Wyniki wyszukiwania

1

Disappearing halophytes and saline habitats in changing environment of SW Slovakia

100%

Feher A.

Ecological Questions

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2011

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tom 14

As a result of changes in land use, the ecologists and botanists already give details only of degradation, ruderalisation and fragmentation of halophytic plant communities (Camphorosmetum annuae, Limonio-Artemisietum santonici etc.) and the decline of halophytes on those sites (missing grazing, ploughing away, hydro-amelioration etc.).

2

Induced embryogenesis via egg cell activation in cereals

51%

Barnabas B., Bakos F., Feher A., Jager K.

Acta Biologica Cracoviensia. Series Botanica. Supplement

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2005

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tom 47

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nr 1

3

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Antibiotic resistance of Escherichia coli isolated from a poultry slaughterhouse

45%

Gregova G., Kmetova M., Kmet V., Venglovsky J., Feher A.

Annals of Agricultural and Environmental Medicine

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2012

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tom 19

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nr 1

The aim of the study was to investigate the antibiotic resistant E. coli strains isolated from bioaerosols and surface swabs in a slaughterhouse as a possible source of poultry meat contamination. The highest air coliforms contamination was during shackling, killing and evisceration of poultry. The strains showed resistance to ampicillin (89%), ceftiofur (62%) and cefquinome (22%), while resistance to ampicillin with sulbactam was only 6%. Resistance to streptomycin and gentamicin was detected in 43% vs. 14% isolates; to tetracycline 33%; to chloramphenicol and florfenicol in 10% vs. 18% isolates; to cotrimoxazol in 35% isolates; to enrofloxacin in 43 % isolates. The higher MIC of ceftazidime (3.6 mg.l-1) and ceftriaxon (5.2 mg.l-1) revealed the presence of ESBLs in 43% of isolates. From 19 selected phenotypically ESBL positive strains, 16 consisted of CMY-2 genes, while CTX-M genes were not detected by PCR. Maldi tof analysis of selected E. coli showed a clear clonal relatedness of environmental strains from various withdrawals.

4

Arabidopsis NAP-related proteins (NRPs) are soluble nuclear proteins immobilized by heat

45%

Ayaydin F., Biro J., Domoki M., Ferenc G., Feher A.

Acta Physiologiae Plantarum

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2015

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tom 37

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nr 02

Nucleosome assembly protein-related proteins (NRPs) are multifunctional proteins having histone chaperone and phosphatase inhibitor properties. Although it is believed that these proteins are nuclear and bind the chromatin, they can be detected in the cytoplasmic but not in the nuclear protein fraction by immunoblotting analysis. It is shown here that under normal conditions, NRPs are nuclear but soluble and leak out of the nuclei during their purification. However, under elevated temperatures (above 42 C), NRPs display significantly reduced mobility and are retained in the nuclei during purification probably due to binding other immobile macromolecules in the nucleus. Our observations highlight the necessity to use different techniques in parallel to unambiguously determine the intracellular localization of proteins. As heat adapted (38 C, 2 h followed by 2 h recovery) and heat shocked (45 C, 1 h), Arabidopsis seedlings were found to have phenotypes similar to those observed in the NRP loss-offunction mutants nrp1-1 nrp2-1 (short, branching roots, increased bleomycin sensitivity), it was also investigated whether the immobilization of NRPs by heat results in disturbed NRP functions. The results indicated, however, that heat affected the investigated traits independent on the presence of NRPs.

Ograniczanie wyników

1 Acta Biologica Cracoviensia. Series Botanica. Supplement

1 Acta Physiologiae Plantarum

1 Annals of Agricultural and Environmental Medicine

1 Ecological Questions

4 Feher A.

1 Ayaydin F.

1 Bakos F.

1 Barnabas B.

1 Biro J.

1 Domoki M.

1 Ferenc G.

1 Gregova G.

1 Jager K.

1 Kmet V.

1 Kmetova M.

1 Venglovsky J.

1 2015

1 2012

1 2011

1 2005

Disappearing halophytes and saline habitats in changing environment of SW Slovakia

Induced embryogenesis via egg cell activation in cereals

Antibiotic resistance of Escherichia coli isolated from a poultry slaughterhouse

Arabidopsis NAP-related proteins (NRPs) are soluble nuclear proteins immobilized by heat