Use of dialkyldithiocarbamato complexes of bismuth(III) for the preparation of nano- and microsized Bi2S3 particles and the X-ray crystal structures of [Bi{S2CN(CH3)(C6H13)}(3)] and [Bi{S2CN(CH3)(C6H13)}(3)(C12H8N2)]

A range of bismuth(III) dithiocarbamato complexes were prepared and characterized. The X-ray crystal structures of the compounds [Bi{S2CN(CH3)(C6H13)}3] (1) and [Bi{S2CN(CH3)- (C6H13)}3(C12H8N2)] (2) are reported. The preparation of Bi2S3 particulates using a wet chemical method and involving the thermalysis of Bi(III) dialkyldithiocarbamato complexes is described. The influence of several experimental parameters on the optical and morphological properties of the Bi2S3 powders was investigated. Nanosized Bi2S3 colloids were obtained having long-term stability and showing a blue shift on the optical band edge; the presence of particles exhibiting quantum size effects is discussed. Morphological welldefined Bi2S3 particles were obtained in which the fiber-type morphology is prevalent.FCT - POCTI/1999/CTM/ 3545

Quenching of Er(III) luminescence by ligand C-H vibrations: Implications for the use of erbium complexes in telecommunications

Copyright 2006 American Institute of Physics. This article may be downloaded for personal use only. Any other use requires prior permission of the author and the American Institute of Physics. This article appeared in Applied Physics Letters 89, 111115 (2006) and may be found at

Near IR luminescent rare earth 3,4,5,6-tetrafluoro-2-nitrophenoxide complexes: Synthesis, X-ray crystallography and spectroscopy

NOTICE: this is the author’s version of a work that was accepted for publication in Near IR luminescent rare earth 3,4,5,6-tetrafluoro-2-nitrophenoxide complexes: Synthesis, X-ray crystallography and spectroscopy. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Near IR luminescent rare earth 3,4,5,6-tetrafluoro-2-nitrophenoxide complexes: Synthesis, X-ray crystallography and spectroscopy, [VOL27, ISSUE5, (2008)] DOI: 10.1016/j.poly.2008.01.02

Catalytic and mechanistic studies into the epoxidation of styrenes using manganese complexes of structurally similar polyamine ligands

The synthesis and catalytic activity of manganese(ii) complexes of two polyamine ligands is reported which highlights how a small structural change in the ligand affects the overall catalytic behaviour.</p

Effects of upper-body, lower-body, or combined resistance training on the ratio of follistatin and myostatin in middle-aged men.

PURPOSE:Due to the mechanistic role of myostatin and follistatin in modulating muscle mass, shifts in the follistatin to myostatin ratio (F:M) may help explain changes in muscular size in response to resistance training (RT). The present study examined whether differential responses in follistatin and myostatin occur based on the amount of active musculature in a RT program in middle-aged men. METHODS:Forty middle-aged men (age = 46.5 ± 3.1 years) were randomly assigned to 1 of 4 groups, upper-body RT (UB; n = 10), lower-body RT (LB; n = 10), combined RT (UB + LB; n = 10) or control (C; n = 10). The training protocol consisted of three exercise sessions per week for 8 weeks. Blood samples were obtained at baseline and 48 h after the final session of the training program. RESULTS:Muscle mass significantly increased (p < 0.05) following UB = 0.76 ± 0.46 kg, LB = 0.90 ± 0.29 kg, UB + LB = 1.38 ± 0.70 kg, compared to no changes after control. Serum follistatin increased in the LB = 0.24 ± 0.06 ng mL-1, UB = 0.27 ± 0.17 ng mL-1, UB + LB = 0.50 ± 0.18 ng mL-1, while serum myostatin decreased in the LB = - 0.11 ± 0.08 ng mL-1 and UB + LB = - 0.34 ± 0.23 ng mL-1, but not UB = 0.07 ± 0.16 ng mL-1. Further, change in concentration following training was larger between UB + LB and either LB or UB alone for both follistatin and myostatin. CONCLUSIONS:Both UB and LB increase muscle mass and alter the F: M ratio; however, the change in these endocrine markers is approximately twice as large if UB and LB is combined. The endocrine response to RT of myostatin and follistatin may depend on the volume of muscle mass activated during training

Telomere elongation in the breast cancer cell line 21NT after treatment with an epigenetic modifying drug

Background: Telomere length dysregulation plays a major role in cancer development and aging. Telomeres are maintained by a group of specialized genes known as shelterin and shelterin-associated proteins. In breast cancer lines it has been shown that shelterin proteins are dysregulated thereby affecting the telomere stability and contributing to the neoplastic conversion of the mammary epithelial cells. Interestingly, the regulation of some of the shelterin genes is thought to be controlled epigenetically. Methods and Results: In this study, we set out to measure the effect of increased shelterin gene expression on telomere length in breast cancer cell line 21NT treated with 5-aza-2-deoxycytidine (5-aza-CdR) using known telomere length assays. We measured telomere lengths using: Telomere Restriction Fragment length (TRF), absolute quantitative-PCR and cytogenetic Interphase Quantitative Fluorescent in situ Hybridization (iQ-FISH). We found that non-cytotoxic levels of 5-aza-CdR affect telomere lengths by causing a significant and stable increase in telomere lengths of the breast cancer cell line. The increase in telomere lengths was consistently observed when various telomere length methods were used. Conclusions: Further investigation is required to understand the underlying mechanism involved, and the significance of telomere length elongation in relation to clinical outcome when epigenetic modifying drugs are utilized.We thank Professor Robert Newbold for his support and for providing the opportunity to carry out this work within the Institute of Cancer Genetics and Pharmacogenomics, Brunel University London. HY was supported by a triennial project grant (Strategic Award) from the National Centre for Replacement, Refinement, and Reduction (NC3Rs) of animals in research (NC. K500045.1 and G0800697)