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#34705559   2021/10/27 To Up

CCCH-zinc finger antiviral protein relieves immunosuppression of T cell induced by avian leukosis virus subgroup J via NLP-PKC-δ-NFAT pathway.

CCCH-zinc finger antiviral protein (ZAP) can recognize and induce the degradation of mRNAs and proteins of certain viruses, as well as exert its antiviral activity by activating T cell. However, the mechanism of ZAP mediating T cell activation during virus infection remains unclear. Here, we found a potential function of ZAP that relieves immunosuppression of T cell induced by avian leukosis virus subgroup J (ALV-J) via a novel signaling pathway that involves norbin like protein (NLP), protein kinase C delta (PKC-δ) and nuclear factor of activated T cell (NFAT). Specifically, ZAP expression activated T cells by promoting the dephosphorylation and nuclear translocation of NFAT. Furthermore, knockdown of ZAP weakened the reactivity and antiviral response of T cells. Mechanistically, ZAP reduced PKC-δ activity by up-regulating and reactivating NLP through competitively binding with viral protein. Knockdown of NLP decreased the dephosphorylation of PKC-δ by ZAP expression. Moreover, we showed that knockdown of PKC-δ reduced the phosphorylation levels of NFAT and enhanced its nuclear translocation. Taken together, these data revealed that ZAP relieves immunosuppression caused by ALV-J and mediates T cell activation through NLP-PKC-δ-NFAT pathway. The evolution of host defense system is driven synchronously in the process of resisting virus invasion. Accordingly, host innate defense factors exert effectively work in suppressing virus replication. However, it remains unclear that whether the host innate defense factors are involved in antiviral immune response against the invasion of immunosuppressive viruses. Here, we found that CCCH-type zinc finger antiviral protein (ZAP) effectively worked in resistance on immunosuppression caused by avian leukosis virus subgroup J (ALV-J), a classic immunosuppressive virus. Evidence showed that ZAP released the phosphatase activity of NLP inhibited by ALV-J and further activated NFAT by inactivating PKC-δ. This novel molecular mechanism that ZAP regulates antiviral immune response by mediating NLP-PKC-δ-NFAT pathway has greatly enriched the understanding of the functions of host innate defense factors and provided important scientific ideas and theoretical basis for the research of immunosuppressive virus and antiviral immunity.
Mingjun Zhu, Jing Zhou, Defang Zhou, Kunmei Yang, Bin Li, Ziqiang Cheng

2309 related Products with: CCCH-zinc finger antiviral protein relieves immunosuppression of T cell induced by avian leukosis virus subgroup J via NLP-PKC-δ-NFAT pathway.

100ug Lyophilized100 μg25100ug Lyophilized100 100ug1050 ug 100ug Lyophilized10000 tests400 ug

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#34705465   2021/10/27 To Up

Deeper Understanding of Mononuclear Manganese(IV)-Oxo Binding Brønsted and Lewis Acids and the Manganese(IV)-Hydroxide Complex.

Binding of Lewis acidic metal ions and Brønsted acid at the metal-oxo group of high-valent metal-oxo complexes enhances their reactivities significantly in oxidation reactions. However, such a binding of Lewis acids and proton at the metal-oxo group has been questioned in several cases and remains to be clarified. Herein, we report the synthesis, characterization, and reactivity studies of a mononuclear manganese(IV)-oxo complex binding triflic acid, {[(dpaq)Mn(O)]-HOTf} (-HOTf). First, -HOTf was synthesized and characterized using various spectroscopic techniques, including resonance Raman (rRaman) and X-ray absorption spectroscopy/extended X-ray absorption fine structure. In particular, in rRaman experiments, we observed a linear correlation between the Mn-O stretching frequencies of -HOTf (e.g., ν at ∼793 cm) and -M (M = Ca, Zn, Lu, Al, or Sc) and the Lewis acidities of H and M ions, suggesting that H and M bind at the metal-oxo moiety of [(dpaq)Mn(O)]. Interestingly, a single-crystal structure of -HOTf was obtained by X-ray diffraction analysis, but the structure was not an expected Mn(IV)-oxo complex but a Mn(IV)-hydroxide complex, [(dpaq)Mn(OH)](OTf) (), with a Mn-O bond distance of 1.8043(19) Å and a Mn-O stretch at 660 cm. More interestingly, reverted to -HOTf upon dissolution, demonstrating that -HOTf and are interconvertible depending on the physical states, such as -HOTf in solution and in isolated solid. The reactivity of -HOTf was investigated in hydrogen atom transfer (HAT) and oxygen atom transfer (OAT) reactions and then compared with those of -M complexes; an interesting correlation between the Mn-O stretching frequencies of -HOTf and -M and their reactivities in the OAT and HAT reactions is reported for the first time in this study.
Deepika G Karmalkar, Mi Sook Seo, Yong-Min Lee, Youngsuk Kim, Eunsung Lee, Ritimukta Sarangi, Shunichi Fukuzumi, Wonwoo Nam

