منابع مشابه
Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases.
Intramembrane proteases have the unusual property of cleaving peptide bonds within the lipid bilayer, an environment not obviously suited to a water-requiring hydrolysis reaction. These enzymes include site-2 protease, gamma-secretase/presenilin, signal peptide peptidase and the rhomboids, and they have a wide range of cellular functions. All have multiple transmembrane domains and, because of ...
متن کاملFunctional Studies of Purified Transmembrane Proteases, Omptins, of Yersinia pestis and Salmonelle enterica
4/2006 Kari Kreander A Study on Bacteria-Targeted Screening and in vitro Safety Assessment of Natural Products 5/2006 Gudrun Wahlström From Actin Monomers to Bundles: The Role of Twinfi lin and a-Actinin in Drosophila melanogaster Development 6/2006 Jussi Joensuu Production of F4 Fimbrial Adhesin in Plants: A Model for Oral Porcine Vaccine against Enterotoxigenic Escherichia coli 7/2006 Heikki ...
متن کاملIdentification of proteases employed by dendritic cells in the processing of protein purified derivative (PPD)
Dendritic cells (DC) are known to present exogenous protein Ag effectively to T cells. In this study we sought to identify the proteases that DC employ during antigen processing. The murine epidermal-derived DC line Xs52, when pulsed with PPD, optimally activated the PPD-reactive Th1 clone LNC.2F1 as well as the Th2 clone LNC.4k1, and this activation was completely blocked by chloroquine pretre...
متن کامل63 Varghese
Epidemiological studies, especially cohort studies have many limitations in countries like India. The present population based molecular epidemiolohgical cohort study was planned to address the prevalence, risk factors and natural history of uterine cervical HPV infection in women in an area of suburban dwellings in South India. Epidemiological data, blood samples and cervical scrape smears wer...
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ژورنال
عنوان ژورنال: Proceedings of the Imperial Academy
سال: 1944
ISSN: 0369-9846,1881-1140
DOI: 10.2183/pjab1912.20.296