Reactive oxygen species (ROS), formed by the partial reduction of oxygen, were for a long time considered to be a byproduct of cellular metabolism. Since, increase in cellular levels of ROS results in oxidative stress leading to damage of nucleic acids, proteins, and lipids resulting in numerous pathological conditions; ROS was considered a bane for aerobic species. Hence, the discovery of NADPH oxidases (NOX), an enzyme family that specifically generates ROS as its prime product came as a surprise to redox biologists. NOX family proteins participate in various cellular functions including cell proliferation and differentiation, regulation of genes and protein expression, apoptosis, and host defence immunological response. Balanced expression and activation of NOX with subsequent production of ROS are critically important to regulate various genes and proteins to maintain homeostasis of the cell. However, dysregulation of NOX activation leading to enhanced ROS levels is associated with various pathophysiologies including diabetes, cardiovascular diseases, neurodegenerative diseases, ageing, atherosclerosis, and cancer. Although our current knowledge on NOX signifies its importance in the normal functioning of various cellular pathways; yet the choice of ROS producing enzymes which can tip the scale from homeostasis toward damage, as mediators of biological functions remain an oddity. Though the role of NOX in maintaining normal cellular functions is now deemed essential, yet its dysregulation leading to catastrophic events cannot be denied. Hence, this review focuses on the involvement of NOX enzymes in various pathological conditions imploring them as possible targets for therapies. Significance of the study The NOXs are multi‐subunit enzymes that generate ROS as a prime product. NOX generated ROS are usually regulated by various molecular factors and play a vital role in different physiological processes. The dysregulation of NOX activity is associated with pathological consequences. Recently, the dynamic proximity of NOX enzymes with different molecular signatures of pathologies has been studied extensively. It is essential to identify the precise role of NOX machinery in its niche during the progression of pathology. Although inhibition of NOX could be a promising approach for therapeutic interventions, it is critical to expand the current understanding of NOX's dynamicity and shed light on their molecular partners and regulators.

The transformation of a normal cell to cancer requires the derail of multiple pathways. Normal signaling in a cell is regulated at multiple stages by the presence of feedback loops, calibration of levels of proteins by their regulated turnover, and posttranscriptional regulation, to name a few. The tumor suppressor protein FBXO31 is a component of the SCF E3 ubiquitin ligase and is required to arrest cells at G1 following genotoxic stresses. Due to its growth-suppression activity, it is underexpressed in many cancers. However, the molecular mechanism underlying the translational regulation of FBXO31 remains unclear. Here we show that the oncogenic microRNAs miR-93 and miR-106a repress FBXO31, resulting in the upregulation of Slug, which is involved in epithelial-mesenchymal transition and cell invasion. FBXO31 targets and ubiquitylates Slug for proteasomal degradation. However, this mechanism is repressed in breast tumors where miR-93 and miR-106a are overexpressed. Our study further unravels an interesting mechanism whereby Slug drives the expression of miR-93 and miR-106a, thus establishing a positive feedback loop to maintain an invasive phenotype. Together, these results establish the presence of interplay between microRNAs and the ubiquitination machinery, which together regulate cancer cell invasion.

In response to diverse stresses, the canonical NF-κB pathway gets activated primarily to protect the cells and maintain their genomic integrity. It activates the cell cycle checkpoints allowing the cells with limited damage to restore a normal life cycle. One of the key events in activation of the canonical NF-κB pathway is the selective proteasomal degradation of IκBα. It has been previously shown that F-box protein βTRCP1 has limited role in directing the proteasomal degradation of IκBα during stress conditions. Here, we report another member of F-box family proteins, FBXO32, as a potential activator of NF-κB signaling during genotoxic stress and inflammatory response. Following genotoxic or inflammatory stress, FBXO32 is stabilized, which leads to polyubiquitination and proteasome mediated degradation of IκBα. We also found that FBXO32 is required for physiological regulation of IκBα levels in unstressed cells. Thus, we decipher the new role of FBXO32 in regulation of NF-κB signaling pathway.

Two new Zn (II)‐dicyanamide (dca) 1‐D chain coordination polymers (CPs), [Zn (LOMe)(μ1‐dca)(μ1,5‐dca)]n (1) and [Zn (LOEt)(μ1‐dca)(μ1,5‐dca)]n (2) have been successfully synthesized from bicompartmental Schiff base ligands N,N′‐Bis(3‐methoxysalicylidenimino)‐1,3‐diaminopropane (H2LOMe), N,N′‐Bis(3‐ethoxysalicylidenimino)‐1,3‐diaminoproane (H2LOEt) respectively and structurally characterized using various spectroscopic protocols like 1H NMR, IR, Raman, UV–Vis, fluorescence as well as elemental analysis, TGA, PXRD and SCXRD studies. X‐ray single crystal study revealed that both the complexes have two different geometrical arrangement of Zn metal centres with distorted square pyramidal Zn(2) and trigonal prismatic geometry Zn(1). Ab‐initio DFT (Density functional theory) has been executed at B3LYP (Becke, 3‐parameter, Lee‐Yang‐Parr) using DGDVP (Diffuse gradient double valence polarised) basis set to explain FMO (Frontier molecular orbital), TD‐DFT (Time‐dependent density functional theory) and photovoltaic efficiency in Dye Sensitized Solar Cell (DSSC). Hirshfeld surface (HS) and 2D fingerprint plot analyses are shed more light on the non‐covalent supramolecular interactions. The steady state and time‐resolved fluorescence measurements have been conducted in DMSO and solid‐state. CPs exhibited bi‐exponential decay in DMSO as well as solid‐state where fluorescence behaviors are mainly intra‐ligand (π → π*) in nature with lifetimes in the range (1.11–1.06 ns). In particular, in vitro cytotoxic activities were evaluated towards MCF7 (breast cancer) cell line, MDA‐MB‐231 (breast carcinoma) cell line and MCF10A (breast epithelial) cell line using MTT assay. CP1 had lower cytotoxic effect against MCF7 (20 μM), MDA‐MB‐231 (15 μM) cell lines in comparison with cisplatin (42.2 ± 8, 128.2 ± 7 μM). CP1 induced classical cell death apoptosis, autophagy and necrosis. Lower IC50 value of CP1 against MDA‐MB‐231 cell line provide new insights in the development of cancer therapeutics.