Zobrazeno 1 - 10
of 148
pro vyhledávání: '"D. Bayle"'
Autor:
Benjamin N. Atkinson, Fredrik Svensson, Hannah Woodward, Paul Whiting, Elliott D. Bayle, Paul V. Fish, Nicky J. Willis, Jean-Paul Vincent, David Steadman
Publikováno v:
Journal of Medicinal Chemistry
Regulation of the Wnt signaling pathway is critically important for a number of cellular processes in both development and adult mammalian biology. This Perspective will provide a summary of current and emerging therapeutic opportunities in modulatin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1daca6a8ed39142ac3fc8a7145d74588
https://doi.org/10.1021/acs.jmedchem.0c01974
https://doi.org/10.1021/acs.jmedchem.0c01974
Autor:
John Skidmore, Jonathan H. Clarke, Elliott D. Bayle, Tashfina Mirza, Stephen P. Andrews, Henriëtte M. G. Willems, Duncan Scott, Timothy P. C. Rooney
Publikováno v:
ACS Med Chem Lett
[Image: see text] Bifunctional molecules known as PROTACs simultaneously bind an E3 ligase and a protein of interest to direct ubiquitination and clearance of that protein, and they have emerged in the past decade as an exciting new paradigm in drug
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33edb481bdf8562badf0dddd3f1ab838
https://doi.org/10.1021/acsmedchemlett.0c00194
https://doi.org/10.1021/acsmedchemlett.0c00194
Autor:
Nicky J. Willis, William Mahy, James Sipthorp, Yuguang Zhao, Hannah L. Woodward, Benjamin N. Atkinson, Elliott D. Bayle, Fredrik Svensson, Sarah Frew, Fiona Jeganathan, Amy Monaghan, Stefano Benvegnù, Sarah Jolly, Luca Vecchia, Reinis R. Ruza, Svend Kjær, Steven Howell, Ambrosius P. Snijders, Magda Bictash, Patricia C. Salinas, Jean-Paul Vincent, E. Yvonne Jones, Paul Whiting, Paul V. Fish
Notum is a carboxylesterase that suppresses Wnt signaling through deacylation of an essential palmitoleate group on Wnt proteins. There is a growing understanding of the role Notum plays in human diseases such as colorectal cancer and Alzheimer's dis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3474b8ac04a0b606e41a67edadf62c69
Autor:
Yuguang Zhao, William Mahy, Nicky J. Willis, Hannah L. Woodward, David Steadman, Elliott D. Bayle, Benjamin N. Atkinson, James Sipthorp, Luca Vecchia, Reinis R. Ruza, Karl Harlos, Fiona Jeganathan, Stefan Constantinou, Artur Costa, Svend Kjær, Magda Bictash, Patricia C. Salinas, Paul Whiting, Jean-Paul Vincent, Paul V. Fish, E. Yvonne Jones
The Wnt signaling suppressor Notum is a promising target for osteoporosis, Alzheimer's disease, and colorectal cancers. To develop novel Notum inhibitors, we used an X-ray crystallographic fragment screen with the Diamond-SGC Poised Library (DSPL) an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f547dc38fab64d9f08bf48b45b75fa9e
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
George Papageorgiou, Paul V. Fish, Elliott D. Bayle, David Steadman, Benjamin N. Atkinson, Nicky J. Willis, William Mahy
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 15, Iss 1, Pp 2790-2797 (2019)
Beilstein Journal of Organic Chemistry
Beilstein Journal of Organic Chemistry
Background: The carboxylesterase Notum has been shown to act as a key negative regulator of the Wnt signalling pathway by mediating the depalmitoleoylation of Wnt proteins. LP-922056 (1) is an orally active inhibitor of Notum. We are investigating th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac8d0fd0c21aef274fede3dc203ef510
https://doi.org/10.3762/bxiv.2019.70.v1
https://doi.org/10.3762/bxiv.2019.70.v1
Publikováno v:
Br J Pharmacol
The production, quality control, and degradation of proteins are a tightly controlled process necessary for cell health. In order to regulate this process, cells rely upon a network of molecular chaperone proteins that bind misfolded proteins and hel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6159754673d1373d5537f60dce676ea9
https://europepmc.org/articles/PMC6715599/
https://europepmc.org/articles/PMC6715599/
Autor:
James Sipthorp, Magda Bictash, Elliott D. Bayle, William Mahy, Fredrik Svensson, George Papageorgiou, Paul V. Fish, E Y Jones, Yuguang Zhao, F. Jeganathan, Benjamin N. Atkinson, David Steadman, Amy Monaghan, S. Frew
Publikováno v:
Bioorganic & Medicinal Chemistry Letters
Graphical abstract
The carboxylesterase Notum is a key negative regulator of the Wnt signaling pathway by mediating the depalmitoleoylation of Wnt proteins. Our objective was to discover potent small molecule inhibitors of Notum suitable for exp
The carboxylesterase Notum is a key negative regulator of the Wnt signaling pathway by mediating the depalmitoleoylation of Wnt proteins. Our objective was to discover potent small molecule inhibitors of Notum suitable for exp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c37351142a9785d9a076a4742c580520
https://doi.org/10.1016/j.bmcl.2019.126751
https://doi.org/10.1016/j.bmcl.2019.126751
Publikováno v:
Organic Syntheses
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab79f0a4e2b03b0873dba2b16fb56e33
https://doi.org/10.1002/0471264229.os094.15
https://doi.org/10.1002/0471264229.os094.15
Autor:
Elliott D. Bayle, Niall Igoe, Cynthia Tallant, Paul Brennan, Pavel Savitsky, Danen Cunoosamy, Oleg Fedorov, David M. Andrews, Susanne Müller, Julia Meier, Sarah Scholze, Catherine Rogers, Stefan Knapp, Yannick Morias, Anne Cheasty, Helen Boyd, Paul V. Fish
Publikováno v:
Journal of Medicinal Chemistry. 60(16)
The bromodomain and plant homeodomain finger-containing (BRPF) family are scaffolding proteins important for the recruitment of histone acetyltransferases of the MYST family to chromatin. Here, we describe NI-57 (16) as new pan-BRPF chemical probe of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3496ca11f99fd1595709e72ac3c381a
http://ora.ox.ac.uk/objects/uuid:
http://ora.ox.ac.uk/objects/uuid: