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During lung infection, bloodstream neutrophils (PMNs) responding to infection travel to the airspace lumen. Although successful arrival of microbicidal PMNs to the airspace is essential for host defense against inhaled pathogens, excessive accumulation of PMNs in the lung contributes to the pathogenesis of several prevalent lung disorders, including acute lung injury, bronchiectasis, and COPD. Unfortunately, there is no treatment for controlling PMN accumulation in the lung.

Immunoglobulins play a key role in the immune system. CDC has developed and tested hybridoma cell lines (monoclonal antibody (mAb) clones) for human IgG and other immunoglobulins. The mAbs generated from those hybridomas could be used as a reagent (second Ab) of anti-human immunoglobins in a diagnostic assay for SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2), the virus that causes COVID-19 (coronavirus disease 2019) and other assays that detect antigen specific antibodies from human sera.

Rotaviruses cause severe gastroenteritis in humans and animals globally. Currently, there are eight known serogroups (A-H) of rotaviruses. Group C rotavirus (GpC RV) causes sporadic cases and outbreaks of acute diarrhea in children and adults worldwide. GpC RV is also associated with diarrhea in swine. Currently, no simple and reliable diagnostic test exists for GpC RV, so disease prevalence remains unknown.

Scientists at NCATS have developed a novel Cellular Thermal Shift Assay (CETSA), named “Real-time CETSA” in which temperature-induced aggregation of proteins can be monitored in cells in real time across a range of compound concentrations and simultaneously across a temperature gradient in a high-throughput manner. Real-time CETSA streamlines the thermal shift assay and allows investigators to capture full aggregation profiles for every sample.

Scientists at NCATS have developed an analog of Methotrexate (MTX) that incorporates the proteasome-targeting properties of E3-ubiquitin ligase small molecule ligands (MTX-PROTACs) to directly bind to the MTX target dihydrofolate reductase (DHFR) and mark the protein for proteasomal degradation. This unique property may dramatically lower the therapeutic dose required in a treatment setting.

The invention includes compounds and compositions for inhibiting phosphoglycerate mutase (PGM) activity. In some examples, the compounds selectively inhibit cofactor-independent PGM (iPGM). In particular embodiments, the compounds include one or more cyclic peptides.

In the last decade, prescription opioid abuse and misuse has been a major contributor to mortality in the United States, resulting in a serious national public health crisis. Nearly 12 million Americans used prescription opioids nonmedically in 2018, with >67,000 people dying from an opioid overdose.

The technology encompasses antibodies and methods that may overcome the shortcomings of commercial checkpoint inhibitors (CPIs). Scientists at NIAID have identified MHC-I specific antibodies that selectively inhibit interactions with inhibitory leukocyte immunoglobin-like receptors (LILRs) but not T-cell receptors. Administration of the antibodies increased proliferation and activation of both innate and adaptive immune system cells, and lead to anti-tumor and anti-viral activity in an array of relevant mouse models of disease.

Feedback vasodilation by endothelium-derived nitric oxide (NO) is under the regulation of globins. NIH Researchers discovered that not only the alpha globin but also the beta globin subunits of hemoglobin are expressed in the human artery wall, with beta globin interacting directly with endothelial nitric oxide synthase (eNOS).

Cytochrome P450s catalyze the metabolism of a wide range of exogenous compounds, including drugs, industrial chemicals, environmental pollutants, and carcinogens. The 2C family of cytochrome P450 metabolizes an extensive number of drugs which include tolbutamide, S-Warfarin, mephenytoin, diazepam and taxol. The inventors cloned the cDNAs for several different CYP2J subfamily members including human CYP2J2, rat CYP2J3, mouse CYP2J5, mouse CYP2J6, and mouse CYP2J9. The recombinant proteins were expressed in insect cells.