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1.
Physiol Behav ; 53(5): 929-36, 1993 May.
Artículo en Inglés | MEDLINE | ID: mdl-8511209

RESUMEN

The aim of the present study was to assess the stimulating effects of bright light (BL) on subjective and objective alertness. Eight subjects were exposed to either bright light or dim light (DL) during a 24-h constant routine (0900-0900). Bright light failed to modify either the 24-h course or the level of body temperature. Compared to DL, BL delayed the circadian trough of motor activity by 2 h. During the night, relative to the dim-light condition, BL significantly increased subjective and objective (EEG test) alertness and improved performances. Thus, BL exposure partly counteracted the effects of sleep deprivation and/or the circadian trough on alertness and performances. During the day, BL only improved the mood and motivation levels. However, the time course of mood and motivation was not affected by the BL exposure, a nocturnal circadian trough occurring at 0630 in both light conditions.


Asunto(s)
Nivel de Alerta , Atención , Ritmo Circadiano , Luz , Reconocimiento Visual de Modelos , Solución de Problemas , Desempeño Psicomotor , Regulación de la Temperatura Corporal , Humanos , Masculino , Motivación , Tiempo de Reacción
2.
Planta ; 180(1): 96-104, 1989 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-24201849

RESUMEN

Suspension-cultured cells of sycamore (Acer pseudoplatanus L.) secrete a number of acid hydrolases and other proteins that have both highmannose and complex asparagine-linked glycans. We used affinity chromatography with concanavalin A and an antiserum specific for complex glycans in conjunction with in vivo-labeling studies to show that all of the secreted proteins carry glycans. The presence of complex glycans on secretory proteins indicates that they are passing through the Golgi complex on the way to the extracellular compartment. The sodium ionophore, monensin, did not block the transport of proteins to the extracellular medium, even though monensin efficiently inhibited the Golgi-mediated processing of complex glycans. The inhibition of N-glycosylation by tunicamycin reduced by 76% to 84% the accumulation of newly synthesized (i.e. radioactively labeled) protein that was secreted by the sycamore cells, while cytoplasmic protein biosynthesis was not affected by this antibiotic. However, in the presence of glycoprotein-processing inhibitors, such as castanospermine and deoxymannojirimycin, the formation of complex glycans was prevented but glycoprotein secretion was unchanged. These results support the conclusion that N-linked glycan processing is not necessary for sorting, but glycosylation is required for accumulation of secreted proteins in the extracellular compartment.

3.
Comp Funct Genomics ; 5(2): 190-5, 2004.
Artículo en Inglés | MEDLINE | ID: mdl-18629073

RESUMEN

The central dogma of molecular biology has provided a meaningful principle for data integration in the field of genomics. In this context, integration reflects the known transitions from a chromosome to a protein sequence: transcription, intron splicing, exon assembly and translation. There is no such clear principle for integrating proteomics data, since the laws governing protein folding and interactivity are not quite understood. In our effort to bring together independent pieces of information relative to proteins in a biologically meaningful way, we assess the bias of bioinformatics resources and consequent approximations in the framework of small-scale studies. We analyse proteomics data while following both a data-driven (focus on proteins smaller than 10 kDa) and a hypothesis-driven (focus on whole bacterial proteomes) approach. These applications are potentially the source of specialized complements to classical biological ontologies.

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