80 research outputs found
1-Phenyl-3-(2,4,6-trimethoxyphenyl)prop-2-en-1-one
In the title compound, C18H18O4, the dihedral angle between the mean planes of the aromatic rings is 7.39 (6)°. The dihedral angles between the linking C—C=C—C plane and the phenyl and benzene rings are 11.27 (5) and 4.20 (5)°, respectively
catena-Poly[[aqua(2,2′-bipyridyl)cobalt(II)]-μ-5-nitroisophthalato]
In the crystal structure of the title compound, [Co(C8H3NO6)(C10H8N2)(H2O)]n, there are two symmetry-independent one-dimensional coordination polymers, which are approximately related by noncrystallographic inversion symmetry. Each zigzag chain is constructed from one CoII ion, one O-monodentate 5-nitroisophthalate (ndc) dianion, one N,N′-bidentate 2,2′-bipyridyl ligand and one water molecule. A symmetry-generated O,O′-bidentate ndc dianion completes the cobalt coordination environment, which could be described as very distorted cis-CoN2O4 octahedral. The bridging ndc ligands result in parallel chains running along the a direction, and O—H⋯O hydrogen bonds arising from the water molecules complete the structure
Dibutyl 5-[(4-ethoxycarbonylphenyl)diazenyl]benzene-1,3-dicarboxylate
In the title compound, C25H30N2O6, the dihedral angle between the aromatic rings is 3.79 (1) Å and the N=N bond shows a trans conformation. Both butyl side chains show evidence of disorder
Bis[2,4-pentanedionato(1−)]bis[4,4,5,5-tetramethyl-2-(4-pyridyl)-imidazoline-1-oxyl 3-oxide]manganese(II)
In the title compound, [Mn(C5H7O2)2(C12H16N3O2)], the manganese(II) cation (site symmetry ) is hexacoordinated by four O and two N atoms in a distorted trans-MnN2O4 octahedral geometry. The four O atoms belonging to two 2,4-pentanedionate anions lie in the equatorial plane and the two N atoms occupy the axial coordination sites
Bis(pentane-2,4-dionato-κ2 O,O′)bis[4,4,5,5-tetramethyl-2-(4-pyridyl)imidazoline-1-oxyl 3-oxide-κN 2]manganese(II)
The title compound, [Mn(C5H7O2)2(C12H16N3O2)2], is isostructural with its NiII-containing analogue [Hao, Mu & Kong (2008 ▶). Acta Cryst. E64, m957]. The asymmetric unit comprises one-half of the molecule and the MnII ion is located on an inversion centre. The coordination geometry around the MnII ion is slightly distorted octahedral, comprised of four O and two N atoms, in which the four O atoms in the equatorial plane come from two pentane-2,4-dionate ligands and the two N atoms in the axial coordination sites from 4,4,5,5-tetramethyl-2-(4-pyridyl)imidazoline-1-oxyl 3-oxide
Triaqua(2,2′-bipyridine)(5-nitroisophthalato-κO)nickel(II) monohydrate
In the title compound, [Ni(C8H3NO6)(C10H8N2)(H2O)3]·H2O, the NiII cation is six-coordinated by a chelating 2,2′-bipyridine ligand, one carboxylate O atom from a 5-nitroisophthalate dianion and three water molecules, with a slightly distorted cis-NiN2O4 octahedral geometry. The neutral complex is isolated, in contrast to coordination polymers formed by MnII, CoII and CuII with the same ligand set, but forms an extensive network of O—H⋯O hydrogen bonds between the coordinated and uncoordinated water molecules and carboxylate groups of the 5-nitroisophthalate ions
The permeability of SPION over an artificial three-layer membrane is enhanced by external magnetic field
BACKGROUND: Sensorineural hearing loss, a subset of all clinical hearing loss, may be correctable through the use of gene therapy. We are testing a delivery system of therapeutics through a 3 cell-layer round window membrane model (RWM model) that may provide an entry of drugs or genes to the inner ear. We designed an in vitro RWM model similar to the RWM (will be referred to throughout the paper as RWM model) to determine the feasibility of using superparamagnetic iron oxide (Fe(3)O(4)) nanoparticles (SPION) for targeted delivery of therapeutics to the inner ear. The RWM model is a 3 cell-layer model with epithelial cells cultured on both sides of a small intestinal submucosal (SIS) matrix and fibroblasts seeded in between. Dextran encapsulated nanoparticle clusters 130 nm in diameter were pulled through the RWM model using permanent magnets with flux density 0.410 Tesla at the pole face. The SIS membranes were harvested at day 7 and then fixed in 4% paraformaldehyde. Transmission electron microscopy and fluorescence spectrophotometry were used to verify transepithelial transport of the SPION across the cell-culture model. Histological sections were examined for evidence of SPION toxicity, as well to generate a timeline of the position of the SPION at different times. SPION also were added to cells in culture to assess in vitro toxicity. RESULTS: Transepithelial electrical resistance measurements confirmed epithelial confluence, as SPION crossed a membrane consisting of three co-cultured layers of cells, under the influence of a magnetic field. Micrographs showed SPION distributed throughout the membrane model, in between cell layers, and sometimes on the surface of cells. TEM verified that the SPION were pulled through the membrane into the culture well below. Fluorescence spectrophotometry quantified the number of SPION that went through the SIS membrane. SPION showed no toxicity to cells in culture. CONCLUSION: A three-cell layer model of the human round window membrane has been constructed. SPION have been magnetically transported through this model, allowing quantitative evaluation of prospective targeted drug or gene delivery through the RWM. Putative in vivo carrier superparamagnetic nanoparticles may be evaluated using this model
The E3 Ubiquitin Ligase SCF(Cyclin F) Transmits AKT Signaling to the Cell-Cycle Machinery
The oncogenic AKT kinase is a key regulator of apoptosis, cell growth, and cell-cycle progression. Despite its important role in proliferation, it remains largely unknown how AKT is mechanistically linked to the cell cycle. We show here that cyclin F, a substrate receptor F-box protein for the SCF (Skp1/Cul1/F-box) family of E3 ubiquitin ligases, is a bona fide AKT substrate. Cyclin F expression oscillates throughout the cell cycle, a rare feature among the 69 human F-box proteins, and all of its known substrates are involved in proliferation. AKT phosphorylation of cyclin F enhances its stability and promotes assembly into productive E3 ligase complexes. Importantly, expression of mutant versions of cyclin F that cannot be phosphorylated by AKT impair cell-cycle entry. Our data suggest that cyclin F transmits mitogen signaling through AKT to the core cell-cycle machinery. This discovery has potential implications for proliferative control in malignancies where AKT is activated
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