The effects of stimulus modality and task integrality: Predicting dual-task performance and workload from single-task levels

The influence of stimulus modality and task difficulty on workload and performance was investigated. The goal was to quantify the cost (in terms of response time and experienced workload) incurred when essentially serial task components shared common elements (e.g., the response to one initiated the other) which could be accomplished in parallel. The experimental tasks were based on the Fittsberg paradigm; the solution to a SternBERG-type memory task determines which of two identical FITTS targets are acquired. Previous research suggested that such functionally integrated dual tasks are performed with substantially less workload and faster response times than would be predicted by suming single-task components when both are presented in the same stimulus modality (visual). The physical integration of task elements was varied (although their functional relationship remained the same) to determine whether dual-task facilitation would persist if task components were presented in different sensory modalities. Again, it was found that the cost of performing the two-stage task was considerably less than the sum of component single-task levels when both were presented visually. Less facilitation was found when task elements were presented in different sensory modalities. These results suggest the importance of distinguishing between concurrent tasks that complete for limited resources from those that beneficially share common resources when selecting the stimulus modalities for information displays

Advances in Understanding Carboxysome Assembly in \u3ci\u3eProchlorococcus\u3c/i\u3e and \u3ci\u3eSynechococcus\u3c/i\u3e Implicate CsoS2 as a Critical Component

The marine Synechococcus and Prochlorococcus are the numerically dominant cyanobacteria in the ocean and important in global carbon fixation. They have evolved a CO2-concentrating-mechanism, of which the central component is the carboxysome, a self-assembling proteinaceous organelle. Two types of carboxysome, α and β, encapsulating form IA and form IB d-ribulose-1,5-bisphosphate carboxylase/oxygenase, respectively, differ in gene organization and associated proteins. In contrast to the β-carboxysome, the assembly process of the α-carboxysome is enigmatic. Moreover, an absolutely conserved α-carboxysome protein, CsoS2, is of unknown function and has proven recalcitrant to crystallization. Here, we present studies on the CsoS2 protein in three model organisms and show that CsoS2 is vital for α-carboxysome biogenesis. The primary structure of CsoS2 appears tripartite, composed of an N-terminal, middle (M)-, and C-terminal region. Repetitive motifs can be identified in the N- and M-regions. Multiple lines of evidence suggest CsoS2 is highly flexible, possibly an intrinsically disordered protein. Based on our results from bioinformatic, biophysical, genetic and biochemical approaches, including peptide array scanning for protein-protein interactions, we propose a model for CsoS2 function and its spatial location in the α-carboxysome. Analogies between the pathway for β-carboxysome biogenesis and our model for α-carboxysome assembly are discussed

Why Primate Models Matter

Research involving nonhuman primates (NHPs) has played a vital role in many of the medical and scientific advances of the past century. NHPs are used because of their similarity to humans in physiology, neuroanatomy, reproduction, development, cognition, and social complexity – yet it is these very similarities that make the use of NHPs in biomedical research a considered decision. As primate researchers, we feel an obligation and responsibility to present the facts concerning why primates are used in various areas of biomedical research. Recent decisions in the United States, including the phasing out of chimpanzees in research by the National Institutes of Health and the pending closure of the New England Primate Research Center, illustrate to us the critical importance of conveying why continued research with primates is needed. Here we review key areas in biomedicine where primate models have been, and continue to be, essential for advancing fundamental knowledge in biomedical and biological research

Genomic Organization, Splice Variants and Expression of CGMl, a CD66-related Member of the Carcinoembryonic Antigen Gene Family

The tumor marker carcinoembryonic antigen (CEA) belongs to a family of proteins which are composed of one immunogiobulin variable domain and a varying number of immunoglobulin constant-like domains. Most of the membrane-bound members, which are anchored either by a glycosylphosphatidylinositol moiety or a transmembrane domain, have been shown to convey cell adhesion in vitro. Here we describe two splice variants of CGMI. a transmembrane member of the CEA family without immunoglobulin constant.like domains. CGM1a and CGM1c contain cytopiasmic domains of 71 and 31 amino acids, respectively, The cytoplasmic region of CGM1a is encoded by four exons (Cyt1-Cyt4). Differential splicing of the Cyt1 exon (53 bp)..

Pennsylvania Folklife Vol. 10, No. 1

• Tramp Work : Penknife Plus Cigar Boxes • Tramps of My Youth • The German Broadside Songs of Pennsylvania • The Rise of Interest in Folk Art • Dutch Treats for Breakfast • The Amish, Citizens of Heaven and America • Collectanea • My Great-Grandmother • Old Sweitzer\u27s Ghost • Pastimes of My Youth • Battalion Day • Seven Days Make One Weekhttps://digitalcommons.ursinus.edu/pafolklifemag/1004/thumbnail.jp

Osteoarthritic changes in vervet monkey knees correlate with meniscus degradation and increased matrix metalloproteinase and cytokine secretion

Meniscus injury increases osteoarthritis risk but its pathobiology in osteoarthritis is unclear. We hypothesized that older adult vervet monkeys would exhibit knee osteoarthritic changes and the degenerative menisci from these animals would secrete matrix metalloproteinases (MMPs) and pro-inflammatory cytokines that contribute to the development of osteoarthritis