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Shuhei Yamaguchi,Nobuhiro Yamaguchi,Masaki Mito,Hiroyuki Deguchi,Peter. J. Baker,Stephen. J. Blundell,Michael. J. Pitcher,Dinah. R. Parker,Simon. J. Clarke 한국물리학회 2013 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.63 No.3
The pressure effects on the 111-type Fe-based superconductor LiFeAs were investigated throughAC susceptibility measurements and X-ray diffraction experiments, and revealed a correlation betweenthe superconducting transition temperature (Tc) and the As-Fe-As bond angle (α) ratherthan the height of As from the Fe layers (hAs). As the pressure was increased, Tc of 17 K at P =0 GPa decreased down to 10 K at P = 5.2 GPa. According to a previous report from an X-raydiffraction experiment, α changes from 101.5˚ at 0 GPa to 97.8˚ at 17 GPa. The obtained changein Tc is consistent with Lee et al.’s plot of Tc as a function of α, and from this result, we concludethat Tc will fall to zero at around α = 98˚.
Characterization of AJH-836, a diacylglycerol-lactone with selectivity for novel PKC isozymes
Cooke, Mariana,Zhou, Xiaoling,Casado-Medrano, Victoria,Lopez-Haber, Cynthia,Baker, Martin J.,Garg, Rachana,Ann, Jihyae,Lee, Jeewoo,Blumberg, Peter M.,Kazanietz, Marcelo G. American Society for Biochemistry and Molecular Bi 2018 The Journal of biological chemistry Vol.293 No.22
<P>Diacylglycerol (DAG) is a key lipid second messenger downstream of cellular receptors that binds to the C1 domain in many regulatory proteins. Protein kinase C (PKC) isoforms constitute the most prominent family of signaling proteins with DAG-responsive C1 domains, but six other families of proteins, including the chimaerins, Ras-guanyl nucleotide-releasing proteins (RasGRPs), and Munc13 isoforms, also play important roles. Their significant involvement in cancer, immunology, and neurobiology has driven intense interest in the C1 domain as a therapeutic target. As with other classes of targets, however, a key issue is the establishment of selectivity. Here, using [H-3]phorbol 12,13-dibutyrate ([H-3]PDBu) competition binding assays, we found that a synthetic DAG-lactone, AJH-836, preferentially binds to the novel PKC isoforms PKC and PKCE relative to classical PKC and PKCII. Assessment of intracellular translocation, a hallmark for PKC activation, revealed that AJH-836 treatment stimulated a striking preferential redistribution of PKCE to the plasma membrane relative to PKC. Moreover, unlike with the prototypical phorbol ester phorbol 12-myristate 13-acetate (PMA), prolonged exposure of cells to AJH-836 selectively down-regulated PKC and PKCE without affecting PKC expression levels. Biologically, AJH-836 induced major changes in cytoskeletal reorganization in lung cancer cells, as determined by the formation of membrane ruffles, via activation of novel PKCs. We conclude that AJH-836 represents a C1 domain ligand with PKC-activating properties distinct from those of natural DAGs and phorbol esters. Our study supports the feasibility of generating selective C1 domain ligands that promote novel biological response patterns.</P>