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Träfflista för sökning "WFRF:(Stefan W) srt2:(1995-1999)"

Search: WFRF:(Stefan W) > (1995-1999)

  • Result 1-10 of 19
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2.
  • Li, Y, et al. (author)
  • Yeast global transcriptional regulators Sin4 and Rgr1 are components of mediator complex/RNA polymerase II holoenzyme.
  • 1995
  • In: Proceedings of the National Academy of Sciences of the United States of America. - 0027-8424 .- 1091-6490. ; 92:24, s. 10864-8
  • Journal article (peer-reviewed)abstract
    • Sin4 and Rgr1 proteins, previously shown by genetic studies to play both positive and negative roles in the transcriptional regulation of many genes, are identified here as components of mediator and RNA polymerase II holoenzyme complexes. Results with Sin4 deletion and Rgr1 truncation strains indicate the association of these proteins in a subcomplex comprising Sin4, Rgr1, Gal11, and a 50-kDa polypeptide. Taken together with the previous genetic evidence, our findings point to a role of the mediator in repression as well as in transcriptional activation.
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3.
  • Nilsson, Annika, 1969, et al. (author)
  • Optical properties of human whole blood - Changes due to slow heating
  • 1996
  • In: LASER-TISSUE INTERACTION AND TISSUE OPTICS II, PROCEEDINGS OF. - : SPIE. - 0819423254 ; 2923, s. 24-34
  • Conference paper (peer-reviewed)abstract
    • Optical properties of human whole blood were measured in vitro, at 633 nm with a double integrating sphere set-up, The blood was kept at constant flow through a flow cell while slowly heating the blood from approximately 25 degrees C to 55 degrees C in a heat exchanger, The results show a small but distinct decrease in the g-factor of 1.7 +/- 0.6\% and a similar increase in the scattering coefficient, mu(s), of 2.9 +/- 0.6\% at approximately 45-46 degrees C. When studying the thermal effect on the blood cells under a white-light transmission microscope, the changes in the scattering properties could be correlated to a sudden change in the shape of the red blood cells, from disc-shaped to spherical, at approximately the same temperature. Furthermore, a continuous manifest increase in the absorption coefficient, mu(a), was seen with temperature rise, on average 83.8 +/- 68.1\% when reaching the temperature 50 degrees C. This might be due to heat-induced haemolysis of the red blood cells, resulting in free light absorbing haemoglobin in the surrounding plasma and thus higher effective light absorption.
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6.
  • Borowiec, Jan W., et al. (author)
  • Circulating cytokines and granulocyte-derived enzymes during complex heart surgery : A clinical study with special reference to heparin-coating of cardiopulmonary bypass circuits
  • 1995
  • In: Scandinavian journal of thoracic and cardiovascular surgery. - 0036-5580. ; 29:4, s. 167-174
  • Journal article (peer-reviewed)abstract
    • Blood contact with artificial surfaces during cardiopulmonary bypass (CPB) triggers a systemic inflammatory response in which complement, granulocytes and cytokines play a major role. Heparin-coated CPB circuits were recently shown to reduce complement and granulocyte activation in such circumstances. The present study comprised 20 complex heart operations, 10 with heparin-coated circuits (group HC) and 10 controls (group C), with evaluation of changes in terminal complement complex, the granulocyte enzymes myeloperoxidase and lactoferrin, and the cytokines interleukin-6 (IL-6) and interleukin-8 (IL-8). Standard heparin dose and uncoated cardiotomy reservoir were used in all cases. In both groups the levels of enzymes and terminal complement complex rose significantly, beginning at conclusion of CPB, above base values, without significant intergroup differences. IL-6 and IL-8 also increased significantly, but tended to be lower in the HC group, starting at CPB end and continuing until 20 hours postoperatively: for IL-6 the difference was significant at CPB end (83 +/- 18 vs 197 +/- 39 micrograms/l, p = 0.21). Significantly increased inflammatory response was thus found during complex heart operations even with use of heparin-coated CPB sets. The heparin-coating of circuits seems to diminish cytokine production.
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7.
  • Graner, Michael W., et al. (author)
  • Splice variants of the Drosophila PS2 integrins differentially interact with RGD-containing fragments of the extracellular proteins tiggrin, Ten-m, and D-laminin α2
  • 1998
  • In: Journal of Biological Chemistry. - : Elsevier BV. - 0021-9258. ; 273:29, s. 18235-18241
  • Journal article (peer-reviewed)abstract
