Abstract Aim To Identify our compliance with GMC guidelines for use of a chaperon in urology outpatient clinic. Method 1st audit included total 12 urologists team (6 consultants and 6 SpR) For each urologist, we checked records 10 patients who attended OPD had physical examination as evidenced the notes and/ or clinic letter N = 120 patient Each urologist was given score ( 0 if no mention chape...

Crystallins are the predominant proteins of eye lens which prevent heat and oxidative-induced stress-induced aggregation other proteins. They may be classified into two superfamilies, α- βγ- crystallins. The crystallins long-lived structural refract light onto retina. microbial can not only bind to calcium ions, but even able coordinate ions such as Mg2+, Sr2+, Co2+, Mn2+, Ni2+, Zn2+ etc. Such ...

BACKGROUND Obstetrics and gynecology units in public hospitals in South Africa (SA) are often overloaded with patients. Most physical examinations/consultations in these units involve vaginal examination (VE) and often because of the rapid turnover of patients the pelvic examination may be performed hurriedly without due consideration being given to the psychosocial aspects of such procedures. ...

The 90-kDa heat shock protein (HSP90) acts as a specific molecular chaperone in the folding and regulates a wide range of associated proteins such as steroid hormone receptors. It is known that HSP90 possesses two different chaperone sites, both in the N- and C-domains, and that the chaperone activity of HSP90 is blocked by binding of geldanamycin (GA) to the N-domain, the same as the ATP-bindi...

Alpha-crystallin is a member of the small heat-shock protein family and functions like a molecular chaperone, and may thus help in maintaining the transparency of the eye lens by protecting the lens proteins from various stress conditions. Non-enzymic glycation of long-lived proteins has been implicated in several age- and diabetes-related complications, including cataract. Dicarbonyl compounds...

Molecular chaperones and heat shock proteins (Hsp) have emerged as critical regulators of proteins associated with neurodegenerative disease pathologies. The very nature of the chaperone system, which is to maintain protein quality control, means that most nascent proteins come in contact with chaperone proteins. Thus, amyloid precursor protein (APP), members of the gamma-secretase complex (pre...

The molecular chaperone heat shock protein 70 (Hsp70) plays a vital role in cellular processes, including protein folding and assembly, and helps prevent aggregation under physiological and stress-related conditions. Although the structural changes undergone by full-length client proteins upon interaction with DnaK (i.e., Escherichia coli Hsp70) are fundamental to understand chaperone-mediated ...

alpha-Synuclein, an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded. Recent studies have demonstrated that alpha-synuclein has chaperone activity both in vitro and in vivo, and that this activity is lost upon removing its C-terminal acidic tail. However, the detailed mechanism of the chaperone action of alpha-synuclein remains unknown. In this st...

Hsp90 is a highly conserved molecular chaperone that is involved in modulating a multitude of cellular processes. In this study, we identify a function for the chaperone in RNA processing and maintenance. This functionality of Hsp90 involves two recently identified interactors of the chaperone: Tah1 and Pih1/Nop17. Tah1 is a small protein containing tetratricopeptide repeats, whereas Pih1 is fo...

We sought new strategies to reduce amounts of the polyglutamine androgen receptor (polyQ AR) and achieve benefits in models of spinobulbar muscular atrophy, a protein aggregation neurodegenerative disorder. Proteostasis of the polyQ AR is controlled by the heat shock protein 90 (Hsp90)- and Hsp70-based chaperone machinery, but mechanisms regulating the protein's turnover are incompletely unders...