An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
Despite many calls, functional brain magnetic resonance imaging (fMRI) studies are relatively rare in the domain of entrepreneurship research. This methodological brief presents the brain-imaging method of resting-state fMRI (rs-fMRI) and illustrates its application in neuroentrepreneurship for the first time. In contrast to the traditional task-based fMRI approach, rs-fMRI observes the brain in the absence of cognitive tasks or presentation of stimuli, which offers benefits for improving our understanding of the entrepreneurial mind. Here, we describe the method and provide methodological motivations for performing brain resting-state functional neuroimaging studies on entrepreneurs. In addition, we illustrate the use of seed-based correlation analysis, one of the most common analytical approaches for analyzing rs-fMRI data. In this illustration, we show that habitual entrepreneurs have increased functional connectivity between the insula (a region associated with cognitive flexibility) and the anterior prefrontal cortex (a key region for explorative choice) as compared to managers. This increased connectivity could help promote flexible behavior. Thus in brief, we provide an exemplar of a novel way to expand our understanding of the brain in the domain of entrepreneurship. We discuss possible directions for future research and challenges to be addressed to facilitate the inclusion of re-fMRI studies into neuroentrepreneurship.
In order to gain more insight into the mechanisms underlying mitochondrial inhibition by haloperidol (HP) pyridinium metabolites, we have studied the three dimensional structure of these compounds. In this paper we report the results of experimental (NMR studies in solution, X-ray diffraction) and theoretical methods (molecular dynamics) applied to HPP+. The chlorophenyl and pyridinium rings are found not to be strictly coplanar and a high degree of mobility was observed in the butyroxy chain. Calculations have shown that the most stable structures adopt conformations corresponding to either gauche or trans rotamers. From these data, a model for the interaction of HPP+ with electron transfer complexes in the mitochondrial respiratory chain has been proposed.
In the crystal structure of (E)-8-(3-chlorostyryl)-1,3,7-trimethylxanthine (CSC) [systematic name: (E)-8-(3-chlorostyryl)-1,3,7-trimethyl-3,7-dihydro-1H-purine-2,6-dione], C16H15ClN4O2, the xanthine ring and the lateral styryl chain are coplanar. The crystal packing involves mainly parallel stacking of these planar molecules. The electrostatic potential calculated on the crystal structure conformation confirms the pharmacophore elements associated with MAO-B inhibition.
The chemokine G protein-coupled receptor CC chemokine receptor 5 (CCR5) is used as an entry gate by CCR5-tropic and dual- or CCR5/CXC chemokine receptor 4-tropic strains of HIV to enter the human host cells. Thus, CCR5 antagonists (i.e., maraviroc) have been proven to be clinically effective by preventing the interaction between viral glycoprotein 120 and CCR5 and thus impeding viral entry into host cells. However, the emergence of HIV strains resistant to CCR5 antagonists has been reported in vitro and in vivo, where the virus has adapted to enter the cells via antagonist-bound CCR5. An alternative strategy that should obviate this mode of viral resistance would entail the ablation of the CCR5 portal for HIV entry from the cell surface through agonist-induced receptor internalization. Although this protective effect has been demonstrated clearly with natural CCR5 ligands, the chemoattractant properties of these chemokines have precluded them from further consideration in terms of drug development. Thus, we sought to explore the possibility of developing novel small molecules and selective CCR5 agonists devoid of eliciting chemotaxis. Indeed, the CCR5 agonists described herein were found to induce profound down-modulation of CCR5 (and not CXC chemokine receptor 4) from the cell surface and its sustained sequestration in the intracellular compartment without inducing chemotaxis in vitro. The bioactivity profile of these novel CCR5 agonists is exemplified by the compound (R)-2-(4-cyanophenyl)-N-(1-(1-(N,1-diphenylmethylsulfonamido)propan-2-yl)piperidin-4-yl)acetamide (ESN-196) that potently inhibits HIV-1 infection in human peripheral blood mononuclear cells and macrophages in vitro with potencies comparable to that of maraviroc and moreover demonstrates full activity against a maraviroc-resistant HIV-1 RU570 strain.
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
The title compound, C7H5N3O2, is an inhibitor of nitric oxide synthase and monoamine oxidase. The N1H tautomer crystallized as a dimer and adopts a planar conformation assisted by intramolecular hydrogen bonding.
