclease -- Physiological Aspects ; Ribonuclease -- Genetic Aspects;
    ISSN: 0036-8075
    E-ISSN: 1095-9203
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  • 9
    Language: English
    In: Science, 04/17/2015, Vol.348(6232), pp.344-347
    Description: Engineering superenzyme functionUnderstanding how protein domains and subunits operate is critical for engineering novel functions into proteins. Arslan et al. introduced intramolecular crosslinks between two domains of the Escherichia coli helicase Rep, which unwinds DNA. By inserting linkers of different lengths, the domains can be held either "open" or "closed." The closed conformation activates the helicase, but it can also generate super-helicases capable of unzipping long stretches of DNA at high speed and with considerable force. Comstock et al. used optical tweezers and fluorescence microscopy to simultaneously measure the structure and function of the bacterial helicase UvrD. They monitored its DNA winding and unwinding activity and its shape during these activities. The motor domain also has a "closed" conformation during DNA unwinding and switches to a reversed "open" conformation during the zipping-up interaction.Science, this issue p. 344 and p. 352 Conformational control of biomolecular activities can reveal functional insights and enable the engineering of novel activities. Here we show that conformational control through intramolecular cross-linking of a helicase monomer with undetectable unwinding activity converts it into a superhelicase that can unwind thousands of base pairs processively, even against a large opposing force. A natural partner that enhances the helicase activity is shown to achieve its stimulating role also by selectively stabilizing the active conformation. Our work provides insight into the regulation of nucleic acid unwinding activity and introduces a monomeric superhelicase without nuclease activities, which may be useful for biotechnological applications.
    Keywords: Bacteria ; Crosslinking ; Winding ; Escherichia Coli ; Proteins ; Deoxyribonucleic Acid ; High Speed ; Control ; Miscellaneous Sciences (So) ; (An);
    ISSN: 0036-8075
    E-ISSN: 1095-9203
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  • 10
    Language: English
    In: American Quarterly, 2015, Vol.67(1), pp.165-188
    Keywords: Clothing Industry – Technology Application ; Visualization (Computer) – Usage
    ISSN: 0003-0678
    Source: Cengage Learning, Inc.
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