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This collection of essays presents the history of art education from a variety of perspectives. Traditional and revisionist issues are seen from broad overviews and through specific concerns. Textual analysis, cultural transmission, and prominent philosophies are discussed. Thirteen essays include: (1) "A History of Art Education Histories" (Donald Soucy); (2) "Elizabeth P. Peabody's Quest for Art in Moral Education" (Robert J. Saunders); (3) "From Old to New Scotland: Nineteenth Century Links between Morality and Art Education" (B. Anne Wood; Donald Soucy); (4) "The Massachusetts Drawing Act of 1870: Industrial Mandate or Democratic Maneuver?" (Paul E. Bolin); (5) "South Kensington in the Farthest Colony" (F. Graeme Chalmers); (6) "Rules and Invention: From Ornament to Design in Art Education" (Mary Ann Stankiewicz); (7) "Culture for the Masses: Art Education and Progressive Reforms, 1880-1917" (Patricia M. Amburgy); (8) "Art Education in the Twentieth Century: A History of Ideas" (Arthur Efland); (9) "Memory Drawing and Visualization in the Teaching of Robert Catterson-Smith and Marion Richardson" (John Swift); (10) "Art Education Curriculum in British Columbia between the Wars: Official Prescription--Unofficial Interpretation" (Anthony W. Rogers); (11) "Educating in Contemporary Art: The First Decade of the London Institute of Contemporary Arts" (David J. Thistlewood); (12) "Cultural Factors in Art Education History: A Study of English and French Quebec, 1940-1980" (Suzanne Lemerise; Leah Sherman); and (13) "A Developmental History of Art Education" (Diana Korzenik). An index is included. (MM)

The ubiquitin-proteasome pathway has an essential role in the regulation of numerous cellular proteins, including those mediating inflammatory conditions and cancer (1-6). Intracellular proteins destined for proteolysis are first tagged with polyubiquitin chains through a cascade of enzyme-catalyzed events. These ‘marked' proteins are then degraded via the 26S proteasome in an ATP-dependent manner (7). The 26S proteasome (EC 3.4.99.46) is a large, multisubunit enzyme (MW=2000 kDa) found in high concentration in all mammalian cells. The ATP hydrolytic activity and the specific subunits that bind ubiquitin in the 26S are located within a protein complex known as the 19S subunit which caps either end of the 20S core. The ATP-independent proteolytic activity of the proteasome is contained within this central 20S core (MW=730 kDa), a multicatalytic protease that has three well characterized peptidase activities. The three peptidases: chymotryptic, tryptic, and postglutamyl peptide hydrolytic activities, are associated with three distinct subunits: β5✻, β2✻, and β1✻, respectively (8). Each site is defined by its ability to hydrolyze peptide substrates in vitro, with hydrophobic, basic or acidic amino acids in the P1 position. [ABSTRACT FROM AUTHOR]

Many classes of MEMS devices, such as those with resonant structures, capacitive readouts, and diaphragm elements, are sensitive to stresses that are exerted by their surrounding package structure. Such stresses can arise as a result of changes in temperature, ambient pressure, or relative humidity. We have demonstrated a dramatic reduction in scale factor bias over temperature for a tuning fork gyroscope by mounting it on an interposer structure within a conventional chip carrier, Fig. 1. Optimization of a MEMS sensor package for high performance subject to various constraints cannot be accomplished by analysis alone Hanson et al. [1]. There are too many unknown parameters, e.g., material properties, process conditions, and components/package interface conditions, to make this feasible. Extensive performance evaluation of packaged sensors is also prohibitively expensive and time consuming. However, recent advances in optoelectronic laser interferometric microscope (OELIM) methodology Furlong and Pryputniewicz [2] offer a considerable promise for effective optimization of the design of advanced MEMS components and MEMS packages. Using OELIM, sub-micron deformations of MEMS structures are readily measured with nanometer accuracy and very high spatial resolution over a range of environmental and functional conditions. This greatly facilitates characterization of dynamic and thermomechanical behavior of MEMS components, packages for MEMS, and other complex material structures. In this paper, the OELIM methodology, which allows noninvasive, remote, full-field-of-view measurements of deformations in near real-time, is presented and its viability for development of MEMS is discussed. Using OELIM methodology, sub-micron displacements of sensors can be readily observed and recorded over a range of operating conditions, Fig. 2. [ABSTRACT FROM AUTHOR]