• Publications
  • Influence
Structure of the ligand‐binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist
Oestrogens exert their physiological effects through two receptor subtypes. Here we report the three‐dimensional structure of the oestrogen receptor beta isoform (ERβ) ligand‐binding domain (LBD) inExpand
  • 920
  • 45
A serine protease triad forms the catalytic centre of a triacylglycerol lipase
TRUE Upases attack triacylglycerols and act at an oil–water interface; they constitute a ubiquitous group of enzymes catalysing a wide variety of reactions, many with industrial potential. But so farExpand
  • 724
  • 13
Structural insights into the mode of action of a pure antiestrogen.
BACKGROUND Estrogens exert their effects on target tissues by binding to a nuclear transcription factor termed the estrogen receptor (ER). Previous structural studies have demonstrated that eachExpand
  • 303
  • 13
How insulin engages its primary binding site on the insulin receptor
Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival. Insulin resistance contributes to the pathogenesisExpand
  • 240
  • 13
A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
LIPASES are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols. They have been classified as serine hydrolases owing to their inhibition by diethylExpand
  • 711
  • 12
Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 Å resolution
Laccase catalyses the oxidation of a variety of organic substrates coupled to the reduction of oxygen to water. It is widely believed to be the simplest representative of the ubiquitous blueExpand
  • 300
  • 11
X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
The three-dimensional structure of the Bacillus stearothermophilus "maltogenic" alpha-amylase, Novamyl, has been determined by X-ray crystallography at a resolution of 1.7 A. Unlike conventionalExpand
  • 108
  • 8
Clear strategy screens for macromolecular crystallization
The development of high-throughput crystallography combined with the wealth of already accumulated information about protein crystallization properties requires constant revision of currentExpand
  • 81
  • 8
Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase.
The already known X-ray structures of lipases provide little evidence about initial, discrete structural steps occurring in the first phases of their activation in the presence of lipids (processExpand
  • 178
  • 7
Structural characterization of human heparanase reveals insights into substrate recognition
Heparan sulfate (HS) is a glycosaminoglycan that forms a key component of the extracellular matrix (ECM). Breakdown of HS is carried out by heparanase (HPSE), an endo-β-glucuronidase of the glycosideExpand
  • 77
  • 6