John W.R. Schwabe

TL;DR: These findings represent the first germline loss-of-function mutations in PPARγ and provide compelling genetic evidence that this receptor is important in the control of insulin sensitivity, glucose homeostasis and blood pressure in man.

TL;DR: The crystal structure of the fully specific complex between the DNA-binding domain from the estrogen receptor and DNA reveals how the protein recognizes its own half site sequence rather than that of the related glucocorticoid receptor, which differs by only two base pairs.

TL;DR: The term zinc finger was first used to describe a 30‐residue, repeated sequence motif found in an unusually abundant Xenopus transcription factor and it was proposed that each motif is folded around a central zinc ion to form an independent minidomain and that adjacent zinc fingers are combined as modules to make up a DNA‐binding domain with the modules “gripping” the DNA.

TL;DR: The structure of the DNA-binding domain from the oestrogen receptor, as determined by two-dimensional 1H NMR techniques, seems to be a general structure for protein-DNA recognition.

TL;DR: The identity of complementary acting signature motifs in SMRT and N-CoR that are sufficient for receptor binding and ligand-induced release are reported and indicate a direct mechanistic link between activation and repression via competition for a common or at least partially overlapping binding site.