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1

Evaluation of the antibacterial activity of cystatin against selected strains of Escherichia coli

100%
Szpak M., Trziszka T., Polanowski A., Grubek J., Golab K., Juszczynska K., Janik P., Malicki A., Szyplik K.
Folia Biologica
|
2014
|
tom 62
|
nr 3
2

Isolation of the homogeneous constituents from non-diffusible sugar-peptide (NSP) fraction originating from bovine plasma. IV. The influence on cell growth of REF and R-XC cells in vitro

100%
Branny J., Klein A., Kawecka M., Wojcik M.
Folia Histochemica et Cytobiologica
|
1985
|
tom 23
|
nr 1-2
3
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Content available

The occurrence of the viruses in tulip crops in Poland

84%
Sochacki D.
Journal of Horticultural Research
|
2013
|
tom 21
|
nr 1
4

Effect of pretreatment of wells in polystyrene plates on adsorption of some human serum proteins

84%
Kochanowska I. E., Rapak A., Szewczuk A.
Archivum Immunologiae et Therapiae Experimentalis
|
1994
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tom 42
|
nr 2
5

Partial reversal of transformed fusiform phenotype by overexpression of calreticulin

84%
Opas M., Fadel M. P.
Cellular and Molecular Biology Letters
|
2007
|
tom 12
|
nr 2
Calreticulin, a Ca2+-storage and chaperone protein of the ER, has also been shown to affect cell adhesiveness. To examine the effects of differential expression of calreticulin on cellular adhesiveness, we used L fibroblast cell lines stably expressing either elevated or reduced amounts of full length, ER-targeted calreticulin. Overexpression of calreticulin correlates with an increase in adhesiveness of L fibroblasts such that these transformed cells acquire epithelioid morphology and form an epithelial-cell sheet when crowded. Functionally, the “reversal” of transformed phenotype in L fibroblasts differentially overexpressing calreticulin can be accounted for by changes in levels of expression of N-cadherin and vinculin. Structurally, however, although the form and extent of cell-cell contacts in L fibroblasts overexpressing calreticulin mimicked those in normal epithelia, electron microscopical examination revealed that cell-cell junctions formed by these transformed cells bore only superficial resemblance to those of normal epithelia in culture. Our data imply that overexpression of calreticulin, while partially reverses fusiform transformed phenotype is in itself insufficient to re-establish bona fide zonulae adherens in transformed fibroblasts.
6

Description of Paramoeba atlantica n. sp. (Amoebozoa, Dactylopodida) – a marine amoeba from the Eastern Atlantic, with emendation of the dactylopodid families

67%
Kudryavtsev A., Pawlowski J., Hausmann K.
Acta Protozoologica
|
2011
|
tom 50
|
nr 3
7

Possible immunomodulating effect of retinol on cytokines secretion in patients with recurrent furunculosis

67%
Nowicka D., Grywalska E., Hymos A., Mielnik M., Rolinski J.
Archivum Immunologiae et Therapiae Experimentalis
|
2018
|
tom 66
|
nr 1
8
Content available remote

Gastrin promotes intestinal polyposis through cholecystokinin-B receptor-mediated proliferative signaling and fostering tumor microenvironment

67%
Han Y.-M., Park J.-M., Park S.-H., Hahm K. B., Hong S. P., Kim E.-H.
Journal of Physiology and Pharmacology
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2013
|
tom 64
|
nr 4
9

Changes in the activity of acetylcholinesterase and Na, K-ATPase in human erythrocytes irradiated with X-rays

67%
Krokosz A., Szweda-Lewandowska Z.
Cellular and Molecular Biology Letters
|
2005
|
tom 10
|
nr 3
10

Decreased protein nitration in macrophages that overexpress indoleamine 2,3-dioxygenase

67%
Keskin D. B., Marshall B., Munn D., Mellor A. L., Gearhart D. A.
Cellular and Molecular Biology Letters
|
2007
|
tom 12
|
nr 1
The activity of indoleamine 2, 3-dioxygenase (IDO; E.C. 1.13.11.42) catalyzes the oxidative cleavage of tryptophan to form kynurenine. IDO activity consumes superoxide anions; therefore, we postulated that over-expression of IDO might mitigate superoxide-anion dependent, oxidative modification of cellular proteins in vitro. We prepared and characterized RAW 264.7 macrophages that were stably transfected with either an IDO expression vector or the control (empty) vector. We detected IDO mRNA, protein, and enzyme activity in the IDO-transfected macrophages, but not in the macrophages transfected with the empty vector. To generate superoxide anions in situ, we treated the IDO-and control-transfected cultures with xanthine or hypoxanthine, and then used ELISA methods to quantitate the relative levels of oxidatively modified proteins in total cell lysates. The levels of protein carbonyls were similar in IDO-transfected and vector-transfected macrophages; however, protein nitration was significantly less in IDO-transfected cells compared to control transfectants. In addition, steady-state levels of superoxide anions were significantly lower in the IDO-transfected cultures compared with control transfectants. Our results are consistent with the concept that, besides degrading tryptophan, IDO activity may protect cells from oxidative damage.
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