    • Two new potential ligands of the Drosophila PS2 integrins have been characterized by functional interaction in cell culture. These potential ligands are a new Drosophila laminin α2 chain encoded by the wing blister locus and Ten-m, an extracellular protein known to be involved in embryonic pattern formation. As with previously identified PS2 ligands, both contain RGD sequences, and RGD-containing fragments of these two proteins (DLAM-RGD and TENM-RGD) can support PS2 integrin-mediated cell spreading. In all cases, this spreading is inhibited specifically by short RGD-containing peptides. As previously found for the PS2 ligand tiggrin (and the tiggrin fragment TIG- RGD), TENM-RGD induces maximal spreading of cells expressing integrin containing the α(PS2C) splice variant. This is in contrast to DLAM-RGD, which is the first Drosophila polypeptide shown to interact preferentially with cells expressing the α(PS2) (M8) splice variant. The β(PS) integrin subunit also varies in the presumed ligand binding region as a result of alternative splicing. For TIG-RGD and TENM-RGD, the β splice variant has little effect, but for DLAM-RGD, maximal cell spreading is supported only by the β(PS4A) form of the protein. Thus, the diversity in PS2 integrins due to splicing variations, in combination with diversity of matrix ligands, can greatly enhance the functional complexity of PS2-ligand interactions in the developing animal. The data also suggest that the Splice variants may alter regions of the subunits that are directly involved in ligand interactions, and this is discussed with respect to models of integrin structure.
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8.
  • Graner, Michael W., et al. (author)
  • Splice variants of the Drosophila PS2 integrins differentially interact with the extracellular ligands Tiggrin, D-laminin alpha 2 and Ten-m.
  • 1998
  • In: Journal of Biological Chemistry. - 1083-351X. ; 273:29, s. 18235-18241
  • Journal article (peer-reviewed)abstract
    • Two new potential ligands of theDrosophila PS2 integrins have been characterized by functional interaction in cell culture. These potential ligands are a new Drosophila laminin α2 chain encoded by the wing blister locus and Ten-m, an extracellular protein known to be involved in embryonic pattern formation. As with previously identified PS2 ligands, both contain RGD sequences, and RGD-containing fragments of these two proteins (DLAM-RGD and TENM-RGD) can support PS2 integrin-mediated cell spreading. In all cases, this spreading is inhibited specifically by short RGD-containing peptides. As previously found for the PS2 ligand tiggrin (and the tiggrin fragment TIG-RGD), TENM-RGD induces maximal spreading of cells expressing integrin containing the αPS2C splice variant. This is in contrast to DLAM-RGD, which is the first Drosophila polypeptide shown to interact preferentially with cells expressing the αPS2 m8 splice variant. The βPS integrin subunit also varies in the presumed ligand binding region as a result of alternative splicing. For TIG-RGD and TENM-RGD, the β splice variant has little effect, but for DLAM-RGD, maximal cell spreading is supported only by the βPS4A form of the protein. Thus, the diversity in PS2 integrins due to splicing variations, in combination with diversity of matrix ligands, can greatly enhance the functional complexity of PS2-ligand interactions in the developing animal. The data also suggest that the splice variants may alter regions of the subunits that are directly involved in ligand interactions, and this is discussed with respect to models of integrin structure.
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9.
  • Gustafson, Stefan, et al. (author)
  • ICAM-1 is a cell-surface receptor for hyaluronan.
  • 1995
  • In: 6th Interscience World Conference on Inflammation, Antirheumatics, Analgesics, Immunomodulators, Geneva, Switzerland, 28-30 March, Abstract. ; 160, s. 28-
  • Review (other academic/artistic)
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  • Result 1-10 of 19
Type of publication
journal article (13)
other publication (2)
conference paper (2)
book chapter (1)
review (1)
Type of content
peer-reviewed (15)
other academic/artistic (4)
Author/Editor
Lohmander, L. Stefan (3)
Gustafson, Stefan (3)
Forsberg, Nina (3)
Wikstrom, Tarja (3)
McCourt, Peter (3)
Baumgartner, Stefan (2)
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Venge, Per (2)
Madsen, K. (2)
Seipel, Stefan (2)
Thelin, Stefan (2)
Borowiec, Jan W. (2)
Schneider, W (2)
Graner, Michael W. (2)
Bunch, Thomas A. (2)
Kerschen, Arthur (2)
Brower, Danny L. (2)
Li, Y. (1)
Kim, Y. J. (1)
Abrahamson, Magnus (1)
Andersson-Engels, St ... (1)
Froneman, P. W (1)
Pakhomov, E. A. (1)
Dahlberg, Leif (1)
Roos, Harald (1)
Gössling, Stefan (1)
Katzir, A (1)
Nilsson, Annika, 196 ... (1)
Malfertheiner, P (1)
Nilsson, Leif (1)
Karlsson, Stefan (1)
Koch, S (1)
Lindqvist, Ulla (1)
Graf, W. (1)
Stefan, Lohmander L. (1)
Borgström, Anders (1)
Appelros, Stefan (1)
Tötterman, Thomas H. (1)
Bach, W (1)
Ek, Bo (1)
Bertilsson, Stefan, ... (1)
Friess, H (1)
Uhl, W (1)
Büchler, M W (1)
Hagman, Leif (1)
Pekna, M. (1)
Wagner, IV (1)
Peterson, Christer (1)
Sandy, John D (1)
Mumford, Richard A. (1)
Lilja, K (1)
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University
Lund University (10)
Uppsala University (6)
University of Gävle (2)
Umeå University (1)
Linköping University (1)
Chalmers University of Technology (1)
Language
English (17)
German (1)
French (1)
Research subject (UKÄ/SCB)
Medical and Health Sciences (6)
Natural sciences (3)
Social Sciences (2)

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