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Changes in yeast surface hydrophobicity and zeta-potential with yeast cell age were correlated with differences in adhesion.
Atomic force microscopy images demonstrated changes in yeast cell morphology by exposure to these contaminants in the dye Pb II) binary system grown in a bioaccumulation medium.
Measured responses were change in yeast protein ranging from 1.13 to 1.91 mg/mL, change in cell concentration ranging from 2.30 to 3.90 mg/mL and specific growth rate ranging from 0.21 0.51.100% hydrolysis and initial pH of 5.0 gave the highest changes in yeast protein (1.92 mg/mL) and cell concentration (3.90 mg/mL); 100% hydrolysis and pH 5.5 gave the highest specific growth rate.
For the first step in this strategy, we profiled protein abundance changes in yeast cells treated with rapamycin, a highly specific inhibitor of Tor1/2 [19], [19].
The genome-wide impact of the accumulation of DNA repair intermediates was compared to our previous results of gene expression changes in yeast upon exposure to an alkylating agent, namely methyl methanesulfonate (MMS) [1].
The levels of transcript variation were close to those reported in studies on DNA repair gene changes in yeast and Arabidopsis mutants [57], [75], but higher than those in human cells, whose levels change around 1.2 to 1.5-fold [59].
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For example, the mRNA abundance changes in yeasts occur in a time window of 20 to 240 min after rapamycin treatment, while the protein abundance changes mostly occur at 4 and 6 h of the treatment [ 44].
Taken together, these data indicate that in general genes are similarly important for buffering environmental and genetic change in yeast.
Providing a separate water source had no effect on the change in lifespan associated with a change in yeast:sugar.
Using this technique we identified 153 genes differentially expressed (DE) with at least a 1.8-fold change in yeast cells in response to yeast 24 h after interaction with P. digitatum (antagonist-pathogen: Mf-Pdig).
This hypothesis was confirmed both by EM and FRET studies, which showed that WASP triggers a conformational change in yeast or human Arp2/3 complex, shifting it from an "open" (inactive) state to a "closed" (primed for nucleation) state (Goley et al. 2004; Rodal et al. 2005b).
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