Comparison of GHRSST SST analysis in the Arctic Ocean and Alaskan coastal waters using saildrones
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Engineering topics
Publications and source records attributed to Tang, Wenqing.
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We have examined the L-band radiometer and radar data from NASA’s Soil Moisture Active Passive (SMAP) mission for ocean research and applications. We find that the SMAP data are in excellent agreement with the geophysical model function (GMF) derived from the Aquarius data up to a wind speed of 20 ms-1. For severe wind conditions, the higher resolution data from SMAP allowed us to assess the sensitivity of L-band radiometer signals to hurricane force winds. We applied the L-band GMF to the retrieval of ocean surface wind and SSS from the SMAP data. Comparison with the European Center for Medium-Range Weather Forecasting, WindSat and RapidSCAT wind speeds suggests that SMAP’s radiometer wind speed reaches an excellent accuracy of about 1.1-1.7 ms-1 below a wind speed of 20 ms-1. We have also found that the maximum wind speed derived from the SMAP radiometer data can reach 140 knots for severe storms and are generally in good agreement with the hurricane track analysis and operational aircraft Stepped Frequency Microwave Radiometer wind speeds. The spatial patterns of the SMAP SSS agree well with climatological distributions, but exhibit several unique spatial and temporal features.
Ocean surface wind (U) is air in motion and stress (τ) is the turbulent transport of momentum between the ocean and the atmosphere. While the strong wind of a tropical cyclone (TC) causes destruction at landfall, it is the surface stress that drags down the TC. There was almost no stress measurement except in dedicated field campaigns and the stress we used was almost entirely derived from wind through a drag coefficient (C(sub D)), as defined by C(sub D) = τ / ( ρ U(exp 2)). In TC, there is difficulty in measuring strong wind and large uncertainty in the drag coefficient.
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Highlights: •β1,4GT1 interacts with EGFR both in vitro and in vivo. •β1,4GT1 co-localizes with EGFR on the cell surface. •β1,4GT1 inhibits {sup 125}I-EGF binding to EGFR. •β1,4GT1 inhibits EGF induced EGFR dimerization and phosphorylation. -- Abstract: Our previous studies showed that cell surface β1,4-galactosyltransferase 1 (β1,4GT1) negatively regulated cell survival through inhibition and modulation of the epidermal growth factor receptor (EGFR) signaling pathway in human hepatocellular carcinoma (HCC) SMMC-7721 cells. However, the underlying mechanism remains unclear. Here we demonstrated that β1,4-galactosyltransferase 1 (β1,4GT1) interacted with EGFR in vitro by GST pull-down analysis. Furthermore, we demonstrated that β1,4GT1 bound to EGFR in vivo by co-immunoprecipitation and determined the co-localization of β1,4GT1 and EGFR on the cell surface via confocal laser scanning microscopy analysis. Finally, using {sup 125}I-EGF binding experiments and Western blot analysis, we found that overexpression of β1,4GT1 inhibited {sup 125}I-EGF binding to EGFR, and consequently reduced the levels of EGFR dimerization and phosphorylation. In contrast, RNAi-mediated knockdown of β1,4GT1 increased the levels of EGFR dimerization and phosphorylation. These data suggest that cell surface β1,4GT1 interacts with EGFR and inhibits EGFR activation.