chaperones are produced by prokaryotic, yeast and higher eukaryotic cells for various purposes. over-expression of each chaperone or sets of them affect the production level of a recombinant protein in the cell. on the basis of this hypothesis, five different plasmids with 5 different combinations of 6 chaperones molecule, transformed into escherichia coli along with human basic fibroblast grow...

Chaperones are produced by prokaryotic, yeast and higher eukaryotic cells for various purposes. Over-expression of each chaperone or sets of them affect the production level of a recombinant protein in the cell. On the basis of this hypothesis, five different plasmids with 5 different combinations of 6 chaperones molecule, transformed into Escherichia coli along with human basic Fibroblast Grow...

We report here interesting synergistic effects of proline and sorbitol, two well-known chemical chaperones, in the inhibition of fibrillation of two proteins, insulin and lysozyme. A combination of many biophysical techniques has been used to understand the structural morphology and modes of interaction of the chaperones with the proteins during fibrillation. Both the chaperones establish stron...

NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron-el...

PURPOSE Many mutations in rhodopsin, including P23H, result in misfolding and mislocalization of the protein. It has been demonstrated that pharmacologic chaperones are effective in assisting the proper folding and targeting of P23H opsin. This study was designed to investigate a high-throughput screening strategy for identification of pharmacologic chaperones by using a combination of in silic...

Molecular chaperones are the key instruments of bacterial protein homeostasis. Chaperones not only facilitate folding client proteins, but also transport them, prevent their aggregation, dissolve aggregates and resolve misfolded states. Despite this seemingly large variety, single can perform several these functions even on multiple different clients, thus suggesting a biophysical mechanism und...

Introduction: Deep heated oils produce toxins that endanger people's health. The current study aims to investigate the simultaneous effect of aerobic training and Octopamine consumption on the mitophagy of brown adipose tissue after the induction of intoxication through deeply heated oil in male wistar rats. Method: 40 male wistar rats after four weeks of feedi...

Alzheimer disease is a neurological disorder that is characterized by the presence of fibrils and oligomers composed of the amyloid beta (Abeta) peptide. In models of Alzheimer disease, overexpression of molecular chaperones, specifically heat shock protein 70 (Hsp70), suppresses phenotypes related to Abeta aggregation. These observations led to the hypothesis that chaperones might interact wit...

The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and co-factors, interactors receptors, its canonical role is protein quality control. A malfunction of the CS may cause diseases, known as chaperonopathies. These are caused by qualitatively and/or quantitatively abnormal chaperones. Since ubiquitous, chaperonopathies systemic, affecting various tissues ...