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- Buckle, J. V., et al.
(författare)
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Observations of chemical differentiation in clumpy molecular clouds
- 2006
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Ingår i: Faraday Discussions. - : Royal Society of Chemistry (RSC). - 1359-6640 .- 1364-5498. ; 133, s. 63 - 82
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Tidskriftsartikel (refereegranskat)abstract
- We have extensively mapped a sample of dense molecular clouds (L1512, TMC-1C, L1262, Per7, L1389, L1251E) in lines of HC 3 N, CH 3 OH, SO and C 18 O. We demonstrate that a high degree of chemical differentiation is present in all of the observed clouds. We analyse the molecular maps for each cloud, demonstrating a systematic chemical differentiation across the sample, which we relate to the evolutionary state of the cloud. We relate our observations to the cloud physical, kinematical and evolutionary properties, and also compare them to the predictions of simple chemical models. The implications of this work for understanding the origin of the clumpy structures and chemical differentiation observed in dense clouds are discussed. © The Royal Society of Chemistry 2006.
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- Dunlop, Rachael A, et al.
(författare)
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Oxidized Proteins : Mechanisms of Removal and Consequences of Accumulation
- 2009
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Ingår i: IUBMB LIFE. - : Wiley. - 1521-6543 .- 1521-6551. ; 61:5, s. 522-527
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Tidskriftsartikel (refereegranskat)abstract
- Elevated levels of oxidized proteins are reported in diseased tissue from age-related pathologies such as atherosclerosis, neurodegenerative disorders, and cataract. Unlike the precise mechanisms that exist For the repair of nucleic acids, lipids, and carbohydrates, the primary pathway for the repair of oxidized proteins is complete catabolism to their constitutive amino acids. This process can be inefficient as is evidenced by their accumulation. It is generally considered that damaged proteins are degraded by the proteasome, however, this is only true for mildly oxidized proteins, because substrates must be unfolded to enter the narrow catalytic core. Rather, evidence suggests that moderately or heavily oxidized proteins are endocytosed and enter the endosomal/lysosomal system, indicating co-operation between the proteasomes and the lysosomes. Heavily modified substrates are incompletely degraded and accumulate within the lysosomal compartments resulting in the formation of lipofuscin-like, autofluorescent aggregates. Accumulation eventually results in impaired turnover of large organelles such as proteasomes and mitochondria, lysosomal destablization, leakage of proteases into the cytosol and apoptosis. In this review, we summarize reports published since our last assessments of the field of oxidized protein degradation including a role for modified proteins in the induction of apoptosis.
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- Rodgers, Kenneth J, et al.
(författare)
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Heat shock proteins : keys to healthy ageing?
- 2009
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Ingår i: REDOX REPORT. - 1351-0002. ; 14:4, s. 147-153
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Forskningsöversikt (övrigt vetenskapligt/konstnärligt)abstract
- Organisms produce reactive species throughout their lives, and this may result in damage to proteins and other biological molecules. Oxidatively damaged proteins are normally selectively degraded and replaced, but this process appears to be less efficient in senescent, long-lived post-mitotic cells, as is evidenced by their accumulation in the form of lipofuscin inside the lysosomal compartment. A great deal of research has focused on changes to the proteolytic machinery in the ageing cells in particular the proteasomes although failure of heat shock proteins (HSPs) to bind and deliver oxidised proteins efficiently to the degradation machinery could also contribute to their aggregation and accumulation. Oxidised proteins can be protease-resistant and may even directly inhibit the proteolytic machinery of the cellu The critical role that is played by HSPs in preventing accumulation of oxidised proteins is often overlooked. In this reviews we examine the key role played by HSPs in recognising, removing and preventing the formation of oxidised and damaged proteins in cells. We also examine the evidence supporting the view that failure of one of these pathways could underlie ageing and age-related diseases. Finally, we discuss how modulation of HSP-activity could influence the ageing process and the progression of age-related diseases.
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