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| 2. |
- Bremer, Kåre, et al.
(author)
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An ordinal classification for the families of flowering plants
- 1998
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In: ANNALS OF THE MISSOURI BOTANICAL GARDEN. - : MISSOURI BOTANICAL GARDEN. - 0026-6493. ; 85:4, s. 531-553
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Journal article (other academic/artistic)abstract
- Recent cladistic analyses are revealing the phylogeny of flowering plants in increasing detail, and there is support for the monophyly of many major groups above the family level. With many elements of the major branching sequence of phylogeny established
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| 4. |
- Hall, Anders, et al.
(author)
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Structural basis for different inhibitory specificities of human cystatins C and D
- 1998
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In: Biochemistry. - 0006-2960. ; 37:12, s. 4071-4079
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Journal article (peer-reviewed)abstract
- Human cystatins C and D share almost identical primary structures of two out of the three segments proposed to be of importance for enzyme interactions but have markedly different profiles for inhibition of the target cysteine peptidases, cathepsins B, H, L, and S. To investigate if the N-terminal binding regions of the inhibitors are responsible for the different inhibition profiles, and thereby confer biological selectivity, two hybrid cystatins were produced in Escherichia coli expression systems. In one hybrid, the N-terminal segment of cystatin C was placed on the framework of cystatin D, and the second was engineered with the N-terminal segment of cystatin D on the cystatin C scaffold. Truncated cystatin C and D variants, devoid of their N-terminal segments, were obtained by incubation with glycyl endopeptidase and isolated, in a second approach to assess the importance of the N-terminal binding regions for cystatin function and specificity. The affinities of the four cystatin variants for cathepsins B, H, L, and S were measured. By comparison with corresponding results for wild-type cystatins C and D, it was concluded (1) that both the N-terminal and framework part of the molecules significantly contribute to the observed differences in inhibitory activities of cystatins C and D and (2) that the N-terminal segment of cystatin C increases the inhibitory activity of cystatin D against cathepsin S and cathepsin L but results in decreased activity against cathepsin H. These differences in specificity were explained by the residues interacting with the S2 subsite of peptidases (Val- and Ala-10 in cystatin C and D, respectively). Also, removal of the N-terminal segment results in total loss of enzyme affinity for cystatin D but not for cystatin C. Therefore, structural differences in the framework parts, as well as in the N-terminal segments, are critical for both inhibitory specificity and potency. Homology modeling was used to identify residues likely responsible for the generally reduced inhibitory potency of cystatin D.
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| 5. |
- Thorell, Anders, et al.
(author)
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Exerciseand insulin cause GLUT-4 translocation in human skeletal muscle
- 1999
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In: American Journal of Physiology. - : American Physiological Society. - 0002-9513 .- 2163-5773. ; 277:4, s. E733-E741
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Journal article (peer-reviewed)abstract
- Studies in rodents have established that GLUT-4 translocation is the major mechanism by which insulin and exercise increase glucose uptake in skeletal muscle. In contrast, much less is known about the translocationphenomenon in human skeletal muscle. In the current study, nine healthy volunteers were studied on two different days. On one day, biopsies of vastus lateralis muscle were taken before and after a 2-h euglycemic- hyperinsulinemic clamp (0.8 mU · kg-1 · min-1). On another day, subjects exercised for 60 min at 70% of maximal oxygen consumption (VO(2max)), a biopsy was obtained, and the same clamp and biopsy procedure was performed as that during the previous experiment. Compared with insulin treatment alone, glucose infusion rates were significantly increased during the postexercise clamp for the periods 0-30 min, 30-60 min, and 60-90 min, but not during the last 30 min of the clamp. Plasma membrane GLUT-4 content was significantly increased in response to physiological hyperinsulinemia (32% above rest), exercise (35%), and the combination of exercise plus insulin(44%). Phosphorylation of Akt, a putative signaling intermediary for GLUT-4 translocation, was increased inresponse to insulin (640% above rest), exercise (280%), and exercise plus insulin (1,000%). These data demonstrate that two normal physiological conditions, moderate intensity exercise and physiological hyperinsulinemia ~56 μU/ml, cause GLUT-4 translocation and Akt phosphorylation in human skeletal muscle.
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| 7. |
- Andrews, L, et al.
(author)
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Infrared spectra of cis and trans-(NO)(2)(-) anions in solid argon
- 1998
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In: Journal of Chemical Physics. - 1089-7690 .- 0021-9606. ; 109:1, s. 177-185
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Journal article (peer-reviewed)abstract
- Laser-ablation of over 20 different metal targets with concurrent 10 K codeposition of Ar/NO mixtures produces metal independent infrared bands at 1589.3 cm−1 due to (NO)2+, a new absorption at 1221.0 cm−1, and a band set at 1300.3, 1222.7, 884.4 cm−1. The latter bands decrease more on annealing than the 1221.0 cm−1 band. Isotopic substitution (14NO,15NO, 15N18O, and mixtures) shows that these new vibrations involve two equivalent N–O oscillators, which identifies two new (NO)2 species. The excellent agreement with frequencies, intensities, and isotopic frequency ratios from density functional theory calculations substantiates assignment of the 1221.0 cm−1 band to trans-(NO)2− and the three band set to cis-(NO)2−. The observation of a weak combination band at 2492.0 cm−1 further substantiates assignment of the two N–O stretching modes in cis-(NO)2−
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