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Wyszukujesz frazę "Hryniewicz, Waleria" wg kryterium: Autor


Wyświetlanie 1-2 z 2
Tytuł:
Antimicrobial resistance – a challenge for public health
Autorzy:
Hryniewicz, Waleria
Powiązania:
https://bibliotekanauki.pl/articles/2188040.pdf
Data publikacji:
2019-05-06
Wydawca:
Uniwersytet Jagielloński. Wydawnictwo Uniwersytetu Jagiellońskiego
Tematy:
antimicrobial resistance
call for actions to contain antibiotic resistance
rational antibiotic use
działania ograniczające oporność na antybiotyki
oporność na antybiotyki
racjonalne stosowanie antybiotyków
Opis:
Penicillin, the first antibiotic introduced into clinical practice opened a new era in medicine. The ‘golden age’ of antibiotic discoveries in the 1950s, 60s and 70s significantly helped our fight against bacterial infections. In parallel with the introduction of new drugs, resistance strains were identified. This was, however, neglected because of the belief that pharmaceutical companies would continuously supply us with new products. In contrary, a pipeline of new antibiotics slowly dried out and in the 1980s we realized that the proportion of resistant bacteria was increasing faster than the supply of new antibiotics. New mechanisms of resistance emerged and multidrug and pandrug resistant bacterial strains started to spread globally. Antimicrobial resistance is recognized now as one of the greatest threats to public health worldwide. The WHO and EU as well as national agencies are calling for actions which should be immediately undertaken if we do not want to lose the battle.
Źródło:
Zdrowie Publiczne i Zarządzanie; 2019, 17, 1; 32-39
2084-2627
Pojawia się w:
Zdrowie Publiczne i Zarządzanie
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A novel member of the thermolysin family, cloning and biochemical characterization of metalloprotease from Staphylococcus pseudintermedius
Autorzy:
Wladyka, Benedykt
Bista, Michal
Sabat, Artur
Bonar, Emilia
Grzeszczuk, Sabina
Hryniewicz, Waleria
Dubin, Adam
Powiązania:
https://bibliotekanauki.pl/articles/1040710.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
staphylococcus
calcium
metalloprotease
pathogen
Opis:
Thermolysins constitute a family of secreted bacterial metalloproteases expressed, among others, by several pathogens. Strains of Staphylococcus pseudintermedius isolated from diseased dogs and judged as protease-positive, by skim milk agar plate culture, were investigated for protease content. No proteolytic activity was detected when the bacteria were grown in regular liquid media. Unexpectedly, supplementation of the medium with calcium ions resulted in expression of a metalloprotease and profound changes in the profile of extracellular proteins. On the basis of homology to other staphylococcal metalloproteases, the nucleotide sequence of the gene encoding this protease (Pst) and its flanking regions was determined. The full-length pst codes for a protein with an open reading frame of 505 amino acids. The internal region contains the HEXXH catalytic domain that is conserved in members of the thermolysin family. Regardless of the presence of calcium in the medium, the expression of the protease gene was of the same intensity. This suggests that regulation of the metalloprotease production by calcium ions is at a post-transcriptional level. Isolates of S. pseudintermedius exhibit a proteolytic phenotype due to the metalloprotease expression, however only in presence of calcium ions, which most probably stabilize the structure of the protease.
Źródło:
Acta Biochimica Polonica; 2008, 55, 3; 525-536
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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