Articles | Volume 2, issue 2
Research article
13 Aug 2021
Research article |  | 13 Aug 2021

High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulin

Lilia Milanesi, Clare R. Trevitt, Brian Whitehead, Andrea M. Hounslow, Salvador Tomas, Laszlo L. P. Hosszu, Christopher A. Hunter, and Jonathan P. Waltho


Total article views: 1,484 (including HTML, PDF, and XML)
HTML PDF XML Total Supplement BibTeX EndNote
828 593 63 1,484 226 47 36
  • HTML: 828
  • PDF: 593
  • XML: 63
  • Total: 1,484
  • Supplement: 226
  • BibTeX: 47
  • EndNote: 36
Views and downloads (calculated since 05 Feb 2021)
Cumulative views and downloads (calculated since 05 Feb 2021)

Viewed (geographical distribution)

Total article views: 1,484 (including HTML, PDF, and XML) Thereof 1,330 with geography defined and 154 with unknown origin.
Country # Views %
  • 1


Latest update: 28 Sep 2023
Short summary
The overall aim of the study is to provide a basis from which to improve the ability of tamoxifen family drugs to reduce the activity of a secondary target protein, calmodulin, during tumour development. The main conclusion is that the binding of a tamoxifen analogue is quite unlike that of other anti-calmodulin compounds in that two drug molecules bring the two domains of calmodulin into close proximity, but they are not fixed in orientation relative to the protein.