Metal-Free Catalytic Approach for Allylic C–H Amination Using <i>N</i>‑Heterocycles via sp³ C–H Bond Activation

A versatile metal-free synthesis of allylic <i>N</i>-heterocycles has been developed using a TBAI/TBHP oxidation system. This general protocol could be applied for the C–N bond formation of electron-deficient phthalimides, imidazoles, triazoles, and sulfonamides with cyclic and acylic olefins. The practical use of the method is demonstrated by the amidation of functionalized biologically active substrates

755700 – Supplemental material for A Framework for Improvement: Analyzing Performance-Assessment Scores for Evidence-Based Teacher Preparation Program Reforms

<p>Supplemental material, 755700 for A Framework for Improvement: Analyzing Performance-Assessment Scores for Evidence-Based Teacher Preparation Program Reforms by Kevin C. Bastian, Diana Lys and Yi Pan in Journal of Teacher Education</p

718182sp – Supplemental material for Evaluating Teacher Preparation Programs With Teacher Evaluation Ratings: Implications for Program Accountability and Improvement

<p>Supplemental material, 718182sp for Evaluating Teacher Preparation Programs With Teacher Evaluation Ratings: Implications for Program Accountability and Improvement by Kevin C. Bastian, Kristina M. Patterson and Yi Pan in Journal of Teacher Education</p

Receptor-transporting protein (RTP) family members play divergent roles in the functional expression of odorant receptors

<div><p>Receptor transporting protein (RTP) family members, RTP1S and RTP2, are accessory proteins to mammalian odorant receptors (ORs). They are expressed in the olfactory sensory neurons and facilitate OR trafficking to the cell-surface membrane and ligand-induced responses in heterologous cells. We previously identified different domains in RTP1S that are important for different stages of OR trafficking, odorant-mediated responses, and interaction with ORs. However, the exact roles of RTP2 and the significance of the requirement of the seemingly redundant co-expression of the two RTP proteins <i>in vivo</i> have received less attention in the past. Here we attempted to dissect the functional differences between RTP1S and RTP2 using a HEK293T cell-based OR heterologous expression system. When a set of 24 ORs were tested against 28 cognate ligands, unlike RTP1S, which always showed a robust ability to support odorant-mediated responses, RTP2 had little or no effect on OR responses and exhibited a suppressive effect over that of RTP1S for a subset of the ORs tested. RTP1S and RTP2 showed no significant difference in OR ligand selectivity and co-transfection with RTP2 increased the detection threshold for some ORs. A protein-protein interaction analysis showed positive interactions among OR, RTP1S, and RTP2, corroborating the functional linkages among the three molecules. Finally, further cell-surface and permeabilized immunocytochemical studies revealed that OR and the co-expressed RTP1S proteins were retained in the Golgi when co-transfected with RTP2, indicating that RTP1S and RTP2 could play different roles in the OR trafficking process. By examining the functional differentiations between the two RTP family members, we provided a molecular level explanation to the suppressive effect exerted by RTP2, shedding light on the divergent mechanisms underlying the RTP proteins in regulating the functional expression of ORs.</p></div

OR, RTP1S, and RTP2 interact with each other in HEK293T cells.

<p><i>Left</i>, interactions among MOR258-5 (Category 1), RTP1S and RTP2. <i>Right</i>, interactions among MOR23-1 (Category 2), RTP1S and RTP2. <i>First and second panels</i>, protein lysates of HEK293T cells transfected with Flag-tagged OR and/or HA-tagged RTP1S and Flag-tagged/HA-tagged RTP2 and blotted with anti-Flag or anti-HA antibody. <i>Third panels</i>, co-immunoprecipitation of Flag-tagged proteins with anti-HA antibody. <i>Fourth panels</i>, co-immunoprecipitation of HA-tagged proteins with anti-Flag antibody. Refer to <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0179067#pone.0179067.s004" target="_blank">S4 Fig</a> for the original blots. <i>IB</i>, immunoblot; <i>IP</i>, immunoprecipitation. The asterisks indicate non-specific bands.</p

Catalyst-Free Intramolecular Oxidative Cyclization of <i>N</i>‑Allylbenzamides: A New Route to 2,5-Substituted Oxazoles

A catalyst-free intramolecular oxidative cyclization reaction of <i>N</i>-allylbenzamides has been developed to prepare 2,5-disubstituted oxazoles with good yields. This reaction gives an efficient synthetic strategy to form an oxazole nucleus directly from easily accessible substrates under temperate conditions

RTP1S and RTP2 play divergent roles in OR trafficking.

