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Full-Text Articles in Medicine and Health Sciences
Efficacy Of The Herpes Zoster Subunit Vaccine In Adults 70 Years Of Age Or Older, A L Cunningham, Himal Lal, Martina Kovac, Roman Chlibek, Shinn-Jang Hwang, Javier Diez-Domingo, Olivier Godeaux, Myron J. Levin, Janet E. Mcelhaney, Joan Puig-Barbera, Wilfred W. Yeo
Efficacy Of The Herpes Zoster Subunit Vaccine In Adults 70 Years Of Age Or Older, A L Cunningham, Himal Lal, Martina Kovac, Roman Chlibek, Shinn-Jang Hwang, Javier Diez-Domingo, Olivier Godeaux, Myron J. Levin, Janet E. Mcelhaney, Joan Puig-Barbera, Wilfred W. Yeo
Illawarra Health and Medical Research Institute
BACKGROUND A trial involving adults 50 years of age or older (ZOE-50) showed that the herpes zoster subunit vaccine (HZ/su) containing recombinant varicella-zoster virus glycoprotein E and the AS01B adjuvant system was associated with a risk of herpes zoster that was 97.2% lower than that associated with placebo. A second trial was performed concurrently at the same sites and examined the safety and efficacy of HZ/su in adults 70 years of age or older (ZOE-70). METHODS This randomized, placebo-controlled, phase 3 trial was conducted in 18 countries and involved adults 70 years of age or older. Participants received two doses …
Small Heat-Shock Proteins Prevent A-Synuclein Aggregation Via Transient Interactions And Their Efficacy Is Affected By The Rate Of Aggregation, Dezerae Cox, Emily Selig, Michael D. W Griffin, John A. Carver, Heath Ecroyd
Small Heat-Shock Proteins Prevent A-Synuclein Aggregation Via Transient Interactions And Their Efficacy Is Affected By The Rate Of Aggregation, Dezerae Cox, Emily Selig, Michael D. W Griffin, John A. Carver, Heath Ecroyd
Illawarra Health and Medical Research Institute
The aggregation of a-synuclein (a-syn) into amyloid fibrils is associated with neurodegenerative diseases, collectively referred to as the a-synucleinopathies. In vivo, molecular chaperones, such as the small heat-shock proteins (sHsps), normally act to prevent protein aggregation; however, it remains to be determined how aggregation-prone a-syn evades sHsp chaperone action leading to its disease-associated deposition. This work examines the molecular mechanism by which two canonical sHsps, aB-crystallin (aB-c) and Hsp27, interact with aggregation-prone a-syn to prevent its aggregation in vitro. Both sHsps are very effective inhibitors of ¿-syn aggregation, but no stable complex between the sHsps and a-syn was detected, indicating …