Articles | Volume 2, issue 2
https://doi.org/10.5194/mr-2-629-2021
https://doi.org/10.5194/mr-2-629-2021
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

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Interactive discussion

Status: closed

Comment types: AC – author | RC – referee | CC – community | EC – editor | CEC – chief editor | : Report abuse
  • RC1: 'Comment on mr-2021-7', Walter Chazin, 23 Feb 2021
    • AC1: 'Reply on RC1', Jonathan Waltho, 23 Feb 2021
  • RC2: 'Comment on mr-2021-7', Anonymous Referee #2, 04 Mar 2021
    • AC2: 'Reply on RC2', Jonathan Waltho, 19 Mar 2021

Peer review completion

AR: Author's response | RR: Referee report | ED: Editor decision
AR by Jonathan Waltho on behalf of the Authors (19 Mar 2021)  Author's response    Author's tracked changes    Manuscript
ED: Publish subject to minor revisions (review by editor) (22 Mar 2021) by Sebastian Hiller
AR by Jonathan Waltho on behalf of the Authors (29 Mar 2021)  Author's response    Author's tracked changes    Manuscript
ED: Publish as is (03 Apr 2021) by Sebastian Hiller
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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.