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Inside Cover: Anticancer Therapeutics That Target Selenoenzymes: Synthesis, Characterization, in vitro Cytotoxicity, and Thioredoxin Reductase Inhibition of a Series of Gold(I) Complexes Containing Hydrophilic Phosphine Ligands (ChemMedChem 1/2010)
Author(s) -
Vergara Elena,
Casini Angela,
Sorrentino Francesca,
Zava Olivier,
Cerrada Elena,
Rigobello Maria Pia,
Bindoli Alberto,
Laguna Mariano,
Dyson Paul J.
Publication year - 2010
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200990065
Subject(s) - thioredoxin reductase , chemistry , phosphine , cytotoxicity , dimer , protein data bank (rcsb pdb) , auranofin , combinatorial chemistry , enzyme , stereochemistry , thioredoxin , in vitro , biochemistry , organic chemistry , catalysis , biology , rheumatoid arthritis , immunology
The inside cover picture shows the X‐ray structure of human thioredoxin reductase dimer (TrxR; PDB: 2J3N; ribbon representation), with the catalytic site residues Sec and Cys highlighted (cyan surface). Enzyme activity assays and biochemical studies identified the Sec–Cys dyad as essential for TrxR inhibition by water‐soluble Au I –phosphine complexes. For more details, see the Full Paper by M. Laguna, P. J. Dyson, et al. on p. 96 ff.