...), and that the α1 helix in the β subunit I domain is the key element affected by allosteric modulators. The data suggest an explanation for the limited clinical efficacy of RGD-based integrin antagonists, and we propose that allosteric antagonists could prove to be of greater therapeutic benefit. 1 To whom...

... malignancy. Thus antagonists that inhibit ephrin binding to EphA4 could be useful for a variety of research and therapeutic applications. In the present study we characterize the binding features of three antagonistic peptides (KYL, APY and VTM) that selectively target EphA4 among the Eph receptors...

... functions. However, limitations of existing ErbB4 agonists and antagonists have led us to seek novel ErbB4 antagonists. The Q43L mutant of the ErbB4 agonist NRG2β (neuregulin 2β) stimulates ErbB4 tyrosine phosphorylation, yet fails to stimulate ErbB4 coupling to cell proliferation. Thus in the present paper...

...A. Paul Mould; Ewa J. Koper; Adam Byron; Grit Zahn; Martin J. Humphries Integrin α5β1 is a key receptor for the extracellular matrix protein fibronectin. Antagonists of human integrin α5β1 have therapeutic potential as anti-angiogenic agents in cancer and diseases of the eye. However, the structure...

.... These findings demonstrate that fatty-acyl-CoAs have a novel function in the signalling pathways of PPARα and PPARγ. antagonist lipid metabolism nuclear receptor Biochem. J. (2001) 353, 231 238 (Printed in Great Britain) 231 Fatty-acyl-CoA thioesters inhibit recruitment of steroid receptor co-activator 1...

...Norio MATSUSHIMA; Nobuhiro HAYASHI; Yuji JINBO; Yoshinobu IZUMI Small-angle X-ray scattering (SAXS), which determines the radius of gyration, R g , and the pair distance distribution function, was used to investigate the conformational changes of calmodulin (CaM) on binding to an antagonist...