<p>(A-B) permeabilized staining were performed to examine the subcellular localizations of MOR180-1 (Category 1) and MOR23-1 (Category 2) when they were transfected alone or cotransfected with different RTPs or a combination of the two RTPs. <i>Left panels</i>, red signals represent the localization of OR proteins. <i>Middle panel</i>, green signals represent staining of organelles; <i>first row</i>, staining of ER with calnexin; <i>second row</i>, staining of Golgi with wheat germ agglutinin. <i>Right panels</i>, yellow signals represent OR proteins merged with the corresponding organelle. Blue signals in the <i>second row</i> are DAPI nuclear staining. Scale bar, 100 μm. (C-D) quantification of the cell-surface expression and subcellular localizations of the 4 tested ORs and RTPs. Columns represent the cells of each counting session where the OR or RTP proteins were localized in the ER, the Golgi, or at the cell surface. The <i>y</i>-axis represents the cell numbers of each counting session where the OR or RTP proteins were localized in ER, Golgi, or at the cell surface, shown as mean ± S.E.M. (<i>N</i> = 3). Paired two-tailed <i>t</i> test was used to compare the localizations in certain organelle or at the cell surface when different combinations of OR and RTP were cotransfected. * <i>P</i> < 0.05, ** <i>P</i> < 0.01.</p

Cu-Catalyzed C(sp³)–H Bond Activation Reaction for Direct Preparation of Cycloallyl Esters from Cycloalkanes and Aromatic Aldehydes

Cu-catalyzed dehydrogenation–olefination and esterification of C­(sp³)–H bonds of cycloalkanes with TBHP as an oxidant has been developed. The reaction involves four C–H bond activations and gives cycloallyl ester products directly from cycloalkanes and aromatic aldehydes

RTP1S and RTP2 differ in their abilities to promote the functional activation of ORs.

<p>(A-B) normalized luciferase activities of concentration gradients of 28 odorants from 0 μM to 30, 300 or 320 μM tested against 24 ORs with different combinations of RTPs co-transfected, including RTP1S (red), RTP2 (green), and a combination of the two (purple) in HEK293T cells. An “OR only” negative control is co-transfected with the empty pCI vector (blue). The <i>x</i>-axis represents molar odorant concentrations on a logarithmic scale. The <i>y</i>-axis represents normalized luciferase activity shown as mean ± S.E.M. (<i>N</i> = 3). The scatter diagrams (inset) depict the functional effect induced by the combination of RTP1S and RTP2 compared to RTP1S or RTP2 alone (<i>Materials and methods</i> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0179067#pone.0179067.s001" target="_blank">S1 Fig</a>). The <i>x</i>-axis represents the value of the parameter τ_RTP1S, which represents the ratio of the OR response level when co-transfected with RTP1S to the algebraic sum of individual OR response levels when co-transfected with single RTPs. The <i>y</i>-axis represents the value of the parameter σ, with σ = 1 dividing the diagram into hyper-addition and hypo-addition sections. The responses at lower concentrations that did not elicit OR activation were not plotted.</p

Access to Alkyl-Substituted Lactone via Photoredox-Catalyzed Alkylation/Lactonization of Unsaturated Carboxylic Acids

An efficient photoredox-catalyzed alkylation/lactonization reaction of unsaturated carboxylic acids by using alkyl <i>N</i>-hydroxyphthalimide esters as alkylation reagents has been developed. Varieties of redox-active esters derived from aliphatic carboxylic acids were proved viable in this method, affording alkyl substituted lactones in moderate to good yields. This redox-neutral procedure features mild conditions and operational simplicity, which provides a new strategy for the synthesis of alkyl substituted lactones