Abstract Purpose: To evaluate the diagnostic accuracy of magnetic resonance MR elastography as a method to help diagnose clinically substantial fibrosis in patients with nonalcoholic fatty liver disease NAFLD and, by using MR elastography as a reference standard, to compare various laboratory marker panels in the identification of patients with NAFLD and advanced fibrosis. Informed consent was waived. This study was conducted in patients with NAFLD, who were identified by imaging characteristics consistent with steatosis in a prospective database that tracks all MR elastographic examinations. Six laboratory-based models of fibrosis were compared with MR elastographic results as well as fibrosis stage from liver biopsy results.
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Get e-Alerts Biography Kourosh Honarmand Ebrahimi Kerman, Iran earned his undergraduate degree in Chemical Engineering in , and then he worked for 5 years in the petrochemical industry in Iran.
In he found the opportunity to pursue his dreams and started his M. He obtained his M. Hagen with whom he continued his Ph. Farzan on the glycobiology of HIV-1 envelope glycoprotein. His current research interests include metalloproteins, biocatalysis, and development of label-free methods for studying enzyme kinetics. He completed his Ph. Hagen at the Delft University of Technology.
He then worked as a research scientist at the University of Leiden with H. Steensma and at the Delft University of Technology with W. In he became an assistant professor in biocatalysis at the Delft University of Technology. His research is focused on metalloproteomics, directed evolution of metallo enzymes. Biography Wilfred Fred R. Hagen studied chemistry at the University of Amsterdam, where he also completed his Ph.
Albracht and E. Dunham and R. Veeger at Wageningen University and to set up a group on metalloproteins. In he was also appointed Professor of Bioinorganic Chemistry in Wageningen. His research is focused on the roles of metal ions in biocatalysis and methodological development in EPR spectroscopy.
Of these metals iron is widely used for catalysis of many reactions by living organisms because it can be found in all natural habitats and participate in biological transformations either as a redox center or as a Lewis acid in the catalytic site of many enzymes. Using iron in an oxygenic environment requires organisms to precisely control intracellular availability of free Fe II and Fe III , which are the two most common oxidation states of iron.
To cope with these problems the molecular machinery of living organisms has a sophisticated system to safely control cellular iron trafficking. The subunits are assembled into a spherical-shape structure with symmetry Figure 1 b. Dps and Dps-like proteins have a spherical-shape structure composed of 12 identical subunits; their primary function appears to be protection of DNA against oxidative damage.
Figure 1 Figure 1. Structures of meric nonheme ferritin and heme-containing bacterioferritin. In order to oxidize Fe II they use molecular oxygen or hydrogen peroxide. The storage cavity of the protein is separated from the solution by a protein shell with a thickness of 2 nm. In bacteria and archaea ferritin is the product of self-assembly of 24 identical subunits, 14 each of which is catalytically competent.
The iron-storage function of ferritin has a central role in cellular iron homeostasis. Deletion of the coding gene for the H subunit in mice leads to early embryonic death 15 and mutation in the gene of the L subunit in humans has been observed in neurodegenerative diseases such as neuroferritinopathy. We will review these studies in the frame of six questions Figure 2.
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