Safeguarding the banking system in an environment of financial cycles: an overview

Banks and banking ; Risk ; Banking law ; Bank supervision

Insurance companies as financial intermediaries: risk and return

Insurance industry ; Risk ; Investments

Book reviews

Teaching/Communication/Extension/Profession,

Safeguarding the banking system from financial cycles

Bank failures ; Banks and banking ; Bank loans ; Risk ; Bank supervision

Within host RNA virus persistence : mechanisms and consequences

RER is funded by the Wellcome Trust, UK (Grant 101788/Z/13/Z) and DEG by US National Institutes of Health (R01 NS038932).In a prototypical response to an acute viral infection it would be expected that the adaptive immune response would eliminate all virally infected cells within a few weeks of infection. However many (non-retrovirus) RNA viruses can establish “within host” persistent infections that occasionally lead to chronic or reactivated disease. Despite the importance of “within host” persistent RNA virus infections, much has still to be learnt about the molecular mechanisms by which RNA viruses establish persistent infections, why innate and adaptive immune responses fail to rapidly clear these infections, and the epidemiological and potential disease consequences of such infections.Publisher PDFPeer reviewe

Iodine sorption study on the proposed use of Viton A in a shuttle galley water accumulator

The installation of a Viton A accumulator in the Shuttle galley has been proposed to prevent overpressurization of the hot water supply system. A laboratory study has been conducted to determine if there would be any interaction between the Viton A material and the iodine used to disinfect the water. Coupons of Viton A were exposed for 24 hours to aqueous iodine solutions similar in quality to the Shuttle's potable water. Changes in the iodine residual were monitored to determine the rate of iodine sorption by the coupon. Total organic carbon (TOC) was monitored to determine the rate of desorption of organic materials from the Viton A. The same coupons were then soaked in reagent-grade water for 24 hours, and iodine was monitored to determine the rate of iodine desorption. The coupons were again exposed to iodine solutions for 24 hours and iodine and TOC were monitored. No significant change in the iodine sorption rate was detected between the first and second exposures. A triangle taste test indicated at a 1 percent confidence level that the water exposed to Viton A had a different taste which was less acceptable to the panelists

Alternative Approaches at the Federal and State Level

The reason that the discussions and positions that you heard this morning are no longer being voiced so widely in California is because conditions have continued to deteriorate there rather dramatically. Like the rest of the country, we have a large uninsured population, but the percentage of our uninsured population is larger than the national average as a percentage of the non-elderly population. In the U.S. it\u27s about eighteen percent; in California, it\u27s over twenty-one percent. That means more than five million uninsured people

Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain

<p>Abstract</p> <p>Background</p> <p>IPS-1/MAVS/VISA/Cardif is an adaptor protein that plays a crucial role in the induction of interferons in response to viral infection. In the initial stage of the intracellular antiviral response two RNA helicases, retinoic acid inducible gene-I (RIG-I) and melanoma differentiation-association gene 5 (MDA5), are independently able to bind viral RNA in the cytoplasm. The 62 kDa protein IPS-1/MAVS/VISA/Cardif contains an N-terminal caspase activation and recruitment (CARD) domain that associates with the CARD regions of RIG-I and MDA5, ultimately leading to the induction of type I interferons. As a first step towards understanding the molecular basis of this important adaptor protein we have undertaken structural studies of the IPS-1 MAVS/VISA/Cardif CARD region.</p> <p>Results</p> <p>The crystal structure of human IPS-1/MAVS/VISA/Cardif CARD has been determined to 2.1Å resolution. The protein was expressed and crystallized as a maltose-binding protein (MBP) fusion protein. The MBP and IPS-1 components each form a distinct domain within the structure. IPS-1/MAVS/VISA/Cardif CARD adopts a characteristic six-helix bundle with a Greek-key topology and, in common with a number of other known CARD structures, contains two major polar surfaces on opposite sides of the molecule. One face has a surface-exposed, disordered tryptophan residue that may explain the poor solubility of untagged expression constructs.</p> <p>Conclusion</p> <p>The IPS-1/MAVS/VISA/Cardif CARD domain adopts the classic CARD fold with an asymmetric surface charge distribution that is typical of CARD domains involved in homotypic protein-protein interactions. The location of the two polar areas on IPS-1/MAVS/VISA/Cardif CARD suggest possible types of associations that this domain makes with the two CARD domains of MDA5 or RIG-I. The N-terminal CARD domains of RIG-I and MDA5 share greatest sequence similarity with IPS-1/MAVS/VISA/Cardif CARD and this has allowed modelling of their structures. These models show a very different charge profile for the equivalent surfaces compared to IPS-1/MAVS/VISA/Cardif CARD.</p