The information-loss model: A mathematical theory of age-related cognitive slowing.

A model of cognitive slowing is proposed with the following assumptions: Information is lost during processing, processing occurs in discrete steps with step duration inversely related to the amount of information currently available, and the effect of aging is to increase the proportion of information lost per step. This model correctly predicts a positively accelerated relation between latencies of older and younger adults and provides a unified account of the effects of task complexity, practice, speed–accuracy tradeoffs, and fluctuations in individual performance. Strong support for the thesis that cognitive slowing is global, and not localized in specific age-sensitive components, is provided by the fact that the model accurately predicts the latencies of older adults on the basis of those of younger adults, without regard to the nature of the task, across a latency range of nearly 2 orders of magnitude. (PsycINFO Database Record (c) 2010 APA, all rights reserved)     

Apoptosis: molecular regulation of cell death

This article focuses on the few disorders that produce chronic cholestasis in infants and children. Cholestasis is defined, and a framework for thinking about pathophysiology is provided. Medical management is discussed in the context of the consequences and complications of chronic cholestasis. The limited differential for chronic cholestasis is discussed, and approaches to diagnosis and management of specific disorders are provided.     

Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease

Efficient proteolytic processing of essential junctions of the hepatitis C virus (HCV) polyprotein requires a heterodimeric complex of the NS3 bifunctional protease/helicase and the NS4A accessory protein. A single-chain recombinant form of the protease has been constructed in which NS4A residues 21-32 (GSVVIVGRIILS) were fused in frame to the amino terminus of the NS3 protease domain (residues 3-181) through a tetrapeptide linker. The single-chain recombinant protease has been overexpressed as a soluble protein in E. coli and purified to homogeneity by a combination of metal chelate and size-exclusion chromatography. The single-chain recombinant protease domain shows full proteolytic activity cleaving the NS5A-5B synthetic peptide substrate, DTEDVVCCSMSYTWTGK with a Km and k(cat) of 20.0 +/- 2.0 microM and 9.6 +/- 2.0 min(-1), respectively; parameters identical to those of the authentic NS3(1-631)/NS4A(1-54) protein complex generated in eukaryotic cells (Sali DL et al., 1998, Biochemistry 37:3392-3401).