Quantification of cytotoxicity in mole concentration (µM).

<p>(a) Histogram, (b) dot plot, (c) box plot and (d) normal Q-Q plot of cytotoxicity data set expressed in µM. While histogram shows how cytotoxicity data spread out in certain concentration range, dot plot gives the global dispersion picture in full concentration range, and box plot brings the mean value as reference. Q-Q plot demonstrates that cytotoxicity in µM as the sample set used in the test, deviates significantly from the normal distribution.</p

Quantification of cytotoxicity in weight concentration (mg/mL).

<p>(a) Histogram, (b) dot plot, (c) box plot, and (d) normal Q-Q plot of cytotoxicity data set expressed in mg/mL. While the histogram, dot plot and box plot imply a narrow distribution of cytotoxicity in mg/mL, Q-Q plot also shows considerable deviation from normal distribution.</p

Illustration of the aggregates constrained in a fixed volume and are expressed in different units of concentration.

<p>(a) Mole concentration only represents the amounts of individual units in a certain volume. (b) Mass concentration is able to reflect the solid-like properties such as density, which indicates the interaction and accommodates inhomogeneous distribution of the aggregates.</p

Statistic data of two data sets in mole concentration and mass concentration.

<p>Statistic data of two data sets in mole concentration and mass concentration.</p

Flow chart of study identification, inclusion, exclusion.

<p>Flow chart of study identification, inclusion, exclusion.</p

Characterization and Functional Analysis of the Calmodulin-Binding Domain of Rac1 GTPase

<div><p>Rac1, a member of the Rho family of small GTPases, has been shown to promote formation of lamellipodia at the leading edge of motile cells and affect cell migration. We previously demonstrated that calmodulin can bind to a region in the C-terminal of Rac1 and that this interaction is important in the activation of platelet Rac1. Now, we have analyzed amino acid residue(s) in the Rac1-calmodulin binding domain that are essential for the interaction and assessed their functional contribution in Rac1 activation. The results demonstrated that region 151–164 in Rac1 is essential for calmodulin binding. Within the 151–164 region, positively-charged amino acids K153 and R163 were mutated to alanine to study impact on calmodulin binding. Mutant form of Rac1 (K153A) demonstrated significantly reduced binding to calmodulin while the double mutant K153A/R163A demonstrated complete lack of binding to calmodulin. Thrombin or EGF resulted in activation of Rac1 in CHRF-288-11 or HeLa cells respectively and W7 inhibited this activation. Immunoprecipitation studies demonstrated that higher amount of CaM was associated with Rac1 during EGF dependent activation. In cells expressing mutant forms of Rac1 (K153A or K153A/R163A), activation induced by EGF was significantly decreased in comparison to wild type or the R163A forms of Rac1. The lack of Rac1 activation in mutant forms was not due to an inability of GDP-GTP exchange or a change in subcelllular distribution. Moreover, Rac1 activation was decreased in cells where endogenous level of calmodulin was reduced using shRNA knockdown and increased in cells where calmodulin was overexpressed. Docking analysis and modeling demonstrated that K153 in Rac1 interacts with Q41 in calmodulin. These results suggest an important role for calmodulin in the activation of Rac1 and thus, in cytoskeleton reorganization and cell migration.</p> </div

Patients' demographic and clinical characteristics.

<p>RTA: Road Traffic Accidence.</p><p>PV: Personal Violence.</p><p>All 31 patients showed malocclusion, which was one indication for open reduction and internal fixation. Patients without malocclusion were excluded from this group.</p

Photographs show a 25-year-old male patient undergoing open reduction and rigid internal fixation of right condylar fracture under general anaesthesia.

<p>A: Design; B: Incision; C: Flap elevation and exposure of the SMAS fascia; D: Exposure of condylar fracture; E: Rigid internal fixation; F: Suture.</p

Self-Assembly of Nucleopeptides to Interact with DNAs

As a novel class of biomaterials, nucleopeptides, via the conjugation of nucleobases and peptides, usually self-assemble to form nanofibres driven mainly by hydrogen bonds. Containing nucleobase(s), nucleopeptides have a unique property—interacting with nucleic acids. Here we report the design and characterization of nucleopeptides that self-assemble in water and are able to interact with single stranded DNAs (ssDNAs). Containing nucleobases on their side chains, these nucleopeptides bind with the ssDNAs, and the ssDNAs reciprocally affect the self-assembly of nucleopeptides. In addition, the interactions between nucleopeptides and ssDNAs also decrease their proteolytic resistance against proteinase K, which further demonstrates the binding with ssDNAs. The designed nucleopeptides also interact with the plasmid DNA and deliver hairpin DNA into cells. This work illustrates a new and rational approach to create soft biomaterials by the integration of nucleobases and peptides for the binding with DNAs, which may lead to develop nucleopeptides for controlling DNA in cells

Effect of deletion of Rac1 putative CaM binding domain on interaction with purified bovine brain CaM.

<p>Equal amount (20 µg) of wild type (WT) GST-Rac1 and GST-Rac1 mutant (amino acids 151 to 164 deleted) were incubated with purified CaM (20 µg) in MOPS buffer and allowed to shake for 2 h at 4°C. GST beads were used as negative control. The incubation conditions were WT GST-Rac1 or GST-Rac1 mutant beads with buffer alone, buffer plus 5 mM Ca²⁺ or buffer plus 10 mM EGTA. At the end of the incubation, beads were washed three times and bound proteins were eluted using Laemmli's sample buffer. Western blot analysis was carried out using anti-CaM antibodies. A representative autoradiograph and quantitation is shown above. The experiment was repeated a minimum of three times.</p