In this paper, we study current and upcoming frontiers across the landscape of skeleton-based human action recognition. To begin with, we benchmark state-of-the-art models on the NTU-120 dataset and provide multi-layered assessment of the results. To examine skeleton action recognition 'in the wild', we introduce Skeletics-152, a curated and 3-D pose-annotated subset of RGB videos sourced from Kinetics-700, a large-scale action dataset. The results from benchmarking the top performers of NTU-120 on Skeletics-152 reveal the challenges and domain gap induced by actions 'in the wild'. We extend our study to include out-of-context actions by introducing Skeleton-Mimetics, a dataset derived from the recently introduced Mimetics dataset. Finally, as a new frontier for action recognition, we introduce Metaphorics, a dataset with caption-style annotated YouTube videos of the popular social game Dumb Charades and interpretative dance performances. Overall, our work characterizes the strengths and limitations of existing approaches and datasets. It also provides an assessment of top-performing approaches across a spectrum of activity settings and via the introduced datasets, proposes new frontiers for human action recognition.
A selenium-binding protein (SeBP) from Methanococcus vannielii was recently identified, and its gene was isolated and overexpressed in Escherichia coli [Self, W. T., Pierce, R. & Stadtman, T. C. (2004) IUBMB Life 56, 501-507]. SeBP and recombinant SeBP (rSeBP) migrated as approximately 42-kDa species on native gels and as approximately 33-kDa species on SDS gels. rSeBP consists of identical 8.8-kDa subunits, each containing a single cysteine residue. rSeBP isolated in the absence of reducing agents contained oxidized cysteine (89%) and very little bound selenium (0.05 eq or less per subunit). Complete reduction of the oxidized cysteine residues in rSeBP with Tris(2-carboxyethyl)phosphine required addition of a denaturant, such as 1 M guanidine-hydrochloride. With selenite as the selenium source and the isolated reduced protein as sole reductant, binding of one selenium per tetramer under anaerobic conditions required four cysteine thiol groups, one on each subunit. In the corresponding reaction, with reduced glutathione (GSH), equimolar amounts of selenodiglutathione (GSSeSG) and glutathione disulfide are formed from selenite and 4 GSH. At GSH-to-selenite ratios >4:1, conversion of GSSeSG to a perselenide derivative, GSSe(-), occurs. However, with the reduced rSeBP as sole electron donor in the reaction with selenite, further conversion of the R-SSeS-R product apparently did not occur. Prior alkylation of the cysteine thiol groups in reduced rSeBP prevented selenite reduction and selenium binding under comparable conditions.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.