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- Adolfsson, Göran, 1981, et al.
(författare)
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Realization of spectrally engineered semiconductor Fabry-Perot lasers with narrow geometrical tolerances
- 2011
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Ingår i: Journal of Applied Physics. - : AIP Publishing. - 0021-8979 .- 1089-7550. ; 109:9, s. 093112-
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Tidskriftsartikel (refereegranskat)abstract
- Spectrally engineered semiconductor Fabry-Perot laser resonators are designed to enhance the optical feedback for selected longitudinal modes, which thereby require less gain for lasing. This is achieved by introducing refractive index perturbations along the length of the resonator. However,the physical realization of these resonators is a challenge because of very narrow tolerances; in particular the need for precise positioning of the end facets of the resonator in relation to the perturbations, and the excess propagation loss associated with the perturbations, has been a majorconcern. We report on a method to achieve high-quality end facet mirrors enabling precise positioning relative to the perturbations, the latter which are realized as lateral corrugations of the waveguide. Measurements show that the mirror quality is comparable to that of cleaved mirrorsand that the additional loss introduced by the perturbations adds
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- Ahlsson, Fredrik, et al.
(författare)
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Gestational diabetes and offspring body disproportion
- 2010
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Ingår i: Acta Paediatrica. - : Wiley. - 0803-5253 .- 1651-2227. ; 99:1, s. 89-93
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Tidskriftsartikel (refereegranskat)abstract
- Aim: It has been demonstrated that females born large for gestational age (LGA) in weight but not length are at increased risk of being obese at childbearing age. We addressed the question whether women with gestational diabetes mellitus (GDM) are at increased risk of giving birth to such infants. Methods: Birth characteristics of 884 267 infants of non-diabetic mothers and 7817 of mothers with GDM were analysed. LGA was defined as birth weight or birth length > 2 standard deviation scores for gestational age. Multiple logistic regression analysis was performed. Results: The odds ratio (OR) for a woman with GDM to give birth to an LGA infant that was heavy alone was four times increased (OR: 3.71, 95% CI: 3.41-4.04). Furthermore, in the population of mothers giving birth to LGA infants, the proportion heavy alone was 68% in the group of women with GDM compared with 64.4% in the group of non-diabetic women. The risks were independent of gender of the foetus. Conclusion: Women with GDM have an almost four times higher risk of delivering an LGA infant that is heavy alone. The noted disproportion between weight and length in infants of such mothers may have an impact on the risk of later obesity.
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- Brülde, Bengt, 1959, et al.
(författare)
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nominalism och begreppsrealism
- 2008
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Ingår i: Liedman S, Tännsjö T & Westerståhl D (red.). Den svårfångade relativismen: en uppslagsbok. - Stockholm : Thales.
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Bokkapitel (övrigt vetenskapligt/konstnärligt)
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- Brülde, Bengt, 1959, et al.
(författare)
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socialkonstruktivism
- 2008
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Ingår i: Liedman S, Tännsjö T & Westerståhl D (red.). Den svårfångade relativismen: en uppslagsbok. - Stockholm : Thales.
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Bokkapitel (övrigt vetenskapligt/konstnärligt)
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- Brülde, Bengt, 1959, et al.
(författare)
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Värde och tid
- 2000
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Ingår i: Filosofisk tidskrift. ; 21:2, s. 3-17
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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- Carpenter, Katharine A., et al.
(författare)
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Turn structures in CGRP C-terminal analogues promote stable arrangements of key residue side chains
- 2001
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 40:28, s. 8317-8325
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Tidskriftsartikel (refereegranskat)abstract
- The 37-amino acid calcitonin gene-related peptide (CGRP) is a potent endogenous vasodilator thought to be implicated in the genesis of migraine attack. CGRP antagonists may thus have therapeutic value for the treatment of migraine. The CGRP C-terminally derived peptide [D(31),P(34),F(35)]CGRP(27-37)-NH(2) was recently identified as a high-affinity hCGRP(1) receptor selective antagonist. Reasonable CGRP(1) affinity has also been demonstrated for several related analogues, including [D(31),A(34),F(35)]CGRP(27-37)-NH(2). In the study presented here, conformational and structural features in CGRP(27-37)-NH(2) analogues that are important for hCGRP(1) receptor binding were explored. Structure-activity studies carried out on [D(31),P(34),F(35)]CGRP(27-37)-NH(2) resulted in [D(31),P(34),F(35)]CGRP(30-37)-NH(2), the shortest reported CGRP C-terminal peptide analogue exhibiting reasonable hCGRP(1) receptor affinity (K(i) = 29.6 nM). Further removal of T(30) from the peptide's N-terminus greatly reduced receptor affinity from the nanomolar to micromolar range. Additional residues deemed critical for hCGRP(1) receptor binding were identified from an alanine scan of [A(34),F(35)]CGRP(28-37)-NH(2) and included V(32) and F(37). Replacement of the C-terminal amide in this same peptide with a carboxyl, furthermore, resulted in a greater than 50-fold reduction in hCGRP(1) affinity, thus suggesting a direct role for the amide moiety in receptor binding. The conformational properties of two classes of CGRP(27-37)-NH(2) peptides, [D(31),X(34),F(35)]CGRP(27-37)-NH(2) (X is A or P), were examined by NMR spectroscopy and molecular modeling. A beta-turn centered on P(29) was a notable feature consistently observed among active peptides in both series. This turn led to exposure of the critical T(30) residue to the surrounding environment. Peptides in the A(34) series were additionally characterized by a stable C-terminal helical turn that resulted in the three important residues (T(30), V(32), and F(37)) adopting consistent interspatial positions with respect to one another. Peptides in the P(34) series were comparatively more flexible at the C-terminus, although a large proportion of the [D(31),P(34),F(35)]CGRP(27-37)-NH(2) calculated conformers contained a gamma-turn centered on P(34). These results collectively suggest that turn structures at both the C-terminus and N-terminus of CGRP(27-37)-NH(2) analogues may help to appropriately orient critical residues (T(30), V(32), and F(37)) for hCGRP(1) receptor binding.
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