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1

cAMP-dependent protein kinase: structural basis for function, regulation, and subcellular localization

100%
Taylor S. S., Narayana N., Huang L., Banky P., Wang L., Cheng X.
Cellular and Molecular Biology Letters
|
1998
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tom 03
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nr 3
2

Subcellular localization of two different type-1 casein kinases from yeast

100%
Dukowski P., Szyszka R., Bednara J.
Acta Biochimica Polonica
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1993
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tom 40
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nr 3
Specific antibodies directed against the two yeast type-1 casein kinases (CK1) were used to study the localization of both 45 kDa and 27 kDa casein kinase species in yeast cells by immunofluorescence. Our results indicate that the larger and smaller CK1 species are localised in different compartments of the yeast cell. The 45 kDa enzyme is present in the cytoplasm of the cell both during the logarithmic and stationary growth phase. The 27 kDa CK1 was found in the nucleus in the cells in logarithmic growth phase while the enzyme from the stationary phase was present in the cytoplasm. Our results suggest that the 27 kDa casein kinase may play some role in yeast cell division control by displacement from the nucleus to the cytoplasm.
3

Inhibition of poly[ADP-ribose] polymerase activity affects its subcellular localization and DNA strand break rejoining

88%
Ryabokon N. I., Cieslar-Pobuda A., Rzeszowska-Wolny J.
Acta Biochimica Polonica
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2009
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tom 56
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nr 2
243-248
 Poly(ADP-ribose) polymerase (PARP) plays a crucial role in DNA repair. Modulation of its activity by stimulation or inhibition is considered as a potentially important strategy in clinical practice, especially to sensitize tumor cells to chemo- and radiotherapy through inhibition of DNA repair. Here we studied the effect of the three PARP inhibitors, 5-iodo-6-amino-benzopyrone (INH2BP), 1,5-isoquinolinediol (1,5-dihydroxyisoquinolinediol (1,5-IQD) and 8-hydroxy-2-methylquinazolin-4-[3H]one (NU1025), and for two of them the efficiency in slowing the rejoining of DNA strand breaks induced by H2O2 was compared. Inhibition of PARP changed its intranuclear localization markedly; cells exposed to the inhibitor NU1025 showed a significant tendency to accumulate PARP in large foci, whereas in untreated cells its distribution was more uniform. The speed and efficiency of rejoining of H2O2-induced DNA strand breaks were lower in cells incubated with a PARP inhibitor, and the kinetics of rejoining were modulated in a different manner by each inhibitor. At a concentration of 100 µM the efficiency of the inhibitors could be ranked in the order NU1025 > IQD > INH2BP. The two first compounds were able to decrease the overall PARP activity below the level detected in control cells, while INH2BP showed up to 40% PARP activity after exposure to H2O2.
4

Subcellular localization of UDP-GlcNAc, UDP-Gal and SLC35B4 transporters

75%
Maszczak-Seneczko D., Olczak T., Olczak M.
Acta Biochimica Polonica
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2011
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tom 58
|
nr 3
The mechanisms of transport and distribution of nucleotide sugars in the cell remain unclear. In an attempt to further characterize nucleotide sugar transporters (NSTs), we determined the subcellular localization of overexpressed epitope-tagged canine UDP-GlcNAc transporter, human UDP-Gal transporter splice variants (UGT1 and UGT2), and human SLC35B4 transporter splice variants (longer and shorter version) by indirect immunofluorescence using an experimental model of MDCK wild-type and MDCK-RCAr mutant cells. Our studies confirmed that the UDP-GlcNAc transporter was localized to the Golgi apparatus only and its localization was independent of the presence of endogenous UDP-Gal transporter. After overexpression of UGT1, the protein colocalized with the Golgi marker only. When UGT2 was overexpressed, the protein colocalized with the endoplasmic reticulum (ER) marker only. When UGT1 and UGT2 were overexpressed in parallel, UGT1 colocalized with the ER and Golgi markers and UGT2 with the ER marker only. This suggests that localization of the UDP-Gal transporter may depend on the presence of the partner splice variant. Our data suggest that proteins involved in nucleotide sugar transport may form heterodimeric complexes in the membrane, exhibiting different localization which depends on interacting protein partners. In contrast to previously published data, both splice variants of the SLC35B4 transporter were localized to the ER, independently of the presence of endogenous UDP-Gal transporter.
5
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Prediction of protein subcellular localization using support vector machine with the choice of proper kernel

75%
Hasan M. A. M., Ahmad S., Molla M. K. I.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2017
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tom 98
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nr 2
6

Studies of HIV-Rev in living cells

75%
Brokstad K. A., Andersen V., Kanestrom A., Szilvay A. M., Haukenes G., Kalland K. H.
Cellular and Molecular Biology Letters
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1997
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tom 02
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nr 2
7

BH3-only proteins: the lords of death

75%
Fleischer A., Rebollo A., Ayllon V.
Archivum Immunologiae et Therapiae Experimentalis
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2003
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tom 51
|
nr 1
8
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

ROSMETER: a bioinformatic tool for the identification of reactive oxygen species (ROS) transcriptomic imprints

63%
Rosenwasser S., Sela N., Fluhr R., Friedman H.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2013
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tom 94
|
nr 2
9
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Identification, phylogenetic analyses and subcellular localization of protein phosphatases 2c type (PP2Cs) in Populus trichocarpa

63%
Betlinski B., Vashutina K., Gawronski P., Karpinski S.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2013
|
tom 94
|
nr 2
10
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

The subcellular localization of UVR3 and two putative photolyases, PHR2 and At4g25290

63%
Aggarwal C., Labuz J., Sztatelman O., Banas A. K.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2013
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tom 94
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nr 3
11

Subcellular localization of full-length human myeloid leukemia factor 1 (MLF1) is independent of 14-3-3 proteins

63%
Molzan M., Ottmann C.
Cellular and Molecular Biology Letters
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2013
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tom 18
|
nr 1
Myeloid leukemia factor 1 (MLF1) is associated with the development of leukemic diseases such as acute myeloid leukemia (AML) and myelodysplastic syndrome (MDS). However, information on the physiological function of MLF1 is limited and mostly derived from studies identifying MLF1 interaction partners like CSN3, MLF1IP, MADM, Manp and the 14-3-3 proteins. The 14-3-3-binding site surrounding S34 is one of the only known functional features of the MLF1 sequence, along with one nuclear export sequence (NES) and two nuclear localization sequences (NLS). It was recently shown that the subcellular localization of mouse MLF1 is dependent on 14-3-3 proteins. Based on these findings, we investigated whether the subcellular localization of human MLF1 was also directly 14-3-3-dependent. Live cell imaging with GFP-fused human MLF1 was used to study the effects of mutations and deletions on its subcellular localization. Surprisingly, we found that the subcellular localization of full-length human MLF1 is 14-3-3-independent, and is probably regulated by other as-yet-unknown proteins.
12

The activity of enzymes of different subcellular localization in the wall of aortic aneurysm and parietal thrombus

51%
Gacko M., Worowska A., Glowinski S.
Bulletin of the Polish Academy of Sciences. Biological Sciences
|
2000
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tom 48
|
nr 3
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