25 research outputs found
Authentic recreation: living history and leisure
This essay considers a postmodern interpretation of the concept of authenticity and a criticism of that interpretation advanced from an ethnographic perspective. The author shows how these theoretical issues arise at American Civil War re-enactments by describing the ways by which the re-enactment community establishes authentic appearances at Civil War performances. The essay then considers the commercial activity conducted at Civil War events, and concludes by speaking to the question, posed by the postmodernists, as to whether it is possible to represent the past authentically
Accelerometry analysis of physical activity and sedentary behavior in older adults: a systematic review and data analysis
Finishing the euchromatic sequence of the human genome
The sequence of the human genome encodes the genetic instructions for human physiology, as well as rich information about human evolution. In 2001, the International Human Genome Sequencing Consortium reported a draft sequence of the euchromatic portion of the human genome. Since then, the international collaboration has worked to convert this draft into a genome sequence with high accuracy and nearly complete coverage. Here, we report the result of this finishing process. The current genome sequence (Build 35) contains 2.85 billion nucleotides interrupted by only 341 gaps. It covers ∼99% of the euchromatic genome and is accurate to an error rate of ∼1 event per 100,000 bases. Many of the remaining euchromatic gaps are associated with segmental duplications and will require focused work with new methods. The near-complete sequence, the first for a vertebrate, greatly improves the precision of biological analyses of the human genome including studies of gene number, birth and death. Notably, the human enome seems to encode only 20,000-25,000 protein-coding genes. The genome sequence reported here should serve as a firm foundation for biomedical research in the decades ahead
Authentic recreation: living history and leisure
This essay considers a postmodern interpretation of the concept of authenticity and a criticism of that interpretation advanced from an ethnographic perspective. The author shows how these theoretical issues arise at American Civil War re-enactments by describing the ways by which the re-enactment community establishes authentic appearances at Civil War performances. The essay then considers the commercial activity conducted at Civil War events, and concludes by speaking to the question, posed by the postmodernists, as to whether it is possible to represent the past authentically
Re-Presenting Disability : Activism and Agency in the Museum
"Re-Presenting Disability addresses issues surrounding disability representation in museums and galleries, a topic which is receiving much academic attention and is becoming an increasingly pressing issue for practitioners working in wide-ranging museums and related cultural organisations.
This volume of provocative and timely contributions, brings together twenty researchers, practitioners and academics from different disciplinary, institutional and cultural contexts to explore issues surrounding the cultural representation of disabled people and, more particularly, the inclusion (as well as the marked absence) of disability-related narratives in museum and gallery displays. The diverse perspectives featured in the book offer fresh ways of interrogating and understanding contemporary representational practices as well as illuminating existing, related debates concerning identity politics, social agency and organisational purposes and responsibilities, which have considerable currency within museums and museum studies." -- Publisher's website
Characterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor.
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Previous issue date: 1993New York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New York / Fundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, BrasilNew York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New YorkNew York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New YorkNew York University Medical Center. Department of Medical and Molecular Parasitology. New York, New YorkNew York University Medical Center. Department of Medical and Molecular Parasitology. New York, New YorkThe Johns Hopkins University. Department of Biological Chemistry. Baltimore, MarylandThe Johns Hopkins University. Baltimore, MarylandNew York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New YorkHere we report the presence of a trans-sialidase on the surface of Trypanosoma brucei culturederived
procyclic trypomastigotes. The enzyme is not detected in lysates of bloodstream trypomastigotes
enriched for either stumpy or slender forms. The trans-sialidase catalyzes the transfer
of ot(2-3)-linked sialic acid residues to lactose./3-galactopyranosyl residues are at least 100 times
better acceptors for sialic acid than ot-galactopyranosyl residues. In the absence of efficient acceptors,
the purified enzyme transfers sialic acid to water, i.e., it acts as a sialidase. Although the T. cruzi
and T. brucei trans-sialidases have very similar donor and acceptor specificities, they are antigenicaUy
distinct. Sodium dodecyl sulfate--polyacramide gel electrophoresis under nonreducing conditions
and silver staining of the purified trans-sialidase reveals a single band of 63 kD. When the surface
membrane of live procyclic trypomastigotes is trans-sialylated, using radioactive sialyllactose as
the donor substrate, it appears that the only sialylated surface molecule is procyclin. Pronase
treatment of live parasites removes only part of the surface sialic acid, in agreement with recent
data showing that the glycosylphosphatidylinositol anchor of procyclin is sialylated (Ferguson, M. A. J., M. Murray, H. Rutherford, and M. J. McConville. 1993. Biochem. J. In press)