Wyniki wyszukiwania - Biblioteka Nauki

1

An organism arises from every nucleus

100%

Keklikoglu N.

Folia Histochemica et Cytobiologica

|

2009

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tom 47

|

nr 2

179-183

2

Response of Acanthamoeba castellanii mitochondria to oxidative stress

100%

Trocha L. K. , Stobienia O.

Acta Biochimica Polonica

|

2007

|

tom 54

|

nr 4

797-803

EN

The purpose of this study was to examine the effects of oxidative stress caused by hydroperoxide (H2O2) in the presence of iron ions (Fe2+) on mitochondria of the amoeba Acanthamoeba castellanii. We used isolated mitochondria of A. Castellanii and exposed them to four levels of H2O2 concentration: 0.5, 5, 15, and 25 mM. We measured basic energetics of mitochondria: oxygen consumption in phosphorylation state (state 3) and resting state (state 4), respiratory coefficient rates (RC), ADP/O ratios, membrane potential (ΔΨm), ability to accumulate Ca2+ , and cytochrome crelease. Our results show that the increasing concentrations of H2O2 stimulates respiration in states 3 and 4. The highest concentration of H2O2 caused a 3-fold increase in respiration in state 3 compared to the control. Respiratory coefficients and ADP/O ratios decreased with increasing stress conditions. Membrane potential significantly collapsed with increasing hydroperoxide concentration. The ability to accumulate Ca2+ also decreased with the increasing stress treatment. The lowest stress treatment (0.5 mM H2O2) significantly decreased oxygen consumption in state 3 and 4, RC, and membrane potential. The ADP/O ratio decreased significantly under 5 mM H2O2 treatment, while Ca2+ accumulation rate decreased significantly at 15 mM H2O2. We also observed cytochrome crelease under increasing stress conditions. However, this release was not linear. These results indicate that as low as 0.5 mM H2O2 with Fe2+ damage the basic energetics of mitochondria of the unicellular eukaryotic organism Acanthamoeba castellanii

3

Electron paramagnetic resonance spectroscopy [EPR] as a method for studying the biology of the acellular slime moulds [Myxomycetes]

100%

Plonka P. M. , Rakoczy L.

Acta Physiologiae Plantarum

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1997

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tom 19

|

nr 2

4

Heavy metal biosorption from aqueous solution by simple eukaryotic organisms

100%

Zielinski R. , Kubinski K. , Stefaniak E. , Szyszka R.

Folia Histochemica et Cytobiologica. Supplement

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2001

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tom 39

|

nr 1

5

MiR396 involvement in regulation of somatic embryogenesis in Arabidopsis

84%

Szczygiel-Sommer A. , Gaj M. D.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

|

nr 3

6

Role of autophagy in mammary gland development

84%

Gajewska M. , Sobolewska A. , Kozlowski M. , Motyl T.

Journal of Physiology and Pharmacology. Supplement

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2008

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tom 59

|

nr 9

237-249

7

Developmental biology of Arabidopsis thaliana At1g67580 mutant

84%

Kuta E. , Malec P. , Pilarska M. , Slomka A. , Rataj K. , Ilnicki T.

Acta Biologica Cracoviensia. Series Botanica. Supplement

|

2008

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tom 50

|

nr 1

8

New strains of filamentous fungi isolated from construction materials

84%

Kobialka N. , Mularczyk M. , Kosiorowska K. , Pilarska K. M. , Laba W. , Piegza M. , Robak M.

Electronic Journal of Polish Agricultural Universities. Series: Biotechnology

|

2019

|

tom 22

|

nr 1

9

Animal Dicer and plant Dicer-like proteins

84%

Tworak A. , Urbanowicz A. , Podkowinski J. , Figlerowicz M.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

|

2013

|

tom 94

|

nr 1

10

Response of Amoeba proteus to microinjection with active Rac1 and RhoA proteins

84%

Pawlowska M. , Pomorski P. , Klopocka W. , Redowicz M. J.

Acta Protozoologica

|

2003

|

tom 42

|

nr 3

11

MADS-box genes are involved in floral development and evolution

84%

Saedler H. , Becker A. , Winter K. U. , Kirchner C. , Theissen G.

Acta Biochimica Polonica

|

2001

|

tom 48

|

nr 2

EN

MADS-box genes encode transcription factors in all eukaryotic organisms thus far studied. Plant MADS-box proteins contain a DNA-binding (M), an intervening (I), a Keratin-like (K) and a C-terminal C-domain, thus plant MADS-box proteins are of the MIKC type. In higher plants most of the well-characterized genes are involved in floral development. They control the transition from vegetative to generative growth and determine inflorescence meristem identity. They specify floral organ identity as outlined in the ABC model of floral development. Moreover, in Antirrhinum majus the MADS-box gene products DEF/GLO and PLE control cell proliferation in the developing flower bud. In this species the DEF/GLO and the SQUA proteins form a ternary complex which determines the overall "Bauplan" of the flower. Phylogenetic reconstructions of MADS-box sequences obtained from ferns, gymno- sperms and higher eudicots reveal that, although ferns possess already MIKC type genes, these are not orthologous to the well characterized MADS-box genes from gym- nosperms or angiosperms. Putative orthologs of floral homeotic B- and C-function genes have been identified in different gymnosperms suggesting that these genes evolved some 300-400 million years ago. Both gymnosperms and angiosperms also contain a hitherto unknown sister clade of the B-genes, which we termed Bsister. A novel hypothesis will be described suggesting that B and Bsister might be involved in sex determination of male and female reproductive organs, respectively.

