By Судаков К.В.

;Биологические мотивации КНИГИ ;НАУКА и УЧЕБА Автор: Судаков К.В. Название: Биологические мотивации Издательство: Медицина Год: 1971 Формат: djvu Размер: 4,6 Mb +3% Для сайта: www.mirknig.comКнига посвящена описанию таких эмоциональных состояний как голод, жажда, половое возбуждение, страх. Показана роль мотивации в приспособительных реакциях организма, патология и психофармакология мотиваций.Depozit records zero

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2004). Ctr2 has been shown to make Cu available for all known Cu-requiring processes (Portnoy et al. 2001; Rees et al. 2004). Interestingly, Ctr2 does not appear to be regulated as are the high affinity Cu transporters, Ctr1 and Ctr3 (Portnoy et al. 2001). Sequence homology and predicted topology suggest that Ctr2 utilizes a similar mechanism of transport as Ctr1. This is further supported by genetic and biochemical evidence. It was illustrated that Ctr2 assembles as a homomultimer as does Ctr1 (Rees et al.

Interestingly, the single amino acid substitution R970G confers cadmium resistance in yeast 18 Jaekwon Lee, David Adle, Heejeong Kim (Shirashi et al. 2000). Microarray data confirmed by quantitative PCR shows that Cu or Fe deficiency regulates Pca1 expression (De Freitas et al. 2004). A respiratory deficient phenotype has been described for Δpca1 null mutants (De Freitas et al. 2004). Thus far, the available evidence suggests some role in Cu and/or Fe homeostasis, however, the details still remain to be studied.

Yeast cells with elevated levels of SOD1 in the mitochondria exhibit pro-longed survival in the stationary phase (Sturtz et al. 2001). Given that death of yeast cells in the stationary phase is linked with mitochondrial reactive oxygen production (Jakubowski et al. 2000; Longo et al. 1999; Ashrafi et al. 1999), SOD1 accumulated in the mitochondria may play a significant role in protection against oxidative stress when cells are in the stationary phase. This study may have an important implication with familial amyotropic lateral sclerosis (ALS), a fatal neurodegenerative disease resulting from gain-of function mutations of SOD1 (Rosen et al.

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