Artificial Intelligence System for Automatic Imaging, Quantification, and Identification of Arthropods in Leaf Litter and Pitfall Samples

It is well known that arthropods are the most diverse and abundant eukaryotic organisms on the planet. Museum and research collections have huge insect accumulations from expeditions conducted over history that contain specimens of both temporal and spatial value, including hundreds of thousands of species. This biodiversity data is inaccessible to the research community, resulting in a vast amount of “dark data”. The primary objective of this study is to develop an artificial intelligence-driven system for specimen identification that greatly minimizes the time and expertise required to identify specimens in atypical environments. Successful development will have profound impacts on both ecology and biodiversity sciences as it will increase the resolution for ecological studies and allow us to work through the backlog of insect collections, unlocking tremendous amounts of biodiversity data. Development of the system will address multiple challenges in deep learning, including problems associated with limited training data and moving from known domains into unknown. The cutting-edge AI solutions will be a final component in a smart specimen identification system scalable in multiple platforms and across geographic region

A polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cell

DNA double-strand breaks (DSBs) represent the most toxic DNA damage arisen from endogenous and exogenous genotoxic stresses and are known to be repaired by either homologous recombination or nonhomologous end-joining processes. Although many proteins have been identified to participate in either of the processes, the whole processes still remain elusive. Polycomb group (PcG) proteins are epigenetic chromatin modifiers involved in gene silencing, cancer development and the maintenance of embryonic and adult stem cells. By screening proteins responding to DNA damage using laser micro-irradiation, we found that PHF1, a human homolog of Drosophila polycomb-like, Pcl, protein, was recruited to DSBs immediately after irradiation and dissociated within 10 min. The accumulation at DSBs is Ku70/Ku80-dependent, and knockdown of PHF1 leads to X-ray sensitivity and increases the frequency of homologous recombination in HeLa cell. We found that PHF1 interacts physically with Ku70/Ku80, suggesting that PHF1 promotes nonhomologous end-joining processes. Furthermore, we found that PHF1 interacts with a number of proteins involved in DNA damage responses, RAD50, SMC1, DHX9 and p53, further suggesting that PHF1, besides the function in PcG, is involved in genome maintenance processes