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Previously undertaken mutagenesis studies in yeast [70], [71] identified up to eight residues in eEF1A clustered within domains II and III, which (i) reduce actin disorganization induced by overexpression of eEF1A in yeast, (ii) inhibit actin-bundling without altering translation in vivo, and/or (iii) reduce actin-bundling.
We used (i) thirteen different datasets coming from two organisms (human and yeast), (ii) 110 independent rounds per experiment, and (iii) three kinds of indices to assess nine different algorithms.
The assumed degradation factors during AD are: (i) 90% for soluble sugars, organic acids, ethanol, glycerol, enzyme and yeast; (ii) 50% for polysaccharides, extractives, degradation products and water-soluble lignin; and (iii) 0% for water-insoluble lignin.
These include: (i) anti- Saccharomyces cerevesiae antibodies (ASCA) directed against a cell wall polysaccharide of the yeast; (ii) antineutrophil cytoplasmic antibodies (pANCA); (iii) anti-I2 (associated with anti- Pseudomonas activity) particularly in Crohn's disease (CD); (iv) anti- Eschericia coli outer membrane porin C (anti-OmpC) and (v) anti-flagellin (anti-CBir1) antibodies.
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In this work, we aimed to (i) study the phenotypic diversity of a small subset of commercial wine yeasts; (ii) assess their nitrogen requirements for growth and fermentation; and (iii) analyze their growth kinetics and metabolic traits.
Bacteriomatch bacterial-II-hybrid and Cytotrap yeast-II-hybrid (Agilent) techniques were used to identify partner proteins of BCA2.
Previous binding partners of BCA2 included Rab7, isolated through yeast-II-hybrid screening [ 17], tetherin, which was found though brute-force GST-pulldowns [ 18], and ubiquitin and UBC9 from bacteria-II- hybrid screening [ 7, 16].
Bait vector for yeast-II-hybrid screening was created by cutting the BCA2 construct from BCA2-containing pCMV-Tag-2B [ 7] with BamHI and SalI and ligating into the pSOS vector.
The local amino acid sequence has been compared with similar regions in yeast topoisomerase II and human topoisomerase IIα.
Until now, this helix was only observed when the Toprim domain is also present, whether DNA is complexed (in the structure of the S. pneumoniae topoisomerase IV catalytic core in complex with DNA, 3FOF [26] and the yeast topoisomerase II catalytic core-DNA complex, 2RGR [29]) or not (in the two structures of the yeast topoisomerase II catalytic core, 1BJT [32] and 1BGW [31BGW
Yeast topoisomerase II was purified from S. cerevisiae strain BCY123 harbouring the topoisomerase II expression plasmid YEpTOP2GAL1 as previously described [ 34].
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