12

Purification and characterization of GlcNAc-6-P 2-epimerase from Escherichia coli K92

84%

Ferrero M. A. , Martinez-Blanco H. , Lopez-Velasco F. F. , Ezquerro-Saenz C. , Navasa N. , Rodriguez-Aparicio L. B.

Acta Biochimica Polonica

|

2007

|

tom 54

|

nr 2

EN

N-Acetylmannosamine (ManNAc) is the first committed intermediate in sialic acid metabolism. Thus, the mechanisms that control intracellular ManNAc levels are important regulators of sialic acid production. In prokaryotic organisms, UDP-N-acetylglucosamine (GlcNAc) 2-epimerase and GlcNAc-6-P 2-epimerase are two enzymes capable of generating ManNAc from UDP-GlcNAc and GlcNAc-6-P, respectively. We have purified for the first time native GlcNAc-6-P 2-epimerase from bacterial source to apparent homogeneity (1 200 fold) using Butyl-agarose, DEAE-FPLC and Mannose-6-P-agarose chromatography. By SDS/PAGE the pure enzyme showed a molecular mass of 38.4 ± 0.2 kDa. The maximum activity was achieved at pH 7.8 and 37oC. Under these conditions, the Km calculated for GlcNAc-6-P was 1.5 mM. The 2-epimerase activity was activated by Na++ and inhibited by mannose-6-P but not mannose-1-P. Genetic analysis revealed high homology with bacterial isomerases. GlcNAc-6-P 2-epimerase from E. coli K92 is a ManNAc-inducible protein and is detected from the early logarithmic phase of growth. Our results indicate that, unlike UDP-GlcNAc 2-epimerase, which promotes the biosynthesis of sialic acid, GlcNAc-6-P 2-epimerase plays a catabolic role. When E. coli grows using ManNAc as a carbon source, this enzyme converts the intracellular ManNAc-6-P generated into GlcNAc-6-P, diverting the metabolic flux of ManNAc to GlcNAc.

13

Cloning and preliminary characterization of a GATC-specific beta2-class DNA:m6A methyltransferase encoded by transposon Tn1549 from Enterococcus spp.

84%

Radlinska M. , Piekarowicz A. , Galimand M. , Bujnicki J. M.

Polish Journal of Microbiology

|

2005

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tom 54

|

nr 3

EN

A recent study revealed a subfamily of N6-adenine (m⁶A) methyltransferases that comprises a few functionally studied eukaryotic members acting on mRNA and prokaryotic members acting on DNA as well as numerous uncharacterized open reading frames. Here, we report cloning and functional characterization of a prokaryotic member of this family encoded by transposon Tn1549 from Enterococcus spp.

14

The nucleotide sequence and organization of nuclear 5S rRNA genes in yellow lupine

84%

Nuc K. , Nuc P. , Pawelkiewicz J.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

1993

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tom 41

|

nr 2

15

Yeast: a eucaryotic model to study the genetic regulation of purine metabolism

84%

Lecoq K. , Daignan-Fornier B.

Cellular and Molecular Biology Letters

|

1999

|

tom 04

|

nr 3

16

First record of slime molds in Biebrza National Park (NE Poland)

67%

Slusarczyk D. M.

Acta Mycologica

|

2021

|

tom 56

|

nr 1

17

Tissue-specific expression of 14-3-3 isoforms during barley microspore and zygotic embryogenesis

67%

De F. M. S. , Louwerse J. D. , Lamers G. E. M. , Spaink H. P. , Wang M.

Acta Biologica Cracoviensia. Series Botanica

|

2003

|

tom 45

|

nr 1

EN

Conserved 14-3-3 proteins have been shown to play regulatory roles in eukaryotic cells, including cell cycle control and differentiation. We were interested in the possible involvement of 14-3-3 proteins in the embryogenic process of barley (Hordeum vulgare L.). Barley microspore-derived embryo development was used as a model system. Immunolocalization of three barley 14-3-3 isoforms, 14-3-3A, 14-3-3B and 14-3-3C, was carried out using isoform-specific antibodies. In immature microspore-derived embryos, 14-3-3C was specifically expressed underneath the L1 layer of the shoot apical meristem and in the scutellum. Comparative studies showed that 14-3-3C was also expressed underneath the L1 layer of the shoot apical meristem and in the scutellum of immature zygotic embryos. We further demonstrated that 14-3-3C expression is restricted to L2 layer-derived cells of in vitro shoot meristematic cultures. Our results reveal that 14-3-3C isoform tissue-specific expression is closely related to defined events during differentiation processes in embryogenesis and in vitro meristematic cultures.

18

DNA methyltransferases of Neisseria gonorrhoeae

67%

Piekarowicz A.

Acta Microbiologica Polonica

|

1994

|

tom 43

|

nr 3-4

19

Qualitative analysis of stress proteins induced by cadmium in the blue mussel Mytilus trossulus

67%

Radlowska M. , Pempkowiak J.

Oceanological Studies

|

1996

|

tom 25

|

nr 3

20

DNA methyltransferases of Neisseria gonorrhoeae

67%

Piekarowicz A. , Radlinska M. , Wiernicka-Gnas M.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

1996

|

tom 44

|

nr 3-4