(3-Allyl­oxypicolinato-κ2 N,O 2)bis­[3,5-difluoro-2-(2-pyrid­yl)phenyl-κ2C1,N]iridium(III)

The title complex, [Ir(C11H6F2N)2(C9H8NO3)], consists of one IrIII ion, two C,N-bidentate 3,5-difluoro-2-(2-pyrid­yl)phenyl (F2ppy) ligands and one N,O-bidentate 3-allyl­oxypicolinate (pic-3-Oall) ligand. The IrIII ion is hexa­coordinated by two C atoms and two N atoms from the F2ppy ligands and one N atom and one carboxyl­ate O atom from the pic-3-Oall ligand, displaying a distorted octa­hedral geometry. In the crystal structure, weak inter­molecular C—H⋯F and C—H⋯O hydrogen bonds link the complex mol­ecules into a three-dimensional supra­molecular structure

1-[6-(9H-Carbazol-9-yl)hex­yl]-2-phenyl-1H-benzimidazole

The mol­ecule of the title compound, C31H29N3, contains a hexyl chain, a coordination unit (benzimidazole) and a functional group (carbazole). The benzimidazole ring is not coplanar with either the phenyl ring or the carbazole system, making dihedral angles of 43.26 (3) and 39.03 (2)°, respectively. The dihedral angle between the phenyl ring and the carbazole system is 24.42 (3)°. The hexyl Cβ atom (with respect to benzimidazole) deviates by 1.124 (2) Å from the benzimidazole plane, although the Cα atom lies in the plane. The hexyl Cβ atom (with respect to carbazole) deviates by 1.315 (1) Å from the carbazole plane, although the Cα atom lies in the plane. The crystal structure is stabilized by inter­molecular C—H⋯π inter­actions

Neuroprotective effects of lomerizine on retinal ganglion cells in the diet-induced obese C57BL/6J mice

AIM: To research the neuroprotective effects of lomerizine(LOM)on retinal ganglion cells(RGCs)in the diet-induced obese C57BL/6J mice. <p>METHODS: Fifty-four mice were randomly divided into two groups which were fed a high-fat diet for 19wk. One group mice were lavaged LOM by the dosage of 80mg/kg daily at the same time. The obese mice were selected and divided into diet-induced obesity(DIO)group, diet-induced obesity and lomerizine(DIO+LOM)group. The mice in the control(CON)group were fed a basal diet. The ultrastructural changes of RGCs were detected by transmission electron microscope. The cellular apoptosis was detected by TUNEL. The laser scanning confocal microscope was used to measure intracellular calcium ion concentration. <p>RESULTS: Compared with the CON group, the RGCs in DIO group showed smaller and condensation of nuclear chromatin and increased electron density of the cytoplasm, whereas the changes in DIO+LOM mice were obviously diminished. TUNEL staining showed that the number of apoptosis cells in the ganglion cell layer(GCL)increased in DIO group and the percentage of apoptotic cells was much higher than that in the CON groups(<i>P</i><0.01). The DIO+LOM group mice showed fewer apoptosis cells and the percentage of apoptotic cells in this group were significantly decreased than the DIO mice(<i>P</i><0.05). The Laser scanning confocal microscope detection showed Ca²⁺ staining intensity of RGCs in DIO group increased and its staining intensity ratio was significantly higher than in CON group(<i>P</i><0.01), the Ca²⁺ staining intensity and its staining intensity ratio in DIO+LOM group were significantly decreased than the DIO group(<i>P</i><0.01). <p>CONCLUSION: Lomerizine has neuroprotective effects on damage of retinal ganglion cells in diet-induced obesity mice, which may be related to the attenuation of intracellular Ca²⁺ overload

The cold-induced basic helix-loop-helix transcription factor gene MdCIbHLH1 encodes an ICE-like protein in apple

<p>Abstract</p> <p>Background</p> <p>Plant growth is greatly affected by low temperatures, and the expression of a number of genes is induced by cold stress. Although many genes in the cold signaling pathway have been identified in <it>Arabidopsis</it>, little is known about the transcription factors involved in the cold stress response in apple.</p> <p>Results</p> <p>Here, we show that the apple bHLH (basic helix-loop-helix) gene <it>MdCIbHLH1 </it>(<it>Cold-Induced bHLH1</it>), which encodes an ICE-like protein, was noticeably induced in response to cold stress. The MdCIbHLH1 protein specifically bound to the MYC recognition sequences in the <it>AtCBF3 </it>promoter, and <it>MdCIbHLH1 </it>overexpression enhanced cold tolerance in transgenic <it>Arabidopsis</it>. In addition, the MdCIbHLH1 protein bound to the promoters of <it>MdCBF2 </it>and favorably contributed to cold tolerance in transgenic apple plants by upregulating the expression of <it>MdCBF2 </it>through the CBF (C-repeat-binding factor) pathway. Our findings indicate that MdCIbHLH1 functions in stress tolerance in different species. For example, ectopic <it>MdCIbHLH1 </it>expression conferred enhanced chilling tolerance in transgenic tobacco. Finally, we observed that cold induces the degradation of the MdCIbHLH1 protein in apple and that this degradation was potentially mediated by ubiquitination and sumoylation.</p> <p>Conclusions</p> <p>Based on these findings, <it>MdCIbHLH1 </it>encodes a transcription factor that is important for the cold tolerance response in apple.</p