University of Adelaide

About: University of Adelaide is a education organization based out in Adelaide, South Australia, Australia. It is known for research contribution in the topics: Population & Pregnancy. The organization has 27251 authors who have published 79167 publications receiving 2671128 citations. The organization is also known as: The University of Adelaide & Adelaide University.

Generalized Intersection Over Union: A Metric and a Loss for Bounding Box Regression

Abstract: Intersection over Union (IoU) is the most popular evaluation metric used in the object detection benchmarks. However, there is a gap between optimizing the commonly used distance losses for regressing the parameters of a bounding box and maximizing this metric value. The optimal objective for a metric is the metric itself. In the case of axis-aligned 2D bounding boxes, it can be shown that IoU can be directly used as a regression loss. However, IoU has a plateau making it infeasible to optimize in the case of non-overlapping bounding boxes. In this paper, we address the this weakness by introducing a generalized version of IoU as both a new loss and a new metric. By incorporating this generalized IoU ( GIoU) as a loss into the state-of-the art object detection frameworks, we show a consistent improvement on their performance using both the standard, IoU based, and new, GIoU based, performance measures on popular object detection benchmarks such as PASCAL VOC and MS COCO.

Graphitic carbon nitride materials: controllable synthesis and applications in fuel cells and photocatalysis

Abstract: Graphitic carbon nitrides (g-C3N4) are becoming increasingly significant due to the theoretical prediction of their unusual properties and promising applications ranging from photocatalysis, heterogeneous catalysis, to fuel cells. Recently, a variety of nanostructured and nanoporous g-C3N4 materials have been developed for a wide range of new applications. This feature article gives, at first, an overview on the synthesis of g-C3N4 nanomaterials with controllable structure and morphology, and secondly, presents and categorizes applications of g-C3N4 as multifunctional metal-free catalysts for environmental protection, energy conversion and storage. A special emphasis is placed on the potential applications of nanostructured g-C3N4 in the areas of artificial photocatalysis for hydrogen production, oxygen reduction reaction (ORR) for fuel cells, and metal-free heterogeneous catalysis. Finally, this perspective highlights crucial issues that should be addressed in the future in the aforementioned exciting research areas.

Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch.

Abstract: The hypoxia-inducible factors (HIFs) 1α and 2α are key mammalian transcription factors that exhibit dramatic increases in both protein stability and intrinsic transcriptional potency during low-oxygen stress. This increased stability is due to the absence of proline hydroxylation, which in normoxia promotes binding of HIF to the von Hippel–Lindau (VHL tumor suppressor) ubiquitin ligase. We now show that hypoxic induction of the COOH-terminal transactivation domain (CAD) of HIF occurs through abrogation of hydroxylation of a conserved asparagine in the CAD. Inhibitors of Fe(II)- and 2-oxoglutarate–dependent dioxygenases prevented hydroxylation of the Asn, thus allowing the CAD to interact with the p300 transcription coactivator. Replacement of the conserved Asn by Ala resulted in constitutive p300 interaction and strong transcriptional activity. Full induction of HIF-1α and -2α, therefore, relies on the abrogation of both Pro and Asn hydroxylation, which during normoxia occur at the degradation and COOH-terminal transactivation domains, respectively.

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

Abstract: Mammalian cells adapt to hypoxic conditions through a transcriptional response pathway mediated by the hypoxia-inducible factor, HIF. HIF transcriptional activity is suppressed under normoxic conditions by hydroxylation of an asparagine residue within its C-terminal transactivation domain, blocking association with coactivators. Here we show that the protein FIH-1, previously shown to interact with HIF, is an asparaginyl hydroxylase. Like known hydroxylase enzymes, FIH-1 is an Fe(II)-dependent enzyme that uses molecular O(2) to modify its substrate. Together with the recently discovered prolyl hydroxylases that regulate HIF stability, this class of oxygen-dependent enzymes comprises critical regulatory components of the hypoxic response pathway.