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Nuñ,ez, Ana J.,Shear, Lindsey N.,Dahal, Naween,Ibarra, Ilich A.,Yoon, JiWoong,Hwang, Young Kyu,Chang, Jong-San,Humphrey, Simon M. Royal Society of Chemistry 2011 Chemical communications Vol.47 No.43
<P>PCM-10 is a porous phosphine coordination material based on Ca(<SMALL>II</SMALL>) and <I>tris</I>(<I>p</I>-carboxylated) triphenylphosphine. The material provides a unique 3-dimensional surface of P(<SMALL>III</SMALL>) Lewis base sites, which is ideal for post-synthetic functionalization. The addition of Au(<SMALL>I</SMALL>) yields an advanced material that can selectively adsorb 1-hexene over n-hexane at room temperature.</P> <P>Graphic Abstract</P><P>The 3-dimensional porous coordination polymer, PCM-10, is based on triphenylphosphine. The free phosphine sites within the polymer may be post-synthetically modified with catalytic species, such as AuCl. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c1cc14682c'> </P>
Cleto Alvarez-Aguilar,Maria Lucia Enrí,quez-Ramí,rez,Benigno Figueroa-Nuñ,ez,Anel Gó,mez-Garcí,a,Ernesto Rodrí,guez-Ayala,Cristina Morá,n-Moguel,Victor Manuel 생화학분자생물학회 2007 Experimental and molecular medicine Vol.39 No.3
Metabolic Syndrome (MS) is recognized as a cluster of cardiovascular risk factors. All components of MS have a genetic base. Genes of the renin angiotensin system are potential candidate genes for MS. We investigated whether angiotensin converting en-zyme (ACE) gene polymorphism increases suscep-tibility to MS as an entity in a Mexican population. In a cross-sectional study, 514 individuals were studied including 245 patients with MS and 269 subjects without MS criteria. ACE gene polymorphism was detected using PCR. MS was defined according to The National Cholesterol Education Program Expert Blood Cholesterol in Adults (Adult Treatment Panel III) criteria, except that the raised fasting plasma glucose ≥100 mg/dl criterion for identification of intolerance fasting glucose was modified in accordance with the suggestion of the American Diabetes Association. Patients with MS were sig - nificantly different from subjects without MS in relation to mean body mass index (BMI), waist circumference (WC), systolic blood pressure, diastolic blood pressure, glucose, total cholesterol (C), triglycerides, HDL-C, and LDL-C (P<0.0001). The differences in the mean BMI, WC, glucose, total cholesterol, triglycerides, LDL-C, and HDL-C were maintained in patients with the MS and DD genotypes (P<0.01). The DD genotype was strongly asso - ciated with MS (adjusted OR = 5.48, 95% CI 3.20-9.38, P<0.0001). We concluded that the DD genotype increases susceptibility to MS in a Mexican pop - ulation. These results indicate that pharmacological and non-pharmacological treatment and a reduction in body fat will have important therapeutic im - plications in this disease.
The ribonuclease activity of SAMHD1 is required for HIV-1 restriction
Ryoo, Jeongmin,Choi, Jongsu,Oh, Changhoon,Kim, Sungchul,Seo, Minji,Kim, Seok-Young,Seo, Daekwan,Kim, Jongkyu,White, Tommy E,Brandariz-Nuñ,ez, Alberto,Diaz-Griffero, Felipe,Yun, Cheol-Heui,Hollen Nature Publishing Group, a division of Macmillan P 2014 Nature medicine Vol.20 No.8
The HIV-1 restriction factor SAM domain– and HD domain–containing protein 1 (SAMHD1) is proposed to inhibit HIV-1 replication by depleting the intracellular dNTP pool. However, phosphorylation of SAMHD1 regulates its ability to restrict HIV-1 without decreasing cellular dNTP levels, which is not consistent with a role for SAMHD1 dNTPase activity in HIV-1 restriction. Here, we show that SAMHD1 possesses RNase activity and that the RNase but not the dNTPase function is essential for HIV-1 restriction. By enzymatically characterizing Aicardi-Goutières syndrome (AGS)-associated SAMHD1 mutations and mutations in the allosteric dGTP-binding site of SAMHD1 for defects in RNase or dNTPase activity, we identify SAMHD1 point mutants that cause loss of one or both functions. The RNase-positive and dNTPase-negative SAMHD1<SUB>D137N</SUB> mutant is able to restrict HIV-1 infection, whereas the RNase-negative and dNTPase-positive SAMHD1<SUB>Q548A</SUB> mutant is defective for HIV-1 restriction. SAMHD1 associates with HIV-1 RNA and degrades it during the early phases of cell infection. SAMHD1 silencing in macrophages and CD4<SUP>+</SUP> T cells from healthy donors increases HIV-1 RNA stability, rendering the cells permissive for HIV-1 infection. Furthermore, phosphorylation of SAMHD1 at T592 negatively regulates its RNase activity in cells and impedes HIV-1 restriction. Our results reveal that the RNase activity of SAMHD1 is responsible for preventing HIV-1 infection by directly degrading the HIV-1 RNA.