This study reports the feasibility of recycled polyvinylidene difluoride (PVDF) beads to decolourize methylene blue (MB) from aqueous streams. The beads were characterized using scanning electron microscopy (SEM), X-ray powder diffraction (XRD), thermogravimetric analysis (TGA), and Fourier transform infrared spectroscopy (FT-IR) for its morphological and structural analysis. The effect of various process parameters such as adsorbent dose, initial concentration, contact time, and pH was studied.
View Article and Find Full Text PDFBackground: Endodontically treated teeth with extensive loss of tooth structure lacks sufficient support for a permanent restoration. While restoring them with post and core it is important not to disrupt the apical seal.
Aim: Evaluation of apical leakage after immediate and delayed postspace preparation using two root canal sealers.
Dynamic protein interaction networks such as DNA double-strand break (DSB) signaling are modulated by post-translational modifications. The DNA repair factor 53BP1 is a rare example of a protein whose post-translational modification-binding function can be switched on and off. 53BP1 is recruited to DSBs by recognizing histone lysine methylation within chromatin, an activity directly inhibited by the 53BP1-binding protein TIRR.
View Article and Find Full Text PDFBackground: The aim of the study was to determine the root canal morphology of permanent mandibular incisor teeth in the Indian subpopulation with the use of cone beam computed tomography (CBCT).
Material/methods: CBCT images of 200 patients with 800 permanent mandibular incisors, fulfilling necessary inclusion criteria and aged 18 to 60 years were evaluated. The number of roots, number of root canals and canal configuration were investigated and then classified according to Vertucci's classification of root canals.
P53-binding protein 1 (53BP1) is a multi-functional double-strand break repair protein that is essential for class switch recombination in B lymphocytes and for sensitizing BRCA1-deficient tumours to poly-ADP-ribose polymerase-1 (PARP) inhibitors. Central to all 53BP1 activities is its recruitment to double-strand breaks via the interaction of the tandem Tudor domain with dimethylated lysine 20 of histone H4 (H4K20me2). Here we identify an uncharacterized protein, Tudor interacting repair regulator (TIRR), that directly binds the tandem Tudor domain and masks its H4K20me2 binding motif.
View Article and Find Full Text PDFIntra-erythrocytic growth of malaria parasite is known to induce redox stress. In addition to haem degradation which generates reactive oxygen species (ROS), the parasite is also thought to efflux redox active homocysteine. To understand the basis underlying accumulation of homocysteine, we have examined the transsulphuration (TS) pathway in the parasite, which is known to convert homocysteine to cysteine in higher eukaryotes.
View Article and Find Full Text PDFDue to emerging resistance there is a steady need for new antimalarial drugs. Here, we report a new class of water soluble, non-toxic compounds, aryl-alkyl-lysines, with promising activity against the ring stage of . The optimal compound perturbed the plasma membrane potential and the digestive vacuole of parasites.
View Article and Find Full Text PDFThe malaria parasite experiences a significant amount of redox stress during its growth in human erythrocytes and heavily relies on secretory functions for pathogenesis. Most certainly, the parasite is equipped with machinery to tackle perturbations in the secretory pathway, like the unfolded protein response pathway in higher eukaryotes. Our bioinformatics analysis revealed the complete absence of genes involved in the canonical unfolded protein response pathway in Plasmodium falciparum.
View Article and Find Full Text PDFBackground: Heat shock factor binding protein (HSBP) was originally discovered in a yeast two-hybrid screen as an interacting partner of heat shock factor (HSF). It appears to be conserved in all eukaryotes studied so far, with yeast being the only exception. Cell biological analysis of HSBP in mammals suggests its role as a negative regulator of heat shock response as it appears to interact with HSF only during the recovery phase following exposure to heat stress.
View Article and Find Full Text PDFHost cell remodelling is a hallmark of malaria pathogenesis. It involves protein folding, unfolding and trafficking events and thus participation of chaperones such as Hsp70s and Hsp40s is well speculated. Until recently, only Hsp40s were thought to be the sole representative of the parasite chaperones in the exportome.
View Article and Find Full Text PDFCell surface structures termed knobs are one of the most important pathogenesis related protein complexes deployed by the malaria parasite Plasmodium falciparum at the surface of the infected erythrocyte. Despite their relevance to the disease, their structure, mechanisms of traffic and their process of assembly remain poorly understood. In this study, we have explored the possible role of a parasite-encoded Hsp40 class of chaperone, namely PFB0090c/PF3D7_0201800 (KAHsp40) in protein trafficking in the infected erythrocyte.
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