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- Carlström, Göran, et al.
(författare)
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[7] NMR studies of complex DNA structures : The holliday junction intermediate in genetic recombination
- 1995
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Ingår i: Methods in Enzymology : Nuclear Magnetic Resonance and Nucleic Acids - Nuclear Magnetic Resonance and Nucleic Acids. - 0076-6879. - 9780121821623 ; 261, s. 163-182
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Bokkapitel (refereegranskat)abstract
- Publisher Summary This chapter discusses the current status, of using nuclear magnetic resonance (NMR), to study the structure and dynamics of the holliday junction (HJ). Complex deoxyribonucleic acid (DNA) structures (e.g., triplexes, quadruplexes, junctions) pose difficult problems for study, by NMR, relative to the typical DNA duplexes, because they have nonstandard or distorted local conformations and higher molecular weights that give rise to large resonance linewidths and severe 1H spectral overlap. With more atoms in the system, both assignment and structure calculation become more challenging. The HJ, a four-arm DNA crossover structure, is a transient intermediate formed in the course of genetic recombination as well as during other cellular processes, such as replication and telomere resolution. A significant body of evidence has accumulated, indicating that the structure at the junction has a central role, in determining the outcome of these cellular events. For NMR studies, the titration of the four component 16-mer strands to create an equimolar mixture is critical. Gel electrophoresis has shown that titrations based on the standard ultraviolet (UV) estimates of strand concentrations result in significant amounts of residual single-strand, half-complementary duplex, and three-arm structures.
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- Duan, Rui-Dong, et al.
(författare)
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Sphingolipid hydrolysis enzymes in the gastrointestinal tract
- 1999
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Ingår i: Methods in Enzymology. - 0076-6879. ; 311, s. 276-286
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Forskningsöversikt (refereegranskat)abstract
- In the intestinal tract, there are enzymes that hydrolyze both endogenous and exogenous sphingolipids. The alkaline sphingomyelinases (SMase) of the gut and human bile have been most studied, and a major part of this chapter discusses these enzymes. It also discusses studies of ceramidase, glycosylceramidase, and the digestion of dietary sphingolipids. In the intestinal tract, a distinct enzyme that hydrolyzes SM was discovered in 1969 by Nilsson and named “alkaline SMase.” The alkaline SMase activity is localized specifically in the intestinal tract and is not detectable in other organs, including brain, kidney, lung, spleen, testis, pancreas, and stomach, or in milk and urine. The intestinal alkaline SMase is not bacterial in origin as similar activity is found in ordinary mice and germ-free mice and in meconium of human fetus as early as 26 weeks of gestation. In the intestines of different experimental animals, the highest activities were in rat, mouse, pig, and baboon, lower activity in rabbit, and little activity in the guinea pig. Whether these species differences indicate genetic variation or an influence of diet composition on the expression of the enzyme in the intestine is unknown.
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- Leffler, Hakon, et al.
(författare)
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Strategies for studying bacterial adhesion in Vivo
- 1995. - C
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Ingår i: Adhesion of Microbial Pathogens. - 0076-6879. ; 253, s. 206-220
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Bokkapitel (refereegranskat)abstract
- The ultimate goal of studies on microbial adhesion is to understand what molecular interactions between the host and microbe occur in vivo and the impact of these interactions on disease processes. With this goal in mind, the problem can be approached at four levels. At the biochemical level, the host receptors at the relevant colonization site are identified; at the cell biology level, consequences of bacterial binding to host epithelial cells are studied in cell culture; at the physiological level, the consequences of bacterial binding are studied in experimental animals or humans; and at the population level, the consequences of receptor binding for colonization are studied by epidemiological methods. This chapter provides an example of studies at each level and discusses the implications for what might occur in vivo.
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- HOLMGREN, A, et al.
(författare)
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Glutaredoxin
- 1995
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Ingår i: Methods in enzymology. - : Elsevier. - 0076-6879. ; 252, s. 283-292
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Tidskriftsartikel (refereegranskat)
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