Nearly full color emission has been achieved using quantum dot (QD)–polymer composites. The fluorescence of the resulting composites spans the entire visible range with narrow emission profiles and high photoluminescence (PL) quantum yields. Moreover, mixed colors are easily produced by controlling the mixing ratio of different sized QDs. The Figure shows end‐on rods of QD–polymer composites excited from underneath by a UV lamp.
We present the results of searches for gravitational waves from a large selection of pulsars using data from the most recent science runs (S6, VSR2 and VSR4) of the initial generation of interferometric gravitational wave detectors LIGO (Laser Interferometric Gravitational-wave Observatory) and Virgo. We do not see evidence for gravitational wave emission from any of the targeted sources but produce upper limits on the emission amplitude. We highlight the results from seven young pulsars with large spin-down luminosities. We reach within a factor of five of the canonical spin-down limit for all seven of these, whilst for the Crab and Vela pulsars we further surpass their spin-down limits. We present new or updated limits for 172 other pulsars (including both young and millisecond pulsars). Now that the detectors are undergoing major upgrades, and, for completeness, we bring together all of the most up-to-date results from all pulsars searched for during the operations of the first-generation LIGO, Virgo and GEO600 detectors. This gives a total of 195 pulsars including the most recent results described in this paper.
Synaptic vesicle fusion mediates communication between neurons and is triggered by rapid influx of Ca2+. The Ca2+-triggering step for fusion is regulated by the synaptic vesicle transmembrane protein Synaptotagmin 1 (Syt1). Syt1 contains two cytoplasmic C2 domains, termed C2A and C2B, which coordinate Ca2+ binding. Although C2A and C2B share similar topology, binding of Ca2+ ions to the C2B domain has been suggested as the only critical trigger for evoked vesicle release. If and how C2A domain function is coordinated with C2B remains unclear. In this study, we generated a panel of Syt1 chimeric constructs in Drosophila to delineate the unique and shared functions of each C2 domain in regulation of synaptic vesicle fusion. Expression of Syt 1 transgenes containing only individual C2 domains, or dual C2A-C2A or C2B-C2B chimeras, failed to restore Syt1 function in a syt1−/− null mutant background, indicating both C2A and C2B are specifically required to support fast synchronous release. Mutations that disrupted Ca2+ binding to both C2 domains failed to rescue evoked release, but supported synaptic vesicle docking and endocytosis, indicating these functions of Syt1 are Ca2+-independent. The dual C2 domain Ca2+-binding mutant also enhanced spontaneous fusion, while dramatically increasing evoked release when co-expressed with native Syt1. Taken together, these data indicate that synaptic transmission can be regulated by Syt1 multimerization, and that both C2 domains of Syt1 are uniquely required for modulating Ca2+-independent spontaneous fusion and Ca2+-dependent synchronous release.
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