1567 related Products with: Deeper Understanding of Mononuclear Manganese(IV)-Oxo Binding Brønsted and Lewis Acids and the Manganese(IV)-Hydroxide Complex.

1000 TESTS/0.65ml2.5 mg100 mg200ul10 mg100ul50 ug 1G 25 MG200ug25 mg0.1 mg

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#34705453   2021/10/27 To Up

Development of a Fluorescent-Labeled Trapping Reagent to Detect Reactive Acyl Glucuronides.

Acyl glucuronides are common metabolites of carboxylic acid-containing compounds. Since acyl glucuronides sometimes show high reactivity, they are considered to be involved in drug toxicity. Therefore, it is important to evaluate the risk posed by acyl glucuronides in the development of safe drugs; however, there are no suitable evaluation methods for the early stages of drug discovery. We aimed to develop a trapping reagent that detects reactive acyl glucuronides to assess their risk. We designed a diamine-structured trapping reagent, , and compared its trapping ability with the reported one that has an amino group, and results showed that showed higher accuracy. In the trapping assay with 17 medicines containing a carboxylic acid, trapped acyl glucuronides that had a higher risk of toxicity. In conclusion, can be useful for evaluating the risk of reactive acyl glucuronides.
Chikako Shibazaki, Okishi Mashita, Kyoko Takahashi, Shigeo Nakamura, Tadahiko Mashino, Tomoyuki Ohe

1483 related Products with: Development of a Fluorescent-Labeled Trapping Reagent to Detect Reactive Acyl Glucuronides.

1kit96 tests96 tests

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#34705324   2021/10/27 To Up

Chemical Composition and Cytotoxic Activity of Eucalyptus torquata Luehm. and Eucalyptus salmonophloia F. Muell. Trunk Bark Essential Oils against Human SW620 and MDA-MB-231 Cancer Cell Lines.

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Ghofrane Lahmadi, Aida Lahmar, Mansour Znati, Mohamed Tahar Elaieb, Mohamed Larbi Khouja, Roberta Ascrizzi, Guido Flamini, Abdel Halim Harrath, Leila Chekir-Ghedira, Hichem Ben Jannet

2662 related Products with: Chemical Composition and Cytotoxic Activity of Eucalyptus torquata Luehm. and Eucalyptus salmonophloia F. Muell. Trunk Bark Essential Oils against Human SW620 and MDA-MB-231 Cancer Cell Lines.

1000 0.1 mg1 ml200 100ul10 mg2.5 mg96 wells (1 kit)100ug25 mg100 mg

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#34705001   2021/10/27 To Up

Pincer-supported metal/main-group bonds as platforms for cooperative transformations.

Electron-rich late metals and electropositive main-group elements (metals and metalloids) can be combined to provide an ambiphilic façade for exploring metal-ligand cooperation, yet the instability of the metal/main-group bond frequently limits the study and application of such units. Incorporating main-group donors into pincer frameworks, where they are stabilized and held in proximity to the transition-metal partner, can allow discovery of new modes of reactivity and incorporation into catalytic processes. This Perspective summarizes common modes of cooperativity that have been demonstrated for pincer frameworks featuring metal/main-group bonds, highlighting similarities among boron, aluminium, and silicon donors and identifying directions for further development.
Matthew T Whited

1953 related Products with: Pincer-supported metal/main-group bonds as platforms for cooperative transformations.

100 tests100 assays100ug96 Tests50 assays100ug1,000 tests100Tests500100 assays

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#34704998   2021/10/27 To Up

Role of the (pseudo)halido ligand in ruthenium(II) -cymene α-amino acid complexes in speciation, protein reactivity and cytotoxicity.

