Transition-Metal-Free Cross-Coupling of Aryl Halides with Arylstannanes

Transition-metal-free LiCl-promoted cross-coupling reactions of tetraphenyltin, trichlorophenyl-, dichlorodiphenyl-, and chlorotriphenyl­stannanes with aryl halides in DMF provided access to biaryls in good to high yields. Up to four phenyl groups were transferred from the organostannanes substrates. The aryls bearing electron-withdrawing groups in either halides or organotin substrates gave coupling products in higher yields. The methodology has been applied for the efficient synthesis of ipriflavones

Additional file 1 of Development and application of emotion recognition technology — a systematic literature review

Supplementary Material

Garcinol from <i>Garcinia indica</i> Downregulates Cancer Stem-like Cell Biomarker ALDH1A1 in Nonsmall Cell Lung Cancer A549 Cells through DDIT3 Activation

Nonsmall cell lung cancer (NSCLC) is the predominant type of lung cancer. Patients with NSCLC show high mortality rates because of failure to clean up cancer stem cells (CSCs). The anticancer activity of phytochemical garcinol has been identified in various cancer cell models. However, the effect of garcinol on NSCLC cell lines is still lacking. Of the NSCLC cell lines we tested, A549 cells were the most sensitive to garcinol. Interestingly, Aldehyde Dehydrogenase 1 Family Member A1 (ALDH1A1) was preferentially expressed in A549 cells and downregulated by the addition of garcinol. We also found that garcinol enriched DNA damage-inducible transcript 3 (DDIT3) and then altered DDIT3-CCAAT-enhancer-binding proteins beta (C/EBPβ) interaction resulting in a decreased binding of C/EBPβ to the endogenous ALDH1A1 promoter. Furthermore, garcinol’s inhibition of ALDH1A1 was identified in a xenograft mice model. Garcinol repressed ALDH1A1 transcription in A549 cells through alterations in the interaction between DDIT3 and C/EBPβ. Garcinol could be a potential dietary phytochemical candidate for NSCLCs patients whose tumors harbored high ALDH1A1 expression

Polyglutamine Tract Expansion Increases S-Nitrosylation of Huntingtin and Ataxin-1

<div><p>Expansion of the polyglutamine (polyQ) tract in the huntingtin (Htt) protein causes Huntington’s disease (HD), a fatal inherited movement disorder linked to neurodegeneration in the striatum and cortex. S-nitrosylation and S-acylation of cysteine residues regulate many functions of cytosolic proteins. We therefore used a resin-assisted capture approach to identify these modifications in Htt. In contrast to many proteins that have only a single S-nitrosylation or S-acylation site, we identified sites along much of the length of Htt. Moreover, analysis of cells expressing full-length Htt or a large N-terminal fragment of Htt shows that polyQ expansion strongly increases Htt S-nitrosylation. This effect appears to be general since it is also observed in Ataxin-1, which causes spinocerebellar ataxia type 1 (SCA1) when its polyQ tract is expanded. Overexpression of nitric oxide synthase increases the S-nitrosylation of normal Htt and the frequency of conspicuous juxtanuclear inclusions of Htt N-terminal fragments in transfected cells. Taken together with the evidence that S-nitrosylation of Htt is widespread and parallels polyQ expansion, these subcellular changes show that S-nitrosylation affects the biology of this protein <i>in vivo</i>.</p></div

Additional file 3: of Failure of remission induction by glucocorticoids alone or in combination with immunosuppressive agents in IgG4-related disease: a prospective study of 215 patients

Clinical features, treatments and outcomes of the patients with persistently active disease. (DOCX 70 kb

Full-length Htt and Htt fragments.

<p>(A) Wild-type (wt) full-length Htt. The vertical lines indicates all 70 Cys residues. The horizontal open boxes indicate HEAT repeat motif clusters (Tartari, M. <i>et al</i>., <i>Mol Biol Evol</i>. 2008). The horizontal grey bar labels caspase cleavage sites. Anti-Htt antibodies (MAB2166, MCA2050, and MAB2168) and their binding sites are labeled. (B) Htt N548 fragment (1–548 a.a.) and its posttranslational modifications. The inset is an enlargement of this region. Cysteine residue numbers are indicated. (C) Full-length (FL) Htt constructs for transient expression. (D) Htt N-terminal 1–548 a.a. fragments that approximate proteolytic products of full-length Htt. (E) Constructs for expressing Htt exon1 coding region (1–90 a.a.). (F) C-terminal construct (585–3144 a.a.).</p

Additional file 4: of Failure of remission induction by glucocorticoids alone or in combination with immunosuppressive agents in IgG4-related disease: a prospective study of 215 patients

Clinical features, treatments and outcomes of the patients who relapsed during GC tapering. (DOCX 130 kb

The C214S mutation reduces Htt S-nitrosylation and S-acylation in the context of the normal polyQ tract.

<p>(A) S-nitrosylation (SNO) and S-acylation (S-acyl) of Htt N548Q15, N548Q15-C214S, N548Q128, and N548Q128-C214S. Recombinant proteins were expressed in COS7 cells for one day. The stars indicate significant reduction due to the C214S mutation. C: C214; S: C214S. (B) Quantification of the ratio of Htt N548 S-nitrosylation to total N548 (n = 3). The inset enlarges the scale for N548Q15 and N548Q15-C214S. (C) Quantification of the ratio of Htt N548 S-acylation to the total N548 (n = 3). In (B) and (C), experiments for C214 mutants were performed in parallel with Cys wild-type shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0163359#pone.0163359.g002" target="_blank">Fig 2A</a>. <i>p</i>-values from t-test are indicated if <i>p</i><0.05. The error bar represents the SEM.</p

Aberrant SIRT6 expression contributes to melanoma growth: Role of the autophagy paradox and IGF-AKT signaling

<p>Melanoma is among the most life-threatening cancers. The pathogenesis of melanoma has not been fully elucidated. Recently, dysregulated macroautophagy/autophagy has been found to play a critical but inconsistent role in modulating melanoma growth at different stages, with the regulatory mechanism unclear. The histone deacetylase SIRT6 (sirtuin 6) is a known autophagy regulator, and its involvement in cancer development has been reported. Therefore, we sought to determine the role of SIRT6 in melanoma growth and detect its possible link with autophagy in the current study. We initially observed that the expression of SIRT6 decreased in primary melanoma but increased in metastatic melanoma compared with melanocytic nevus. Notably, the expression of SIRT6 was significantly correlated with the expression of autophagy biomarkers including MAP1LC3/LC3 and SQSTM1/p62. Furthermore, SIRT6 suppressed the growth of primary melanoma but promoted metastatic melanoma development in an autophagy-dependent way <i>in vitro</i>. Moreover, SIRT6 exerted its regulation on melanoma growth via the IGF-AKT signaling pathway, and the intervention of AKT could partly reverse the effects of SIRT6 on melanoma growth by regulating autophagy. At last, we determined the effects of SIRT6 on melanoma development <i>in vivo</i>. Taken together, our findings demonstrate that the bimodal expression of SIRT6 at different melanoma stages plays a critical role in regulating melanoma growth through an autophagy-dependent manner, which indicates the potential of SIRT6 to be a biomarker and a therapeutic target in melanoma.</p

Additional file 1: of Failure of remission induction by glucocorticoids alone or in combination with immunosuppressive agents in IgG4-related disease: a prospective study of 215 patients

Outcomes of remission induction in the patients diagnosed with definite, probable and possible IgG4-RD. (DOCX 71 kb