| 1. |
- Kang, J, et al.
(författare)
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Total chemical synthesis and NMR characterization of the glycopeptide tx5a, a heavily post-translationally modified conotoxin, reveals that the glycan structure is alpha-D-Gal-(1 -> 3)-alpha-D-GalNAc
- 2004
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Ingår i: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 271:23-24, s. 4939-4949
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Tidskriftsartikel (refereegranskat)abstract
- The 13-amino acid glycopeptide tx5a (Gla-Cys-Cys-Gla-Asp-Gly-Trp*-Cys-Cys-Thr*-Ala-Ala-Hyp-OH, where Trp* = 6-bromotryptophan and Thr* = Gal-GalNAc-threonine), isolated from Conus textile, causes hyperactivity and spasticity when injected intracerebral ventricularly into mice. It contains nine post-translationally modified residues: four cysteine residues, two gamma-carboxyglutamic acid residues, and one residue each of 6-bromotryptophan, 4-trans-hydroxyproline and glycosylated threonine. The chemical nature of each of these has been determined with the exception of the glycan linkage pattern on threonine and the stereochemistry of the 6-bromotryptophan residue. Previous investigations have demonstrated that tx5a contains a disaccharide composed of N-acetylgalactosamine (GalNAc) and galactose (Gal), but the interresidue linkage was not characterized. We hypothesized that tx5a contained the T-antigen, beta-D-Gal-(1-->3)-alpha-D-GalNAc, one of the most common O-linked glycan structures, identified previously in another Conus glycopeptide, contalukin-G. We therefore utilized the peracetylated form of this glycan attached to Fmoc-threonine in an attempted synthesis. While the result-ing synthetic peptide (Gla-Cys-Cys-Gla-Asp-Gly-Trp*-Cys-Cys-Thr*-Ala-Ala-Hyp-OH, where Trp* =6-bromotryptophan and Thr* = beta-D-Gal-(1-->3)-alpha-D-GalNAc-threonine) and the native peptide had almost identical mass spectra, a comparison of their RP-HPLC chromatograms suggested that the two forms were not identical. Two-dimensional H-1 homonuclear and C-13-H-1 heteronuclear NMR spectroscopy of native tx5a isolated from Conus textile was then used to determine that the glycan present on tx5a indeed is not the aforementioned T-antigen, but rather alpha-D-Gal-(1-->3)-alpha-D-GalNAc.
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| 2. |
- Stasiewicz, K, et al.
(författare)
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Small Scale Alfvenic structure in the aurora
- 2000
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Ingår i: Space Science Reviews. - : KLUWER ACADEMIC PUBL. - 0038-6308. ; 92:3-4, s. 423-533
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Tidskriftsartikel (refereegranskat)abstract
- This paper presents a comprehensive review of dispersive Alfven waves in space and laboratory plasmas. We start with linear properties of Alfven waves and show how the inclusion of ion gyroradius, parallel electron inertia, and finite frequency effects mo
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| 3. |
- Stenflo, Lennart, et al.
(författare)
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Nonlinear beam generated plasma waves as a source for enhanced plasma and ion acoustic lines
- 2011
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Ingår i: Physics of Plasmas. - : American Institute of Physics (AIP). - 1070-664X .- 1089-7674. ; 18:15, s. 052107-1-052107-14
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Tidskriftsartikel (refereegranskat)abstract
- Observations by, for instance, the EISCAT Svalbard Radar (ESR) demonstrate that the symmetry of the naturally occurring ion line in the polar ionosphere can be broken by an enhanced, nonthermal, level of fluctuations (naturally enhanced ion-acoustic lines, NEIALs). It was in many cases found that the entire ion spectrum can be distorted, also with the appearance of a third line, corresponding to a propagation velocity significantly slower than the ion acoustic sound speed. It has been argued that selective decay of beam excited primary Langmuir waves can explain some phenomena similar to those observed. We consider a related model, suggesting that a primary nonlinear process can be an oscillating two-stream instability, generating a forced low frequency mode that does not obey any ion sound dispersion relation. At later times, the decay of Langmuir waves can give rise also to enhanced asymmetric ion lines. The analysis is based on numerical results, where the initial Langmuir waves are excited by a cold dilute electron beam. By this numerical approach, we can detect fine details of the physical processes, in particular, demonstrate a strong space-time intermittency of the electron waves in agreement with observations. Our code solves the full Vlasov equation for electrons and ions, with the dynamics coupled through the electrostatic field derived from Poisson's equation. The analysis distinguishes the dynamics of the background and beam electrons. This distinction simplifies the analysis for the formulation of the weakly nonlinear analytical model for the oscillating two-stream instability. The results have general applications beyond their relevance for the ionospheric observations.
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| 4. |
- Astermark, Jan, et al.
