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Biophysical and biochemical studies presented here indicate that a substantial number of GPCRs may directly bind and activate a major actin cross-linking protein, Filamin A (FLNa), and that the binding triggers filamin phosphorylation by cellular protein kinases.
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The studies presented here focus upon PrP N-terminal sequences.
The study presented here sets the stage for detailed biochemical interrogation of this complicated assembly process, and ongoing studies in our lab are directed at dissecting the thermodynamic parameters describing these essential steps in virus development.
The study presented here has some limitations.
The study presented here has several limitations.
The ethnographic study presented here, however, does exactly that.
The study presented here contains a number of novel findings.
The study presented here addresses two main questions.
The study presented here was approved by the IACUC of Orthopaedic Hospital.
A combination of data from in vitro biochemical analysis and NMR studies is presented here to reveal the function mechanism of SNF in regulating Sxl splicing.
The crystal structure of rCtFtn and the biochemical results presented here, suggests that rCtFtn presents similar biochemical properties reported for other members of this protein family albeit with distinct structural plasticity.
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CEO of Professional Science Editing for Scientists @ prosciediting.com