A case of giant sebaceous carcinoma localized in the breast area of a male patient

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(1R,4R,5R)-1,3,4-Triphenyl-7-[(R)-1-phenyl­ethyl]-2-oxa-3,7-diaza­spiro­[4.5]decan-10-one

In the title compound, C33H32N2O2, the polysubstituted piperidine ring adopts a chair conformation. The isoxazolidine ring is in an envelope conformation. In the crystal structure, intra- and inter­molecular C—H⋯π inter­actions involving the phenyl rings are observed

The influence of nitric oxide donors on the responses to the nitrergic nerve stimulation in the mouse duodenum

WOS: 000208316200607

The east -west advancement flap (horizontal advancement flap) to repair a defect on the nose ala.

Background The repair of an alar nasal defect is a frequent challenge for dermatologic surgeons for reasons of the high rate of non-melanoma cancers in the area. Objective Our aim was to describe the use of an east\u2013west cheek-based flap (horizontal advancement flap) to repair a surgical defect on the nose ala. Methods Benefits and limits of this surgical procedure are evaluated. Result The resulting S-shaped scar was well-camouflaged among the natural skin lines (melolabial fold and melonasal junction). No architectural distortion of the nose resulted from the procedure. Conclusion In selected patients with small-to-medium-size defects of the nasal ala, the horizontal advancement flap is a simple, reliable and aesthetic reconstruction option

Movement of the s4 segment in the herg potassium channel during membrane depolarization

PubMedID: 19878047The hERG potassium channel is a member of the voltage gated potassium (Kv) channel family, comprising a pore domain and four voltage sensing domains (VSDs). Like other Kv channels, the VSD senses changes in membrane voltage and transmits the signal to gates located in the pore domain; the gates open at positive potentials (activation) and close at negative potentials, thereby controlling the ion flux. hERG, however, differs from other Kv channels in that it is activated slowly but inactivated rapidly - a property that is crucial for the role it plays in the repolarization of the cardiac action potential. Voltage-gating requires movement of gating charges across the membrane electric field, which is accomplished by the transmembrane movement of the fourth transmembrane segment, S4, of the VSD containing the positively charged arginine or lysine residues. Here we ask if the functional differences between hERG and other Kv channels could arise from differences in the transmembrane movement of S4. To address this, we have introduced single cysteine residues into the S4 region of the VSD, expressed the mutant channels in Xenopus oocytes and examined the effect of membrane impermeable parachloromercuribenzene sulphonate on function by the two-electrode voltage clamp technique. Our results show that depolarization results in the accessibility of seven consecutive S4 residues, including the first two charged residues, K525 and R528, to extracellularly applied reagent. These data indicate that the extent of S4 movement in hERG is similar to other Kv channels, including the archabacterial KvAP and the Shaker channel of Drosophila. © 2009 Informa UK Ltd.British Heart Foundation: PG/03/154/16411 Royal SocietyThis work was supported by a grant from the British Heart Foundation (PG/03/154/16411). NYD was a recipient of a visiting fellowship from the Royal Society and TUBITAK (The Scientific and Technical Research Council of Turkey)