The reactions of the dimeric complexes [RuX(η--cymene)] (X = Br, I, SCN) with L-proline (ProH) and -4-hydroxy-L-proline (HypH), in methanol in the presence of NaOH, afforded [RuX(κ,-Pro)(η--cymene)] (X = Br, 1b; I, 1c; SCN, 1d) and [RuX(κ,-Hyp)(η--cymene)] (X = Br, 2b; I, 2c; SCN, 2d), respectively. Alternatively, the one-pot, sequential addition of the appropriate α-amino carboxylate and X salt to [RuCl(η--cymene)] led to [RuX(κ,-Pro)(η--cymene)] (X = N, 1e; NO, 1f; CN 1g) and [Ru(N)(κ,-Hyp)(η--cymene)] (2e). Complexes [Ru(κ,,'-OCCH(NH)(R)O)(η--cymene)] (R = CH, 3h; R = CHMe, 4h; R = CHCH, 5h) were prepared from the reaction of [RuCl(η--cymene)] with the appropriate α-amino acid and NaOH in refluxing isopropanol. Treatment of the L-serine (SerH) derivative [RuCl(κ,-SerH)(η--cymene)] (3a) with 1,3,5-triaza-7-phosphaadamantane (PTA) in water at reflux produced [Ru(κ,-Ser)(κ-PTA)(η--cymene)]Cl ([3i]Cl). The products were isolated in good to excellent yields, and were characterized by elemental analysis, IR and multinuclear NMR spectroscopy. The structures of 1f and 2b-e were ascertained by X-ray diffraction studies. The behaviour of the complexes in water and cell culture medium was investigated by multinuclear NMR and UV-Vis spectroscopy, revealing a considerable influence of the monodentate ligand on the aqueous chemistry. Complexes 1d-e, 2d-e, 3h, 4h and [3i]Cl, showing substantial inertness in aqueous media, were assessed for their cytotoxicity towards A2780 and A2780cisR cancer cell lines and the noncancerous HEK 293T cell line. A selection of compounds was also investigated for Ru uptake in A2780 cells and interactions with cytochrome c as a model protein. Combined, these studies provide insights into the previously debated role of the '' ligand on the biological activity of Ru(II) arene α-amino acid complexes.
Lorenzo Biancalana, Emanuele Zanda, Mouna Hadiji, Stefano Zacchini, Alessandro Pratesi, Guido Pampaloni, Paul J Dyson, Fabio Marchetti

1817 related Products with: Role of the (pseudo)halido ligand in ruthenium(II) -cymene α-amino acid complexes in speciation, protein reactivity and cytotoxicity.

100ug Lyophilized100ug Lyophilized50 100ug Lyophilized100ug Lyophilized100ug Lyophilized96tests100ug Lyophilized100ug Lyophilized100ug Lyophilized1 Set100ug Lyophilized

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#34704993   2021/10/27 To Up

Using quantum dynamics to study the effect of energy efficiency on the reactivity of the OH + DBr reaction.

We report a time-dependent, full dimensional, wave-packet calculation for the reaction of OH + DBr to examine the effect of the energy efficiency on the reactivity. This study shows that the vibrational excitations of the OH and DBr enhance the reaction. However, the rotational excitations of OH and DBr both hinder the reaction. As a result, the vibrational energies of both the OH and DBr reactants are more efficient at promoting the reactivity than the translational energy, while the rotational energies of OH and DBr are less effective than the translational energy. By analyzing the state population of the vibrational and rotational states along the reaction pathway, we also developed an approach in order to explain the enhancement of the vibrational excitation and the hindrance of the rotational excitation of the reaction. We found that the initial-state selected vibrational excited states of OH and DBr are the dominant components, respectively, for surmounting the barrier. However, the initial-state selected rotational excited states of OH and DBr are no longer the dominant states for surmounting the transition state owing to their population changes in the van der Waals well. This quantitative analysis demonstrates the potential well in the entrance valley plays an important role in the energy efficiency with regards to the reactivity.
Yuping Wang, Shuhua Shi, Ruishan Tan, Wei Yan, Delu Gao, Dunyou Wang

1230 related Products with: Using quantum dynamics to study the effect of energy efficiency on the reactivity of the OH + DBr reaction.

