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To determine whether LRRK2 broadly interacts with members of the dynamin superfamily, we compared the interaction of LRRK2 with the classical dynamins, Dnm1, Dnm2 and Dnm3, by co-IP in HEK-293T cells expressing FLAG-tagged LRRK2 and full-length HA-tagged Dnm1-3.
Recently, van Bemmel et al. [44] have compared the interaction of zebularine-containing DNA with bacterial M.Hha I and mammalian DNMT1 to 5-aza-CR-containing DNA.
In this study we compared the interaction of Wild Type, Arctic, Italian, Iowa, and Flemish Aβ (1 40) peptides with supported TBLE lipid bilayers with a focus on aggregate morphology and bilayer disruption.
To further assess the role of the increased Cdk5 activity, we compared the interaction of Cdk5 with the NFs in WT and mutant HSPB1 cells.
To test this possibility, we compared the interaction of ScCdc7 and myc-tagged HsCdc7 with ScDbf4 fused to a tandem affinity purification (TAP) tag (Rigaut et al. 1999).
First, we compared the interaction of integrin liposomes and non-functionalized ("pure") liposomes with SiO2 coated sensors.[ 21, 23, 26] Directly after injection, both the pure liposomes and the integrin liposomes showed a strong binding to the SiO2 sensors as indicated by the respective decrease in frequency and increase in dissipation (see Figure 1 a).
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A report [55] compared the interactions of two types of SWNT (1) iron-rich (non-purified) SWCNT (26% of iron) and (2) iron-stripped (purified) SWNT (0.23 wt% of iron) with RAW264.7 macrophages.
We compared the interactions of local anesthetic stereoisomers with biomimetic membranes consisting of chiral lipid components, the differences of which might be indicative of the drug design for reducing cardiotoxicity.
In the first place, we compared the interactions of SM, DPPE and SLPE with Ch at 25°C.
To first validate T2C in comparison to 3C and 4C-seq we compared the interactions of a single restriction fragment (CTCF AD viewpoint) [ 33] to interactions detected for this fragment by 3C [ 33] and 4C-seq [ 14].
We also compared the interactions of the binding sites of an important regulatory transcription factor in mouse primary erythroid cells, the Ldb1 complex, and the insulator binding protein Ctcf.
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