943 resultados para Konrad IV, King of the Romans, 1228-1254.


Relevância:

100.00% 100.00%

Publicador:

Resumo:

Edited by Raffaele Salari.

Relevância:

100.00% 100.00%

Publicador:

Resumo:

Mode of access: Internet.

Relevância:

100.00% 100.00%

Publicador:

Resumo:

Concerning the politics of the day.

Relevância:

100.00% 100.00%

Publicador:

Resumo:

The electromyographic activity of the shoulder muscles deltoid - anterior portion (DA) and pectoralis major - clavicular portion (PMC) was tested on 24 male volunteers using a 2 channel TEC A TE4 electromyograph and Hewlett Packard surface electrodes during the execution of four different modalities of frontal-lateral cross, dumbbells exercises. The results showed that all of the tested exercises developed high levels of action potential for both muscles. So, we jusfity the indication of all of them for physical fitness programmes for DA and PMC. Some suggestions to the use of the tested exercises are presented.

Relevância:

100.00% 100.00%

Publicador:

Resumo:

Upon sensing of peptide pheromone, Enterococcus faecalis efficiently transfers plasmid pCF10 through a type IV secretion (T4S) system to recipient cells. The PcfF accessory factor and PcfG relaxase initiate transfer by catalyzing strand-specific nicking at the pCF10 origin of transfer sequence (oriT). Here, we present evidence that PcfF and PcfG spatially coordinate docking of the pCF10 transfer intermediate with PcfC, a membrane-bound putative ATPase related to the coupling proteins of gram-negative T4S machines. PcfC and PcfG fractionated with the membrane and PcfF with the cytoplasm, yet all three proteins formed several punctate foci at the peripheries of pheromone-induced cells as monitored by immunofluorescence microscopy. A PcfC Walker A nucleoside triphosphate (NTP) binding site mutant (K156T) fractionated with the E. faecalis membrane and also formed foci, whereas PcfC deleted of its N-terminal putative transmembrane domain (PcfCDelta N103) distributed uniformly throughout the cytoplasm. Native PcfC and mutant proteins PcfCK156T and PcfCDelta N103 bound pCF10 but not pcfG or Delta oriT mutant plasmids as shown by transfer DNA immunoprecipitation, indicating that PcfC binds only the processed form of pCF10 in vivo. Finally, purified PcfCDelta N103 bound DNA substrates and interacted with purified PcfF and PcfG in vitro. Our findings support a model in which (i) PcfF recruits PcfG to oriT to catalyze T-strand nicking, (ii) PcfF and PcfG spatially position the relaxosome at the cell membrane to stimulate substrate docking with PcfC, and (iii) PcfC initiates substrate transfer through the pCF10 T4S channel by an NTP-dependent mechanism.

Relevância:

100.00% 100.00%

Publicador:

Resumo:

Signatur des Originals: S 36/F03237