CCDC 955622: Experimental Crystal Structure Determination

Related Article: Christopher C. Underwood, Bradley S. Stadelman, Mark L. Sleeper, Julia L. Brumaghim|2013|Inorg.Chim.Acta|405|470|doi:10.1016/j.ica.2013.02.027,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

CCDC 975012: Experimental Crystal Structure Determination

Related Article: Martin M. Kimani, Craig A. Bayse, Bradley S. Stadelman, and Julia L. Brumaghim|2013|Inorg.Chem.|52|11685|doi:10.1021/ic401366c,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

CCDC 988778: Experimental Crystal Structure Determination

Related Article: Bradley S. Stadelman, Martin M. Kimani, Craig A. Bayse, Colin D. McMillen, Julia L. Brumaghim|2016|Dalton Trans.|45|4697|doi:10.1039/C5DT03384E,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

CCDC 988779: Experimental Crystal Structure Determination

Related Article: Bradley S. Stadelman, Martin M. Kimani, Craig A. Bayse, Colin D. McMillen, Julia L. Brumaghim|2016|Dalton Trans.|45|4697|doi:10.1039/C5DT03384E,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

CCDC 988776: Experimental Crystal Structure Determination

Related Article: Bradley S. Stadelman, Martin M. Kimani, Craig A. Bayse, Colin D. McMillen, Julia L. Brumaghim|2016|Dalton Trans.|45|4697|doi:10.1039/C5DT03384E,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

CCDC 988777: Experimental Crystal Structure Determination

Related Article: Bradley S. Stadelman, Martin M. Kimani, Craig A. Bayse, Colin D. McMillen, Julia L. Brumaghim|2016|Dalton Trans.|45|4697|doi:10.1039/C5DT03384E,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

Oxidation of Biologically Relevant Chalcogenones and Their Cu(I) Complexes: Insight into Selenium and Sulfur Antioxidant Activity

Hydroxyl radical damage to DNA causes disease, and sulfur and selenium antioxidant coordination to hydroxyl-radical-generating Cu⁺ is one mechanism for their observed DNA damage prevention. To determine how copper binding results in antioxidant activity, biologically relevant selone and thione ligands and Cu⁺ complexes of the formula [Tpm*Cu­(L)]⁺ [Tpm* = tris­(3,5-dimethylpyrazolyl)­methane; L = <i>N</i>,<i>N</i>′-dimethylimidazole selone or thione] were treated with H₂O₂ and the products analyzed by ¹H, ¹³C­{¹H}, and ⁷⁷Se­{¹H} NMR spectroscopy, mass spectrometry, and X-ray crystallography. Upon H₂O₂ treatment, selone and thione binding to Cu⁺ prevents oxidation to Cu²⁺; instead, the chalcogenone ligand is oxidized. Thus, copper coordination by sulfur and selenium compounds can provide targeted sacrificial antioxidant activity

Arsenic and Its Methylated Metabolites Inhibit the Differentiation of Neural Plate Border Specifier Cells

Exposure to arsenic in food and drinking water has been correlated with adverse developmental outcomes, such as reductions in birth weight and neurological deficits. Additionally, studies have shown that arsenic suppresses sensory neuron formation and skeletal muscle myogenesis, although the reason why arsenic targets both of these cell types in unclear. Thus, P19 mouse embryonic stem cells were used to investigate the mechanisms by which arsenic could inhibit cellular differentiation. P19 cells were exposed to 0, 0.1, or 0.5 μM sodium arsenite and induced to form embryoid bodies over a period of 5 days. The expression of transcription factors necessary to form neural plate border specifier (NPBS) cells, neural crest cells and their progenitors, and myocytes and their progenitors were examined. Early during differentiation, arsenic significantly reduced the transcript and protein expression of Msx1 and Pax3, both needed for NPBS cell formation. Arsenic also significantly reduced the protein expression of Sox 10, needed for neural crest progenitor cell production, by 31–50%, and downregulated the protein and mRNA levels of NeuroD1, needed for neural crest cell differentiation, in a time- and dose-dependent manner. While the overall protein expression of transcription factors in the skeletal muscle lineage was not changed, arsenic did alter their nuclear localization. MyoD nuclear translocation was significantly reduced on days 2–5 between 15 and 70%. At a 10-fold lower concentration, monomethylarsonous acid (MMA III) appeared to be just as potent as inorganic arsenic at reducing the mRNA levels Pax3 (79% vs84%), Sox10 (49% vs 65%), and Msx1 (56% vs 56%). Dimethylarsinous acid (DMA III) also reduced protein and transcript expression, but the changes were less dramatic than those with MMA or arsenite. All three arsenic species reduced the nuclear localization of MyoD and NeuroD1 in a similar manner. The early changes in the differentiation of neural plate border specifier cells may provide a mechanism for arsenic to suppress both neurogenesis and myogenesis

CCDC 1820835: Experimental Crystal Structure Determination

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.,Related Article: Rodrigo Castro-Ramírez, Naytzé Ortiz-Pastrana, Ana B. Caballero, Matthew T. Zimmerman, Bradley S. Stadelman, Andrea A. E. Gaertner, Julia L. Brumaghim, Luís Korrodi-Gregório, Ricardo Pérez-Tomás, Patrick Gamez, Norah Barba-Behrens|2018|Dalton Trans.|47|7551|doi:10.1039/C8DT00716