Open thoracotomy versus VATS versus RATS for segmentectomy: a systematic review & Bayesian network meta-analysis.

Background: Recent trials suggest that more conservative resections such as segmentectomy are non-inferior to more radical approaches. Most segmentectomy can be safely performed using video-assisted thoracoscopic surgery (VATS). The clinical benefits of robotic-assisted thoracoscopic surgery (RATS) remain unclear.

Influence of neuromuscular electrical stimulation on the conduction velocity measured using EMG signals provided by linear arrays of electrodes.

Neuromuscular electrical stimulation (NMES) can alter the functioning of muscles and even assist muscle rehabilitation. In this paper, we evaluate the effect of NMES on the conduction velocity (CV) of the brachial biceps' motor units. We used a linear array of electrodes to acquire electromyographic signals, as different subjects perform isometric voluntary contractions (IVCs), with and without prior NMES.

Oligomerisation and thermal stability of polyvalent integrin alpha5beta1 ligands.

Synthetic oligomeric integrin alpha5beta1 ligands, specifically immobilised to surfaces, facilitate increased fibroblast cell spreading compared with that associated with the monomer. These ligands consist of a N-terminal fibronectin domain pair, a spacer and a di-, tri- or tetrameric coiled coil. However, it is not yet clear what effect fusion of the fibronectin domains has on the predicted oligomerisation of the coiled coils.

IGFBP-3 and IGFBP-5 associate with the cell binding domain (CBD) of fibronectin.

We have used Surface Plasmon Resonance (SPR) - based biosensor technology to investigate the interaction of the six high affinity insulin-like growth factor binding proteins (IGFBP 1-6) with the cell binding domain (CBD) of fibronectin. Using a biotinylated derivative of the ninth and tenth TypeIII domains of FN ((9-10)FNIII), we show that IGFBP-3 and -5 bind to FN-CBD. We show that this binding is inhibited by IGF-I and that, for IGFBP-5, binding occurs through the C-terminal heparin binding domain of the protein.