Temple University

About: Temple University is a education organization based out in Philadelphia, Pennsylvania, United States. It is known for research contribution in the topics: Population & Poison control. The organization has 32154 authors who have published 64375 publications receiving 2219828 citations.

Smartphones and Cognition: A Review of Research Exploring the Links between Mobile Technology Habits and Cognitive Functioning.

Abstract: While smartphones and related mobile technologies are recognized as flexible and powerful tools that, when used prudently, can augment human cognition, there is also a growing perception that habitual involvement with these devices may have a negative and lasting impact on users’ ability to think, remember, pay attention, and regulate emotion. The present review considers an intensifying, though still limited, area of research exploring the potential cognitive impacts of smartphone-related habits, and seeks to determine in which domains of functioning there is accruing evidence of a significant relationship between smartphone technology and cognitive performance, and in which domains the scientific literature is not yet mature enough to endorse any firm conclusions. We focus our review primarily on three facets of cognition that are clearly implicated in public discourse regarding the impacts of mobile technology – attention, memory, and delay of gratification – and then consider evidence regarding the broader relationships between smartphone habits and everyday cognitive functioning. Along the way, we highlight compelling findings, discuss limitations with respect to empirical methodology and interpretation, and offer suggestions for how the field might progress toward a more coherent and robust area of scientific inquiry.​

A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase.

Abstract: We have isolated and characterized a plasmid (pChug 20.1) that contains the cDNA of a nuclear uracil DNA glycosylase (UDG) gene isolated from normal human placenta. This cDNA directed the synthesis of a fusion protein (Mr 66,000) that exhibited UDG activity. The enzymatic activity was specific for a uracil-containing polynucleotide substrate and was inhibited by a glycosylase antibody or a beta-galactosidase antibody. Sequence analysis demonstrated an open reading frame that encoded a protein of 335 amino acids of calculated Mr 36,050 and pI 8.7, corresponding to the Mr 37,000 and pI 8.1 of purified human placental UDG. No homology was seen between this cDNA and the UDG of herpes simplex virus, Escherichia coli, and yeast; nor was there homology with the putative human mitochondrial UDG cDNA or with a second human nuclear UDG cDNA. Surprisingly, a search of the GenBank data base revealed that the cDNA of UDG was completely homologous with the 37-kDa subunit of human glyceraldehyde-3-phosphate dehydrogenase. Human erythrocyte glyceraldehyde-3-phosphate dehydrogenase was obtained commercially in its tetrameric form. A 37-kDa subunit was isolated from it and shown to possess UDG activity equivalent to that seen for the purified human placental UDG. The multiple functions of this 37-kDa protein as here and previously reported indicate that it possesses a series of activities, depending on its oligomeric state. Accordingly, mutation(s) in the gene of this multifunctional protein may conceivably result in the diverse cellular phenotypes of Bloom syndrome.