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The Type Ia supernova (SN Ia) 2014J in M82 (d~3.5 Mpc) was serendipitously discovered by S. Fossey's group on 2014 Jan. 21 UT and has been confirmed to be the nearest known SN Ia since at least SN 1986G. Although SN 2014J was not discovered until ~7 days after first light, both the Katzman Automatic Imaging Telescope at Lick Observatory and K. Itagaki obtained several prediscovery observations of SN 2014J. With these data, we are able to constrain the object's time of first light to be Jan. 14.75 UT, only 0.82+/-0.21 d before our first detection. Interestingly, we find that the light curve is well described by a varying power law, much like SN 2013dy, which makes SN 2014J the second example of a changing power law in early-time SN Ia light curves. A low-resolution spectrum taken on Jan. 23.388 UT, ~8.70 after first light, shows that SN 2014J is a heavily reddened but otherwise spectroscopically normal SN Ia.
The scope of this volume is limited to metamaterials based on microstructural phenomena involving purely mechanical interactions. In general the exotic behavior of metamaterials is obtained by using multiscale architectured internal structures: it is assumed here that at the lowest considered scale a mechanical description is sufficient. The literature in the field being enormous, only a targeted selection of mechanical metamaterials has been considered, aiming to give an analysis of the literature relevant to the specific application developed in Chapter 3.
Abstract Transition metal chemistry is essential to life, where metal binding to DNA, RNA, and proteins underpins all facets of the central dogma of biology. In this context, metals in proteins are typically studied as static active site cofactors. However, the emergence of transition metal signaling, where mobile metal pools can transiently bind to biological targets beyond active sites, is expanding this conventional view of bioinorganic chemistry. This Minireview focuses on the concept of metalloallostery, using copper as a canonical example of how metals can regulate protein function by binding to remote allosteric sites (e.g., exosites). We summarize advances in and prospects for the field, including imaging dynamic transition metal signaling pools, allosteric inhibition or activation of protein targets by metal binding, and metal‐dependent signaling pathways that underlie nutrient vulnerabilities in diseases spanning obesity, fatty liver disease, cancer, and neurodegeneration.
Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
