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A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis

Martin Gill Orcid Logo, Paul J. Jarman, Vanessa Hearnden, Simon D Fairbanks, Marcella Bassetto, Hannes Maib, John Palmer, Kathryn R. Ayscough, Jim A. Thomas Orcid Logo, Carl Smythe

Angewandte Chemie International Edition, Volume: 61, Issue: 27, Start page: e202117449

Swansea University Authors: Martin Gill Orcid Logo, Marcella Bassetto

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DOI (Published version): 10.1002/anie.202117449

Abstract

The dinuclear RuII complex [(Ru(phen)2)2(tpphz)]4+ binds to G-actin monomers, preventing assembly into F-actin. This inhibits actin fibre assemblies within live cells and causes disruption to late cytokinesis by interfering with the function of endosomal sorting complexes required for transport (ESC...

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Published in: Angewandte Chemie International Edition
ISSN: 1433-7851 1521-3773
Published: Wiley 2022
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URI: https://cronfa.swan.ac.uk/Record/cronfa59895
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first_indexed 2022-04-21T15:18:37Z
last_indexed 2023-01-11T14:41:29Z
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spelling 2022-10-28T15:17:32.2713333 v2 59895 2022-04-21 A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis 485d85b532851e8863cd19c6af7e00f7 0000-0002-1371-5676 Martin Gill Martin Gill true false b97beeed16f8e0524551233ade909565 Marcella Bassetto Marcella Bassetto true false 2022-04-21 CHEM The dinuclear RuII complex [(Ru(phen)2)2(tpphz)]4+ binds to G-actin monomers, preventing assembly into F-actin. This inhibits actin fibre assemblies within live cells and causes disruption to late cytokinesis by interfering with the function of endosomal sorting complexes required for transport (ESCRT) during abscission. These results reveal new possibilities for metal complexes as biomedical tools and novel therapeutic leads. Journal Article Angewandte Chemie International Edition 61 27 e202117449 Wiley 1433-7851 1521-3773 Actin ;Cytokinesis; Cytoskeleton; Polypyridyl Complexes; Ruthenium 4 7 2022 2022-07-04 10.1002/anie.202117449 COLLEGE NANME Chemistry COLLEGE CODE CHEM Swansea University Another institution paid the OA fee Medical Research Council. Grant Number: R/162348 2022-10-28T15:17:32.2713333 2022-04-21T16:10:35.9796169 Faculty of Science and Engineering School of Engineering and Applied Sciences - Chemistry Martin Gill 0000-0002-1371-5676 1 Paul J. Jarman 2 Vanessa Hearnden 3 Simon D Fairbanks 4 Marcella Bassetto 5 Hannes Maib 6 John Palmer 7 Kathryn R. Ayscough 8 Jim A. Thomas 0000-0002-8662-7917 9 Carl Smythe 10 59895__23984__97af1914ed264c37ac7d8fc790a04220.pdf 59895.pdf 2022-05-05T09:44:17.3153525 Output 1230440 application/pdf Version of Record true © 2022 The Authors. This is an open access article under the terms of the Creative Commons Attribution License true eng http://creativecommons.org/licenses/by/4.0/
title A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis
spellingShingle A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis
Martin Gill
Marcella Bassetto
title_short A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis
title_full A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis
title_fullStr A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis
title_full_unstemmed A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis
title_sort A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis
author_id_str_mv 485d85b532851e8863cd19c6af7e00f7
b97beeed16f8e0524551233ade909565
author_id_fullname_str_mv 485d85b532851e8863cd19c6af7e00f7_***_Martin Gill
b97beeed16f8e0524551233ade909565_***_Marcella Bassetto
author Martin Gill
Marcella Bassetto
author2 Martin Gill
Paul J. Jarman
Vanessa Hearnden
Simon D Fairbanks
Marcella Bassetto
Hannes Maib
John Palmer
Kathryn R. Ayscough
Jim A. Thomas
Carl Smythe
format Journal article
container_title Angewandte Chemie International Edition
container_volume 61
container_issue 27
container_start_page e202117449
publishDate 2022
institution Swansea University
issn 1433-7851
1521-3773
doi_str_mv 10.1002/anie.202117449
publisher Wiley
college_str Faculty of Science and Engineering
hierarchytype
hierarchy_top_id facultyofscienceandengineering
hierarchy_top_title Faculty of Science and Engineering
hierarchy_parent_id facultyofscienceandengineering
hierarchy_parent_title Faculty of Science and Engineering
department_str School of Engineering and Applied Sciences - Chemistry{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Engineering and Applied Sciences - Chemistry
document_store_str 1
active_str 0
description The dinuclear RuII complex [(Ru(phen)2)2(tpphz)]4+ binds to G-actin monomers, preventing assembly into F-actin. This inhibits actin fibre assemblies within live cells and causes disruption to late cytokinesis by interfering with the function of endosomal sorting complexes required for transport (ESCRT) during abscission. These results reveal new possibilities for metal complexes as biomedical tools and novel therapeutic leads.
published_date 2022-07-04T04:17:33Z
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score 11.035634

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