500 Units1 ml11250 IU

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#34704879   2021/10/27 To Up

Acute Titanium dioxide nanoparticles exposure impaired spatial cognitive performance through neurotoxic and oxidative mechanisms in Wistar rats.

Titanium dioxide nanoparticles (TiO2-NPs) are used in many commercial products. However, their effects on human and animal organism remained to be clarified.
Rihane Naima, Mrad Imen, Jeljeli Mustapha, Hafedh Abdelmalek, Kacem Kamel, Mohsen Sakly, Amara Amara

1194 related Products with: Acute Titanium dioxide nanoparticles exposure impaired spatial cognitive performance through neurotoxic and oxidative mechanisms in Wistar rats.

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#34704808   2021/10/27 To Up

Mapping SARS-CoV-2 Antibody Epitopes in COVID-19 Patients with a Multi-Coronavirus Protein Microarray.

The rapid worldwide spread of SARS-CoV-2 has accelerated research and development for controlling the COVID-19 pandemic. A multi-coronavirus protein microarray was created containing full-length proteins, overlapping protein fragments of various lengths, and peptide libraries from SARS-CoV-2 and four other human coronaviruses. Sera from confirmed COVID-19 patients as well as unexposed individuals were applied to multicoronavirus arrays to identify specific antibody reactivity. High-level IgG, IgM, and IgA reactivity to structural proteins S, M, and N of SARS-CoV-2, as well as accessory proteins such as ORF3a and ORF7a, were observed that were specific to COVID-19 patients. Antibody reactivity against overlapping 100-, 50-, and 30-amino acid fragments of SARS-CoV-2 proteins was used to identify antigenic regions. Numerous proteins of SARS-CoV, Middle East respiratory syndrome coronavirus (MERS-CoV), and the endemic human coronaviruses HCoV-NL63 and HCoV-OC43 were also more reactive with IgG, IgM, and IgA in COVID-19 patient sera than in unexposed control sera, providing further evidence of immunologic cross-reactivity between these viruses. Whereas unexposed individuals had minimal reactivity against SARS-CoV-2 proteins that poorly correlated with reactivity against HCoV-NL63 and HCoV-OC43 S2 and N proteins, COVID-19 patient sera had higher correlation between SARS-CoV-2 and HCoV responses, suggesting that antibodies against SARS-CoV-2 cross-react with HCoV epitopes. Array responses were compared with validated spike protein-specific IgG enzyme-linked immunosorbent assays (ELISAs), showing agreement between orthologous methods. SARS-CoV-2 microneutralization titers were low in the COVID-19 patient sera but correlated with array responses against S and N proteins. The multi-coronavirus protein microarray is a useful tool for mapping antibody reactivity in COVID-19 patients. With novel mutant SARS-CoV-2 variants of concern on the rise, knowledge of immune specificities against SARS-CoV-2 proteins is increasingly important for understanding the impact of structural changes in antibody-reactive protein epitopes on naturally acquired and vaccine-induced immunity, as well as broader topics of cross-reactivity and viral evolution. A multi-coronavirus protein microarray used to map the binding of COVID-19 patient antibodies to SARS-CoV-2 proteins and protein fragments as well as to the proteins of four other coronaviruses that infect humans has shown specific regions of SARS-CoV-2 proteins that are highly reactive with patient antibodies and revealed cross-reactivity of these antibodies with other human coronaviruses. These data and the multi-coronavirus protein microarray tool will help guide further studies of the antibody response to COVID-19 and to vaccination against this worldwide pandemic.
David Camerini, Arlo Z Randall, Krista Trappl-Kimmons, Amit Oberai, Christopher Hung, Joshua Edgar, Adam Shandling, Vu Huynh, Andy A Teng, Gary Hermanson, Jozelyn V Pablo, Megan M Stumpf, Sandra N Lester, Jennifer Harcourt, Azaibi Tamin, Mohammed Rasheed, Natalie J Thornburg, Panayampalli S Satheshkumar, Xiaowu Liang, Richard B Kennedy, Angela Yee, Michael Townsend, Joseph J Campo

1221 related Products with: Mapping SARS-CoV-2 Antibody Epitopes in COVID-19 Patients with a Multi-Coronavirus Protein Microarray.

100ug Lyophilized200ul100ug Lyophilized100ug Lyophilized100ug Lyophilized1 Set1 Set1 Set1 Set1 Set1 Set100ug Lyophilized

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