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Page - acrobat - 12/27/2009 - 06:34 - 0 comments - 0 attachments
Ebook Planning your medical career a guide to careers support
Submitted by antoq on Wed, 12/03/2008 - 02:40What is the purpose of this guide? All doctors progressing through training will need to give thought, and dedicate time, to planning their career. This guide aims to provide trainee doctors, in both primary and secondary care, with an overview of the support options that are available to them.
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Ebook Corporate Governance, Regulation, and Bank Risk Taking
Submitted by puput on Wed, 08/11/2010 - 07:51By selecting, financing, and monitoring firms, banks influence capital allocation, economic activity, and risk (Allen and Gale, 2000, and Levine, 2006). Many governments, however, fear that a bank’s private governance arrangements, including its ownership and management structure, will not produce a desirable allocation of capital, and therefore enact regulations to shape bank behavior (Benston and Kaufman, 1996; Barth et al., 2006). Yet, no previous empirical research studies how a bank’s ownership structure combines with a wide array of national laws and regulations to shape bank risk taking.
In this paper, we evaluate the impact of ownership structure, franchise value, investor protection laws, and bank regulations on the risk taking behavior of banks around the world; thus, we simultaneously examine an individual bank’s private governance structure and the policy environment in which it operates. In contrast, past work examines subsets of these factors. For example, Demirgüç-Kunt and Detragiache’s (2002) cross-country study of deposit insurance and banking crises does not control for regulations designed to limit bank risk taking or for bank-level governance traits. In turn, Saunders et al. (1990) and Demsetz et al. (1997) show how ownership structure, franchise value, and other bank-level characteristics influence bank risk taking in the United States. They cannot, however, test whether numerous laws and regulations shape bank risk taking, and it is unclear whether their results generalize to banks in other countries with different policies. By collecting new data on bank ownership and managerial structure and merging it with data on bank regulations and investor protection laws, we examine how a bank’s private governance arrangements combine with national policies to influence risk taking.
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Free ebook Biochemical, biophysical, and cellular investigations of the interactions of transferrin receptor with transferrin an
Submitted by antoq on Thu, 10/30/2008 - 01:01Hereditary hemochromatosis (HH) is a prevalent genetic disorder that results in the daily excess absorption of dietary iron. If untreated this disease leads to systemic organ failure and death. HH is caused by mutations to the gene coding for a protein called HFE, a type I transmembrane glycoprotein with a demonstrated role in regulating cellular iron homeostasis. HFE binds to the cell-surface receptor transferrin receptor (TfR), a dimeric type II transmembrane glycoprotein responsible for iron uptake into most mammalian cell types. TfR binds iron-loaded transferrin (Fe-Tf) from the blood and transports it to acidic recycling endosomes where iron is released from Fe-Tf in a TfR-facilitated process. Iron-free transferrin (apo-Tf) remains bound to TfR and is recycled to the cell surface, where apo-Tf rapidly dissociates from TfR upon exposure to the basic pH of blood. HFE and Fe-Tf can bind simultaneously to TfR to form a ternary complex, but HFE binding to TfR lowers the apparent affinity of the Fe-Tf/TfR interaction. This reduction could result from direct competition between HFE and Fe-Tf for receptor binding sites, from negative cooperativity, or both. We sought to understand the mechanism of HFE, Fe-Tf, and apo-Tf binding by TfR to help define HFE's role in iron homeostasis. We determined the binding constants for HFE, Fe-Tf, and apo-Tf to an extensive set of site-directed TfR mutants and discovered that HFE and Tf bind to an overlapping site on TfR, indicating the two proteins compete with each other for receptor binding. The mutagenesis results also identified differences in the contact points between TfR and the two forms of Tf, Fe-Tf and apo-Tf. By combining the mutations that are required for apo-Tf, but not Fe-Tf, binding we find that a highly conserved hydrophobic patch on the TfR surface is required for the receptor-mediated stimulation of iron release from Fe-Tf. From these data we propose a structure-based model for the mechanism of TfR-assisted iron release.
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