Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

Wyszukujesz frazę "Augustyn, Agata." wg kryterium: Autor


Wyświetlanie 1-2 z 2
Tytuł:
Irony behind diminutives: a cognitive linguistic analysis of popular technical terms
Autorzy:
Augustyn, Rafał
Gniecka, Agata
Powiązania:
https://bibliotekanauki.pl/articles/606347.pdf
Data publikacji:
2011
Wydawca:
Uniwersytet Marii Curie-Skłodowskiej. Wydawnictwo Uniwersytetu Marii Curie-Skłodowskiej
Tematy:
Conceptual Integration Theory
Current Discourse Space
Opis:
Based on a study of English popular technical terms the article claims that in order to properly account for the ironic use of diminutives, one has to assume a cognitive view of meaning. Following Fauconnier and Turner’s (2002) Conceptual Integration Theory and Langacker’s (2008) notion of Current Discourse Space, we suggest that the ironic meanings of the stemaffix combinations involving diminutives should be seen as instances of conceptual blending that are determined by the context in which such formations occur, including the speakerhearer interaction in the specific context of a given usage event within the current discourse space.
Źródło:
Lublin Studies in Modern Languages and Literature; 2011, 35; 31-49
0137-4699
Pojawia się w:
Lublin Studies in Modern Languages and Literature
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the regulatory RACK1A protein and Ggamma subunits of the signal transducing heterotrimeric G protein
Autorzy:
Olejnik, Kamil
Bucholc, Maria
Anielska-Mazur, Anna
Lipko, Agata
Kujawa, Martyna
Modzelan, Marta
Augustyn, Agnieszka
Kraszewska, Elzbieta
Powiązania:
https://bibliotekanauki.pl/articles/1039863.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein complexes
Nudix
AtNUDT7
Arabidopsis thaliana
heterotrimeric G protein
RACK1A
Opis:
Arabidopsis thaliana AtNUDT7 Nudix pyrophosphatase hydrolyzes NADH and ADP-ribose in vitro and is an important factor in the cellular response to diverse biotic and abiotic stresses. Several studies have shown that loss-of-function Atnudt7 mutant plants display many profound phenotypes. However the molecular mechanism of AtNUDT7 function remains elusive. To gain a better understanding of this hydrolase cellular role, proteins interacting with AtNUDT7 were identified. Using AtNUDT7 as a bait in an in vitro binding assay of proteins derived from cultured Arabidopsis cell extracts we identified the regulatory protein RACK1A as an AtNUDT7-interactor. RACK1A-AtNUDT7 interaction was confirmed in a yeast two-hybrid assay and in a pull-down assay and in Bimolecular Fluorescence Complementation (BiFC) analysis of the proteins transiently expressed in Arabidopsis protoplasts. However, no influence of RACK1A on AtNUDT7 hydrolase catalytic activity was observed. In vitro interaction between RACK1A and the AGG1 and AGG2 gamma subunits of the signal transducing heterotrimeric G protein was also detected and confirmed in BiFC assays. Moreover, association between AtNUDT7 and both AGG1 and AGG2 subunits was observed in Arabidopsis protoplasts, although binding of these proteins could not be detected in vitro. Based on the observed interactions we conclude that the AtNUDT7 Nudix hydrolase forms complexes in vitro and in vivo with regulatory proteins involved in signal transduction. Moreover, we provide the initial evidence that both signal transducing gamma subunits bind the regulatory RACK1A protein.
Źródło:
Acta Biochimica Polonica; 2011, 58, 4; 609-616
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

    Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies