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| 2. |
- Hill, Russell, et al.
(författare)
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Origin of Life
- 1994
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Ingår i: Nature. - 0028-0836 .- 1476-4687. ; 371, s. 646-
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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| 3. |
- Lindahl, B. I. B., et al.
(författare)
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Mind as a Force Field : Comments on a New Interactionistic Hypothesis
- 1994
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Ingår i: Journal of Theoretical Biology. - London : Academic Press. - 0022-5193 .- 1095-8541. ; 171, s. 111-122
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Tidskriftsartikel (refereegranskat)abstract
- The survival and development of consciousness in biological evolution call for an explanation. An interactionistic mind-brain theory seems to have the greatest explanatory value in this context.An interpretation of an interactionistic hypothesis, recently proposed by Karl Popper, is discussed both theoretically and based on recent experimental data. In the interpretation, the distinction between the conscious mind and the brain is seen as a division into what is subjective and what is objective, and not as an ontological distinction between something immaterial and something material. The interactionistic hypothesis is based on similarities between minds and physical forces. The conscious mind is understood to interact with randomly spontaneous spatio-temporal patterns of action potentials through an electromagnetic field. Consequences and suggestions for future studies are discussed.
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| 4. |
- Lindahl, B. I. B., et al.
(författare)
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Multiple Cause-of-Death Data as a Tool for Detecting Artificial Trends in the Underlying Cause Statistics : A Methodological Study
- 1994
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Ingår i: Scandinavian Journal of Public Health. - : SAGE Publications. - 1403-4948 .- 1651-1905. ; 22:2, s. 145-158
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Tidskriftsartikel (refereegranskat)abstract
- The aims of the study were: (i) to identify trends in the underlying cause-of-death statistics that are due to changes in the coders’ selection and coding of causes, and (ii) to identify changes in the coders’ documented registration principles that can explain the observed trends in the statistics.31 Basic Tabulation List categories from the Swedish national cause-of-death register for 1970-1988 were studied. The coders’ tendency to register a condition as the underlying cause of death (the underlying cause ratio) was estimated by dividing the occurrence of the condition as underlying cause (the underlying cause rate) with the total registration of the condition (the multiple cause rate). When the development of the underlying cause rate series followed more closely the underlying cause ratio series than the multiple cause rate series, and a corresponding change in the registration rules could be found, rhe underlying cause rate trend was concluded to be due to changes in the coders’ tendency to register the condition.For thirteen categories (fourteen trends), the trends could be explained by changes in the coders’ interpretation practice: five upward, four insignificant, and five downward trends. In addition, for three categories the trends could be explained by new explicit ICD-9 rules.
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| 5. |
- Akerström, B, et al.
(författare)
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Binding properties of protein Arp, a bacterial IgA-receptor
- 1991
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Ingår i: Molecular Immunology. - 0161-5890. ; 28:4-5, s. 57-349
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Tidskriftsartikel (refereegranskat)abstract
- A cell surface receptor that binds to the Fc region of IgA is expressed by certain strains of group A streptococci. The physico-chemical properties and binding characteristics of this receptor, called protein Arp, were studied. Like bacterial receptors that bind IgG, protein Arp has an elongated shape and no disulfide bonds. The affinity constant of protein Arp for three different molecular forms of IgA was determined, and was found to be more than ten-fold higher for serum IgA than for two complexed forms of IgA: secretory IgA and IgA bound to alpha 1-microglobulin. Cleavage of protein Arp with CNBr resulted in a peptide corresponding to the region located outside the cell wall, except for the N-terminal 52 amino acids. This CNBr-fragment did not bind IgA, which strongly suggests that the IgA-binding region of protein Arp is located in the N-terminal part of the molecule. In addition to the binding of IgA, protein Arp also binds to IgG weakly. The pH-dependence of these two types of binding is different, with maximal binding of IgA at neutral pH (5-7) and maximal binding of IgG at acidic pH (3-5). Both for IgA and IgG, protein Arp shows strong specificity for immunoglobulins of human origin.
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| 6. |
- Akerström, B, et al.
(författare)
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Protein Arp and protein H from group A streptococci. Ig binding and dimerization are regulated by temperature
- 1992
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Ingår i: Journal of immunology. - 0022-1767. ; 148:10, s. 43-3238
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Tidskriftsartikel (refereegranskat)abstract
- Cell surface proteins that bind to the Fc part of Ig are expressed by many strains of group A streptococci, an important human pathogen. Two such bacterial strains, AP4 and AP1, were shown to bind IgA and IgG, respectively, in a temperature-dependent manner. The binding of radiolabeled Ig to the bacterial cells was lower at 37 degrees C than at 22 and 4 degrees C. Similarly, protein Arp, the IgA-binding protein isolated from strain AP4, and protein H, the IgG-binding protein isolated from strain AP1, displayed a strong Ig-binding at 22 degrees C and lower temperatures, and virtually no binding at all at 37 degrees C. The effect was reversible: lowering of the temperature restored the binding and vice versa. A gradual shift between binding and nonbinding took place between 27 and 37 degrees C. Gel chromatography and velocity sedimentation centrifugation showed that protein Arp and protein H appeared as noncovalently associated dimers at 10 and 22 degrees C, and as monomers at 37 degrees C. These results strongly suggest that the dimerization of protein Arp and protein H, rather than the low temperature itself, yielded the strong Ig-binding of the proteins at 10 and 22 degrees C. Indeed, after covalent cross-linking of the dimers at 10 degrees C by incubation with low concentrations of glutaraldehyde, full Ig-binding was achieved even at 37 degrees C. A carboxyl-terminal proteolytic fragment of protein Arp, which completely lacked the IgA-binding capacity at any temperature, showed the same temperature-dependent dimerization as intact protein Arp, suggesting that the Ig-binding part of the protein is not required for dimerization. The implications of these results for the function of Ig-binding group A streptococcal proteins, and their role in the host-parasite relationship are discussed.
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