Kondrupvalentin2245

(PsycInfo Database Record (c) 2021 APA, all rights reserved).In this study, we conducted a citation network analysis of the Journal of Counseling Psychology (JCP) to elucidate the scope, evolution, and interconnections of JCP publications as reflected in how authors use (i.e., cite) these publications. We used CitNetExplorer to analyze a network of 4,718 JCP publications and 16,959 citation links. The analysis yielded 19 clusters in JCP's citation network. Z-DEVD-FMK supplier The most dominant facet of the citation network focused on counseling, counseling process, and counseling outcome. The clusters in this facet shifted from an early focus on perceptions of counselors to continuing examinations of what happens in counseling. Another dominant facet comprised clusters on vocational psychology, shifting from an earlier focus on vocational choice and interest, to career counseling and decision making, to vocational and academic development processes and predictors. These major facets converged toward a continuing cluster focused on methodology and analysis along with race, gender, sexuality, and other diversity scholarship. This suggests that diversity-focused publications in JCP often employ and cite methodological and analytic advances. The results also reveal discontinued areas of scholarship in JCP that are ripe for revisiting and rebuilding in new directions (e.g., anger and social justice activism; clinical judgment and artificial intelligence). The results suggest that a promising next step in the evolution of JCP would be for authors to engage with and cite diversity scholarship as central to "general" domains of JCP scholarship. (PsycInfo Database Record (c) 2021 APA, all rights reserved).Developing a rapid, simple, and sensitive method to analyze drugs is critical to forensic research study because of the widespread occurrence of the matrix effect. Herein, we develop a method using thermal-assisted carbon fiber ionization mass spectrometry that can be used to directly analyze drugs in biological fluid. The key feature of this technique is that the biological samples such as urine and blood can be achieved online as precipitated protein on the carbon fiber tip and thermally desorbed by the metal ceramics heater, which can reduce the matrix effects and improve the sensitivity. Analytes including raw urine, blood, oral fluid, drink, tobacco tar, drug tablets, and paper cards can be rapidly identified and analyzed within a few minutes regardless of their physical variations. Due to its simplicity and noninvasive analysis, this method can be used for drugged driving analysis and to achieve point-of-care drug testing in clinical and forensic chemistry.A novel palladium-catalyzed decarboxylative cascade cyclization for the assembly of diverse fused heteropolycycles by employing α-oxocarboxylic acids as three-carbon insertion units is reported. This protocol enables the synthesis of isoquinolinedione- and indolo[2,1-a]isoquinolinone-fused benzocycloheptanones in moderate to good yields by the use of different aryl iodides, including alkene-tethered 2-iodobenzamides and 2-(2-iodophenyl)-1H-indoles. Notably, the approach achieves simultaneous construction of both six- and seven-membered rings via sequential intramolecular carbopalladation, C-H activation, and decarboxylation.A new solid-phase peptide synthesis and bioprofiling of the antimicrobial activity of lugdunin, a fibupeptide, enable a comprehensive structure-activity relationship (SAR) study (MRSA Staphylococcus aureus). Distinct lugdunin analogues with variation of the three important amino acids Val2, Trp3, and Leu4 are readily available based on the established high-output synthesis. This efficient synthesis concept takes advantage of the presynthesized thiazolidine building block. To gain further knowledge of SAR, d-Val2, and d-Leu4 were replaced with aliphatic amino acids. For l-Trp3 derivatization, a set of non-natural aromatic amino acids with manifold substitution and annulation patterns precisely shows structural imperatives, starting from the exchange of d-Val6 → d-Trp6 with a 2-fold improved biological activity. d-Trp6-lugdunin analogues with additional variation of d-Val2 and d-Leu4 residues were designed and synthesized followed by antimicrobial profiling. For the first time, these SAR studies deliver valuable information on the tolerance of other amino acids to d-Val2, l-Trp3, and d-Leu4 in the sequence of lugdunin.The first asymmetric synthetic approach to biologically relevant 3,3-diphenyloloxindoles was developed using para-quinone methides derived from isatins and phenols. Chiral phosphoric acid efficiently catalyzed the reaction and delivered 3,3-diphenyloloxindoles under mild conditions with up to an equivalent yield and excellent enantioselectivity (up to >99% ee). The chirality was maintained in further synthesis.Proteins fold on relatively smooth free energy landscapes which are biased toward the native state, but even simple topologies which fold rapidly can experience roughness on their free energy landscape. The details of these interactions are difficult to elucidate experimentally. Closely related to the problem of deciphering the details of the free energy landscape is the problem of defining the interactions in the denatured state ensemble (DSE) which is populated under native conditions, that is, under conditions where the native state is stable. The DSE of many proteins deviates from random coil models, but quantifying and defining the energetics of the transiently populated interactions in this ensemble is extremely challenging. Characterization of the DSE of proteins which fold to compact structures is also relevant to studies of intrinsically disordered proteins (IDPs) since interactions in the dynamic ensemble populated by IDPs can modulate their behavior. Here we show how experimental thermodynamic and pKa measurements can be combined with computational thermodynamic integration to quantify interactions in the DSE. We show that non-native side chain interactions can stabilize native backbone structure in the DSE and demonstrate that that even rapidly folding proteins can form energetically significant non-native interactions in their DSE. As an example, we characterize a non-native salt bridge that stabilizes local native backbone structure in the DSE of a widely studied fast-folding protein, the villin headpiece helical domain. The combined computational experimental approach is applicable to other protein unfolded states and provides insight that is impossible to obtain with either method alone.