991 resultados para Semiconductor junctions
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"Work Performed Under Contract No. AC02-77CH00178."
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"October 21, 1963"
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Mode of access: Internet.
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"August 1973."
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Mode of access: Internet.
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Mode of access: Internet.
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Mode of access: Internet.
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Mode of access: Internet.
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"This activity was supported by the Defense Advanced Research Projects Agency and the National Bureau of Standards."
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Includes bibliographical references (p. 14).
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Project conducted in cooperation with Minnesota Agricultural Experiment Station and St. Anthony Falls Hydraulic Laboratory of the University of Minnesota.
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Includes bibliography.
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Title varies slightly.
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"February 1991."
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The muscle isoform. of clathrin heavy chain, CHC22, has 85% sequence identity to the ubiquitously expressed CHC17, yet its expression pattern and function appear to be distinct from those of well-characterized clathrin-coated vesicles. In mature muscle CHC22 is preferentially concentrated at neuromuscular and myotendinous junctions, suggesting a role at sarcolemmal contacts with extracellular matrix. During myoblast differentiation, CHC22 expression is increased, initially localized with desmin and nestin and then preferentially segregated to the poles of fused myoblasts. CHC22 expression is also increased in regenerating muscle fibers with the same time course as embryonic myosin, indicating a role in muscle repair. CHC22 binds to sorting nexin 5 through a coiled-coil domain present in both partners, which is absent in CHC17 and coincides with the region on CHC17 that binds the regulatory light-chain subunit. These differential binding data suggest a mechanism for the distinct functions of CHC22 relative to CHC17 in membrane traffic during muscle development, repair, and at neuromuscular and myotendinous junctions.