Highly selective inhibition of histone demethylases by de novo macrocyclic peptides

JmjC histone demethylases (KDMs) are cancer targets due to their links to cell proliferation, but selective inhibition remains a challenge. Here the authors identify potent inhibitors of KDM4A-C—viain vitroselection from a vast library of cyclic peptides—that show selectivity over other KDMs.

Guardado en:
Detalles Bibliográficos
Autores principales: Akane Kawamura, Martin Münzel, Tatsuya Kojima, Clarence Yapp, Bhaskar Bhushan, Yuki Goto, Anthony Tumber, Takayuki Katoh, Oliver N. F. King, Toby Passioura, Louise J. Walport, Stephanie B. Hatch, Sarah Madden, Susanne Müller, Paul E. Brennan, Rasheduzzaman Chowdhury, Richard J. Hopkinson, Hiroaki Suga, Christopher J. Schofield
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
Materias:
Q
Acceso en línea:https://doaj.org/article/ef8ec2f09725496691198a2fa7af4d88
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:ef8ec2f09725496691198a2fa7af4d88
record_format dspace
spelling oai:doaj.org-article:ef8ec2f09725496691198a2fa7af4d882021-12-02T14:42:05ZHighly selective inhibition of histone demethylases by de novo macrocyclic peptides10.1038/ncomms147732041-1723https://doaj.org/article/ef8ec2f09725496691198a2fa7af4d882017-04-01T00:00:00Zhttps://doi.org/10.1038/ncomms14773https://doaj.org/toc/2041-1723JmjC histone demethylases (KDMs) are cancer targets due to their links to cell proliferation, but selective inhibition remains a challenge. Here the authors identify potent inhibitors of KDM4A-C—viain vitroselection from a vast library of cyclic peptides—that show selectivity over other KDMs.Akane KawamuraMartin MünzelTatsuya KojimaClarence YappBhaskar BhushanYuki GotoAnthony TumberTakayuki KatohOliver N. F. KingToby PassiouraLouise J. WalportStephanie B. HatchSarah MaddenSusanne MüllerPaul E. BrennanRasheduzzaman ChowdhuryRichard J. HopkinsonHiroaki SugaChristopher J. SchofieldNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Akane Kawamura
Martin Münzel
Tatsuya Kojima
Clarence Yapp
Bhaskar Bhushan
Yuki Goto
Anthony Tumber
Takayuki Katoh
Oliver N. F. King
Toby Passioura
Louise J. Walport
Stephanie B. Hatch
Sarah Madden
Susanne Müller
Paul E. Brennan
Rasheduzzaman Chowdhury
Richard J. Hopkinson
Hiroaki Suga
Christopher J. Schofield
Highly selective inhibition of histone demethylases by de novo macrocyclic peptides
description JmjC histone demethylases (KDMs) are cancer targets due to their links to cell proliferation, but selective inhibition remains a challenge. Here the authors identify potent inhibitors of KDM4A-C—viain vitroselection from a vast library of cyclic peptides—that show selectivity over other KDMs.
format article
author Akane Kawamura
Martin Münzel
Tatsuya Kojima
Clarence Yapp
Bhaskar Bhushan
Yuki Goto
Anthony Tumber
Takayuki Katoh
Oliver N. F. King
Toby Passioura
Louise J. Walport
Stephanie B. Hatch
Sarah Madden
Susanne Müller
Paul E. Brennan
Rasheduzzaman Chowdhury
Richard J. Hopkinson
Hiroaki Suga
Christopher J. Schofield
author_facet Akane Kawamura
Martin Münzel
Tatsuya Kojima
Clarence Yapp
Bhaskar Bhushan
Yuki Goto
Anthony Tumber
Takayuki Katoh
Oliver N. F. King
Toby Passioura
Louise J. Walport
Stephanie B. Hatch
Sarah Madden
Susanne Müller
Paul E. Brennan
Rasheduzzaman Chowdhury
Richard J. Hopkinson
Hiroaki Suga
Christopher J. Schofield
author_sort Akane Kawamura
title Highly selective inhibition of histone demethylases by de novo macrocyclic peptides
title_short Highly selective inhibition of histone demethylases by de novo macrocyclic peptides
title_full Highly selective inhibition of histone demethylases by de novo macrocyclic peptides
title_fullStr Highly selective inhibition of histone demethylases by de novo macrocyclic peptides
title_full_unstemmed Highly selective inhibition of histone demethylases by de novo macrocyclic peptides
title_sort highly selective inhibition of histone demethylases by de novo macrocyclic peptides
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/ef8ec2f09725496691198a2fa7af4d88
work_keys_str_mv AT akanekawamura highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT martinmunzel highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT tatsuyakojima highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT clarenceyapp highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT bhaskarbhushan highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT yukigoto highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT anthonytumber highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT takayukikatoh highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT olivernfking highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT tobypassioura highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT louisejwalport highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT stephaniebhatch highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT sarahmadden highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT susannemuller highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT paulebrennan highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT rasheduzzamanchowdhury highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT richardjhopkinson highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT hiroakisuga highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
AT christopherjschofield highlyselectiveinhibitionofhistonedemethylasesbydenovomacrocyclicpeptides
_version_ 1718389845464711168