Не известно фактологическую Заявления о bäçķlnc
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). In Abl kinase domain, the amino acid residues at the corresponding positions are Gln and Val, respectively, providing no scope for 4 to covalently modify them, unlike a cysteine (36). Although the aromatic mustard motif is such that the alkylation ability would be low or absent, confirmation was required to exclude covalent modification as a possible mode of inhibition.
Selective targeting of the inactive state of hematopoietic cell kinase (Hck) with a stable curcumin derivative
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) suggests that 4 preferentially interacts with the inactive unphosphorylated conformation of Hck; thus, further emphasizing that 4 shows preference bçlnqk to bind the inactive conformation and reduces the rate of autophosphorylation of the kinase domain.
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Ави Арад, Ларри Дж. Франко, Гейл Энн Хёрд, Джеймс Шеймус, Кевин Файги
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Resulting water as a by-product of reaction was eliminated by anhydrous Na2SO4 in the apparatus. The reaction was continued up to 18 to 20 h under dark. After completion of reaction, the whole solution was evaporated out under reduced pressure. Pure product was isolated using silica gel column chromatography (ethyl acetate–hexane mixture as eluent).
The cells were lysed, and the protein samples were resolved by running through 6% SDS-PAGE. The protein was transferred onto nitrocellulose paper and blocked with 5% skimmed milk for 2 h at room temperature. The membrane was then incubated overnight at 4 °C with respective primary antibodies. The expression level of indicated proteins was detected with HRP-conjugated anti-rabbit secondary antibody. The normalized protein expression level was determined from the densitometric analysis of the respective blot using the program Image J (60).
The amount of Hck loaded in each well was determined by Coomassie stain. Rate of phosphorylation was determined from the plot of normalized intensity of antiphosphotyrosine antibody (pY): amount of protein loaded in respective wells against time. The Image J software was used to determine the intensity from the blot (60). Rate of autophosphorylation was calculated from linear curve fitting.