However, other researches suggest that the motor cortex is not an integral part of the network for action-word representation but is recruited only to execute tasks that critically require the retrieval of sensorimotor attributes associated with words. In order to enlighten this controversial literature, three groups of healthy participants were submitted to transcranial direct current stimulation (tDCS) (cathodal, anodal and sham stimulations)

of the left primary motor cortex during the execution of a picture recognition task. Results show that cathodal stimulation improves the participants’ ability to detect either mismatching motor vs. no motor sentence-drawing associations, while no significant difference has not been reported for compatible associations. The current result is in line with the suggestion that motor regions play a critical selleck products role in detecting dissonant outcomes. (C) 2012 Elsevier Ireland Ltd. All rights reserved.”
“Loop 5 (L5) is a conserved loop that projects from the alpha 2-helix adjacent to the nucleotide site of all kinesin-family motors. L5 is critical to the function of the mitotic kinesin-5 family motors and is the binding site for several kinesin-5 inhibitors that are currently in clinical trials. Its conformational dynamics and its role in motor

function are not fully understood. Our previous work using EPR spectroscopy suggested that L5 alters the nucleotide pocket conformation of the kinesin-5 motor Eg5 (Larson et al., 2010). EPR spectra MG-132 of a spin-labeled

nucleotide analog bound at the nucleotide site of Eg5 display a highly immobilized component that is absent if L5 is shortened or if the inhibitor STLC is added (Larson et al., 2010), which X-ray structures suggest stabilizes an L5 conformation pointing away from the nucleotide site. These data, coupled with the proximity of L5 to the nucleotide site suggest L5 could interact with a bound nucleotide, modulating function. Here we use molecular dynamics (MD) simulations of Eg5 to explore the interaction of L5 with the nucleotide site in greater detail. We performed MD simulations in which the L5-domain of the Eg5 ADP X-ray structure was manually deformed via backbone bond rotations. The L5-domain of Eg5 was sufficiently lengthy that portions of L5 could be located in proximity to bound ADP. The MD check details simulations evolved to thermodynamically stable structures at 300 K showing that L5 can interact directly with bound nucleotide with significant impingement on the ribose hydroxyls, consistent with the EPR spectroscopy results. Taken together, these data provide support for the hypothesis that L5 modulates Eg5 function via interaction with the nucleotide-binding site. (C) 2011 Elsevier Ltd. All rights reserved.”
“Baculovirus mediated gene transduction of mammalian cells (BacMam) is an emerging technique for rapid recombinant protein expression in mammalian cells.