A global long-term (1981–2000) land surface temperature product for NOAA AVHRR

Land surface temperature (LST) plays an important role in the research of climate change and various land surface processes. Before 2000, global LST products with relatively high temporal and spatial resolutions are scarce, despite a variety of operational satellite LST products. In this study, a global 0.05∘×0.05∘ historical LST product is generated from NOAA advanced very-high-resolution radiometer (AVHRR) data (1981–2000), which includes three data layers: (1) instantaneous LST, a product generated by integrating several split-window algorithms with a random forest (RF-SWA); (2) orbital-drift-corrected (ODC) LST, a drift-corrected version of RF-SWA LST; and (3) monthly averages of ODC LST. For an assumed maximum uncertainty in emissivity and column water vapor content of 0.04 and 1.0 g cm−2, respectively, evaluated against the simulation dataset, the RF-SWA method has a mean bias error (MBE) of less than 0.10 K and a standard deviation (SD) of 1.10 K. To compensate for the influence of orbital drift on LST, the retrieved RF-SWA LST was normalized with an improved ODC method. The RF-SWA LST were validated with in situ LST from Surface Radiation Budget (SURFRAD) sites and water temperatures obtained from the National Data Buoy Center (NDBC). Against the in situ LST, the RF-SWA LST has a MBE of 0.03 K with a range of −1.59–2.71 K, and SD is 1.18 K with a range of 0.84–2.76 K. Since water temperature only changes slowly, the validation of ODC LST was limited to SURFRAD sites, for which the MBE is 0.54 K with a range of −1.05 to 3.01 K and SD is 3.57 K with a range of 2.34 to 3.69 K, indicating good product accuracy. As global historical datasets, the new AVHRR LST products are useful for filling the gaps in long-term LST data. Furthermore, the new LST products can be used as input to related land surface models and environmental applications. Furthermore, in support of the scientific research community, the datasets are freely available at https://doi.org/10.5281/zenodo.3934354 for RF-SWA LST (Ma et al., 2020a), https://doi.org/10.5281/zenodo.3936627 for ODC LST (Ma et al., 2020c), and https://doi.org/10.5281/zenodo.3936641 for monthly averaged LST (Ma et al., 2020b)

Importin α5 negatively regulates importin β1-mediated nuclear import of Newcastle disease virus matrix protein and viral replication and pathogenicity in chicken fibroblasts

The matrix (M) protein of Newcastle disease virus (NDV) is demonstrated to localize in the nucleus via intrinsic nuclear localization signal (NLS), but cellular proteins involved in the nuclear import of NDV M protein and the role of M's nuclear localization in the replication and pathogenicity of NDV remain unclear. In this study, importin β1 was screened to interact with NDV M protein by yeast two-hybrid screening. This interaction was subsequently confirmed by co-immunoprecipitation and pull-down assays. In vitro binding studies indicated that the NLS region of M protein and the amino acids 336–433 of importin β1 that belonged to the RanGTP binding region were important for binding. Importantly, a recombinant virus with M/NLS mutation resulted in a pathotype change of NDV and attenuated viral replication and pathogenicity in chicken fibroblasts and SPF chickens. In agreement with the binding data, nuclear import of NDV M protein in digitonin-permeabilized HeLa cells required both importin β1 and RanGTP. Interestingly, importin α5 was verified to interact with M protein through binding importin β1. However, importin β1 or importin α5 depletion by siRNA resulted in different results, which showed the obviously cytoplasmic or nuclear accumulation of M protein and the remarkably decreased or increased replication ability and pathogenicity of NDV in chicken fibroblasts, respectively. Our findings therefore demonstrate for the first time the nuclear import mechanism of NDV M protein and the negative regulation role of importin α5 in importin β1-mediated nuclear import of M protein and the replication and pathogenicity of a paramyxovirus

An acetylcholinesterase inhibition biosensor based on a reduced graphene oxide/silver nanocluster/chitosan nanocomposite for detection of organophosphorus pesticides

A sensitive electrochemical acetylcholinesterase (AChE) biosensor based on a reduced graphene oxide (rGO) and silver nanocluster (AgNC) modified glassy carbon electrode (GCE) was developed. rGO and AgNC nanomaterials with excellent conductivity, catalytic activity and biocompatibility offered an extremely hydrophilic surface, which facilitated the immobilization of AChE to fabricate the organophosphorus pesticide biosensor. Carboxylic chitosan (CChit) was used as a cross-linker to immobilize AChE on a rGO and AgNC modified GCE. The AChE biosensor showed favorable affinity to acetylthiocholine chloride (ATCl) and could catalyze the hydrolysis of ATCl. Based on the inhibition effect of organophosphorus pesticides on the AChE activity, using phoxim as a model compound, the inhibition effect of phoxim was proportional to its concentration ranging from 0.2 to 250 nM with a detection limit of 81 pM estimated at a signal-to-noise ratio of 3. The developed biosensor exhibited good sensitivity, stability and reproducibility, thus providing a promising tool for analysis of enzyme inhibitors and direct analysis of practical samples

Impact of Initialized Land Surface Temperature and Snowpack on Subseasonal to Seasonal Prediction Project, Phase I (LS4P-I): organization and experimental design

International audienc