Fast-spiking parvalbumin^+ GABAergic interneurons: From cellular design to microcircuit function

The success story of fast-spiking, parvalbumin-positive (PV+) GABAergic interneurons (GABA, γ-aminobutyric acid) in the mammalian central nervous system is noteworthy. In 1995, the properties of these interneurons were completely unknown. Twenty years later, thanks to the massive use of subcellular patch-clamp techniques, simultaneous multiple-cell recording, optogenetics, in vivo measurements, and computational approaches, our knowledge about PV+ interneurons became more extensive than for several types of pyramidal neurons. These findings have implications beyond the “small world” of basic research on GABAergic cells. For example, the results provide a first proof of principle that neuroscientists might be able to close the gaps between the molecular, cellular, network, and behavioral levels, representing one of the main challenges at the present time. Furthermore, the results may form the basis for PV+ interneurons as therapeutic targets for brain disease in the future. However, much needs to be learned about the basic function of these interneurons before clinical neuroscientists will be able to use PV+ interneurons for therapeutic purposes

Bis(1,3,4-thia­diazol-2-yl) disulfide

The title compound, C4H2N4S4, lies about a twofold rotation axis situated at the mid-point of the central S—S bond. Each of two thia­diazole rings is essentially planar, with an rms deviation for the unique thia­diazole ring plane of 0.0019 (7) Å. C—H⋯N hydrogen bonds link adjacent mol­ecules, forming zigzag chains along the c axis. In addition, these chains are connected by inter­molecular S⋯S inter­actions [S⋯S = 3.5153 (11) Å] , forming corrugated sheets, and further fabricate a three-dimensional supra­molecular structure by inter­molecular N⋯S contacts [S⋯N = 3.1941 (17) Å]

catena-Poly[[[bis­[2,2′-(propane-1,3-diyl­dithio)bis­(1,3,4-thia­diazole)-κN 4]copper(II)]-bis­[μ-2,2′-(propane-1,3-diyldithio)bis­(1,3,4-thia­diazole)-κ2 N 4:N 4′]] bis­(perchlorate)]

In the title compound, {[Cu(C7H8N4S4)4](ClO4)2}n, the CuII atom, occupying a crystallographic inversion centre, is six-coordinated by six N atoms of three symmetry-related 2,2′-(propane-1,3-diyldithio)bis­(1,3,4-thia­diazole) (L) ligands in a slightly distorted octa­hedral geometry. The ligand L adopts two kinds of coordination modes in the crystal structure; one is a monodentate coordination mode and serves to complete the octa­hedral coordination of the Cu atom and the other is an N:N′-bidentate bridging mode in a trans configuration, bridging Cu atoms via translation symmetry along the b axis into a chain structure. The perchlorate ions serve as acceptors for inter­molecular C—H⋯O hydrogen bonds, which link the chains into a three-dimensional network

Poly[[tris­[μ-2,2′-(butane-1,4-diyl­dithio)bis­(1,3,4-thia­diazole)-κ2 N 4:N 4′]copper(II)] bis­(perchlorate)]

In the title compound, {[Cu(C8H10N4S4)3](ClO4)2}n, the CuII atom is located on a threefold inversion axis coordinated by six N atoms of symmetry-equivalent 2,2′-(butane-1,4-diyl­dithio)bis­(1,3,4-thia­diazole) ligands in a slightly distorted octa­hedral geometry. Adjacent CuII atoms are linked by the bridging bidentate thia­diazole ligands, which are situated about inversion centers. This leads to the formation of a three-dimensional network structure

Multi-Objective Ant Colony Algorithm in EPC Risk Control

AbstractAccording to the risks and risk control target in energy performance contracting (EPC), this paper has designed the risk control measure set. On the basis, a risk control model is put forward, including the risk evaluation, risk control cost, risk loss. Then, a multi-objective ant colony algorithm, based on Pareto theory, is used to solve the model. A series of Pareto optimal solutions are got by example. The result shows that the solutions have the better diversity and convergence. At the same time, the model can find the best combination of various risk control measures in EPC, which can provide direct evidence for the company of EPC

Poly[[bis­(acetonitrile-κN)bis­[μ2-2,2′-(methyl­enedithio)bis­(1,3,4-thia­diazole)-κ2 N 4:N 4′]copper(II)] bis­(perchlorate) acetonitrile solvate]

In the title compound, {[Cu(C5H4N4S4)2(C2H3N)2](ClO4)2·C2H3N}n, the CuII atom occupies a crystallographic inversion centre and is six-coordinated by six N atoms of four symmetry-related 2,2′-(methyl­enedithio)bis­(1,3,4-thia­diazole) (L) ligands and two acetonitrile mol­ecules in a slightly distorted octa­hedral geometry. The ligand L adopts an N:N′-bidentate bridging mode in a trans configuration, bridging the Cu atoms via translation symmetry, forming a two-dimensional layer-like structure. The perchlorate ions serve as acceptors for inter­molecular C—H⋯O hydrogen bonds, which link the layers into a three-dimensional network. The ClO4 − anion is disordered with an occupation ratio of 0.658:0.342

Poly[μ2-chlorido-(μ2-3H +-1,3,4-thia­diazo­lium-2-thiol­ato-κ2 S:S)silver(I)]

In the title compound, [AgCl(C2H2N2S2)]n, the AgI ion has a distorted tetra­hedral geometry, defined by two S atoms of two symmetry-related 1,3,4-thia­diazo­lium-2-thiol­ate ligands and two chloride ions. The AgI ions are bridged into a two-dimensional network parallel to the ab plane by chloride ions and thia­diazole ligands. In the network, the AgI ions are separated by 4.0316 (12) Å along the a axis and by 4.8822 (13) Å along the b axis. N—H⋯Cl hydrogen bonds are observed within the network

Expression, purification and structural analysis of functional GABA transporter 1 using the baculovirus expression system

The γ-aminobutyric acid (GABA) transporter 1 (GAT1) belongs to a family of Na+ and Cl−-coupled transport proteins and possesses 12 putative transmembrane domains. To perform structural analyses of the GAT1 protein, the GAT1/green fluorescent protein (GFP) fusion protein was functionally expressed in insect Sf9 cells by the BAC-TO-BAC® baculovirus expression system. A two-step procedure to purify the GAT1/GFP fusion protein from insect Sf9 cells has been established and involves immunoaffinity chromatography using self-prepared anti-GFP antibodies and size-exclusion fast protein liquid chromatography (SE- FPLC). A yield of 200–300 μg of the GAT1/GFP protein could be purified from 400–600 mL of infected Sf9 cells. The purified protein was analyzed by transmission electron microscopy (TEM), which revealed that the GAT1/GFP fusion protein was isolated in its monomeric form