(författare)
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Effects of gamma-carboxyglutamic acid and epidermal growth factor-like modules of factor IX on factor X activation. Studies using proteolytic fragments of bovine factor IX
- 1992
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Ingår i: Journal of Biological Chemistry. - 1083-351X. ; 267:5, s. 3249-3256
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Tidskriftsartikel (refereegranskat)abstract
- Factor IX is a vitamin K-dependent zymogen of a serine protease. The NH2-terminal half of the molecule consists of a Ca(2+)-binding gamma-carboxyglutamic acid (Gla)-containing module and two modules homologous to the epidermal growth factor (EGF) precursor. To elucidate the role of these non-catalytic modules of factor IXa beta in factor X activation, we have isolated and characterized fragments of bovine factor IX, containing one or both of the EGF-like modules as well as these modules linked to the Gla module. The fragments were used as inhibitors of factor IXa beta-mediated factor X activation in a plasma clotting system and in systems with purified components of the Xase complex. Fragments consisting of either the two EGF-like modules of factor IX linked together or the NH2-terminal EGF-like module alone were found to inhibit factor Xa generation both in the presence and absence of the cofactor, factor VIIIa. Moreover, a fragment consisting of the corresponding modules of factor X had a similar effect. We therefore propose that factor IXa beta and factor X interact directly through their EGF-like modules on or in the vicinity of a phospholipid surface. We have also found that the isolated Gla module of factor IX inhibits the formation of factor Xa both in the presence and absence of phospholipid but not in the absence of factor VIIIa. Our results are compatible with a model of the Xase complex, in which both the serine protease part and the Gla module of factor IXa beta interact with factor VIIIa.
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| 5. |
- Astermark, Jan, et al.
(författare)
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The gamma-carboxyglutamic acid and epidermal growth factor-like modules of factor IXa beta. Effects on the serine protease module and factor X activation
- 1994
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Ingår i: Journal of Biological Chemistry. - 1083-351X. ; 269:5, s. 3682-3689
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Tidskriftsartikel (refereegranskat)abstract
- Blood coagulation factors IX and X are two serine proteases with a similar modular structure. The non-catalytic part of each protein consists of a gamma-carboxyglutamic acid (Gla)-containing module and two modules homologous to the epidermal growth factor (EGF) precursor. We have now found that the NH2-terminal EGF-like module of both factors IX and X inhibits factor Xa formation in a Gla-independent manner, both in the presence and absence of phospholipid and the cofactor, factor VIIIa. In contrast, the COOH-terminal EGF-like module has no such effect. Our data indicate that the NH2-terminal EGF-like module of factor IXa beta interacts either with the corresponding module or with the serine protease module in the substrate, factor X, without affecting the hydrolysis of low molecular weight substrates. Using antibodies as structural probes, we found that Ca2+ binding to the Gla module of factor IXa beta induces a conformational transition in the serine protease module. No evidence was found for a direct interaction between the Gla module and factor VIIIa. We therefore propose that the Gla module in factor IXa beta is indirectly involved in the cofactor interaction, in that Ca2+ binding to sites in this module induces a conformation in the serine protease module that is commensurate with factor VIIIa interaction. In addition, the immunochemical approach revealed a Gla-independent Ca2+ binding site in the serine protease module (apparent Kd of approximately 120 microM) that also might influence its conformation. Antibodies against the EGF-like modules of factor IX were used to probe Ca2+ binding to these modules in intact and in Gla-domainless factor IXa beta. The data indicate a Ca2+ binding site with an apparent Kd of approximately 50 microM in the NH2-terminal EGF-like module of both factor IX species.
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| 6. |
- Edenbrandt, Carl-Magnus, et al.
(författare)
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Molecular analysis of the gene for vitamin K dependent protein S and its pseudogene. Cloning and partial gene organization
- 1990
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Ingår i: Biochemistry. - 0006-2960. ; 29:34, s. 8-7861
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Tidskriftsartikel (refereegranskat)abstract
- Protein S is a vitamin K dependent plasma protein and a cofactor to activated protein C, a serine protease that regulates blood coagulation. The haploid genome contains two protein S genes (alpha and beta) with the protein S alpha-gene corresponding to the cloned cDNA. We have now isolated and mapped overlapping genomic clones that cover an area of 50 kilobases of the protein S alpha-gene which code for the 3' part of the gene, i.e., the thrombin-sensitive region, the four domains that are homologous to the epidermal growth factor (EGF) precursor, the COOH-terminal part of protein S that is homologous to a plasma sex hormone binding globulin (SHBG), and, finally, the 3' untranslated region. The thrombin-sensitive region and the EGF-like domains are each coded on a separate exon. The sizes of the exons coding for the COOH-terminal half of protein S and the location of the introns are nearly identical with those in the homologous SHBG gene. Furthermore, the phase class of the splice junctions is the same in these two genes. We have also isolated and mapped genomic clones that cover 25 kilobases of the protein S beta-gene, which was found to contain stop codons and a 2 bp deletion which introduces a frame shift, suggesting that it is a pseudogene. The structure of the two protein S genes and a comparison with the vitamin K dependent clotting factors support a model for their origin by exon shuffling and recruitment of the 3' part of the gene from an ancestor shared with the sex hormone binding globulin.
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| 7. |
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| 8. |
- Eliasson, B, et al.
(författare)
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Preface to special issue
- 2013
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Ingår i: Journal of Plasma Physics. - : Cambridge University Press. - 0022-3778 .- 1469-7807. ; 79:6, s. 981-981
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- This special issue is devoted to the memory of Professor Padma Kant Shukla, who passed away 26 January 2013 on his travel to New Delhi, India to receive the prestigious Hind Rattan (Jewel of India) award. Padma was born in Tulapur, Uttar Pradesh, India, 7 July 1950, where he grew up and got his education. He received a PhD degree in Physics at the Banaras Hindu University, Varanasi, Uttar Pradesh, India, in 1972, under the supervision of late Prof. R. N. Singh, and a second PhD degree in Theoretical Plasma Physics from Umeå University in Sweden in 1975, under the supervision of Prof. Lennart Stenflo. He worked at the Faculty of Physics & Astronomy, Ruhr-University Bochum, Germany since January 1973, where he was a permanent faculty member and Professor of International Affairs, a position that was created for him to honour his international accomplishments and reputation.
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| 9. |
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| 10. |
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