Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Nicholas J. Cundy"'
Autor:
Eric W. J. Gates, Nicholas D. Calvert, Nicholas J. Cundy, Federica Brugnoli, Pauline Navals, Alexia Kirby, Nicoletta Bianchi, Gautam Adhikary, Adam J. Shuhendler, Richard L. Eckert, Jeffrey W. Keillor
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 16, p 12546 (2023)
Transglutaminase 2 (TG2) is a multifunctional enzyme primarily responsible for crosslinking proteins. Ubiquitously expressed in humans, TG2 can act either as a transamidase by crosslinking two substrates through formation of an Nε(ɣ-glutaminyl)lysi
Externí odkaz:
https://doaj.org/article/cc08aac5a3ef4e499a2f325c29def26c
Autor:
Nicholas J. Cundy, Jane Arciszewski, Eric W. J. Gates, Sydney L. Acton, Kyle D. Passley, Ernest Awoonor-Williams, Elizabeth K. Boyd, Nancy Xu, Élise Pierson, Catalina Fernandez-Ansieta, Marie R. Albert, Nicole M. R. McNeil, Gautam Adhikary, Richard L. Eckert, Jeffrey W. Keillor
Publikováno v:
RSC Medicinal Chemistry. 14:378-385
A novel peptidic scaffold was used to design a library of inhibitors that exhibit exceptional efficiency against tissue transglutaminase, providing a framework for the development of potent research tools.
Autor:
Nicole M.R. McNeil, Eric W.J. Gates, Neda Firoozi, Nicholas J. Cundy, Jessica Leccese, Sarah Eisinga, Joel D.A. Tyndall, Gautam Adhikary, Richard L. Eckert, Jeffrey W. Keillor
Publikováno v:
European journal of medicinal chemistry. 232
Tissue transglutaminase (TG2) is a multifunctional protein that catalyses protein crosslinking in the extracellular matrix, and functions as an intracellular G-protein. While both activities have been associated with human diseases, its role as a G-p
Autor:
Emma Lloyd Raven, Richard S. Grainger, John Gordon, Omar S. Qureshi, Thomas A. Jowitt, Catherine A. Brady, Nicholas J. Cundy, Nicholas M. Barnes, Roseanna K. Hare, Andrew G. Leach, Sam Butterworth, Tina Tang
Publikováno v:
RSC Chemical Biology
Cundy, N J, Hare, R K, Tang, T, Leach, A G, Jowitt, T A, Qureshi, O, Gordon, J, Barnes, N M, Brady, C A, Raven, E L, Grainger, R S & Butterworth, S 2021, ' Design, synthesis and evaluation of tryptophan analogues as tool compounds to study IDO1 activity ', RSC Chemical Biology . https://doi.org/10.1039/D0CB00209G
Cundy, N J, Hare, R K, Tang, T, Leach, A G, Jowitt, T A, Qureshi, O, Gordon, J, Barnes, N M, Brady, C A, Raven, E L, Grainger, R S & Butterworth, S 2021, ' Design, synthesis and evaluation of tryptophan analogues as tool compounds to study IDO1 activity ', RSC Chemical Biology . https://doi.org/10.1039/D0CB00209G
The metabolism of l-tryptophan to N-formyl-l-kynurenine by indoleamine-2,3-dioxygenase 1 (IDO1) is thought to play a critical role in tumour-mediated immune suppression. Whilst there has been significant progress in elucidating the overall enzymatic
Autor:
Alice Lanne, Yixin Cui, Edward Browne, Philip G. E. Craven, Nicholas J. Cundy, Nicholas J. Coltman, Katie Dale, Antonio Feula, Jon Frampton, Aaron Goff, Mariwan A. Hama Salih, Xingfen Lang, Xingjian Li, Christopher W. Moon, Michael Morton, Jordan Pascoe, Xudan Peng, Vanessa Portman, Cara Press, Timothy Schulz-Utermoehl, Micky Tortorella, Zhengchao Tu, Zoe E. Underwood, Changwei Wang, Akina Yoshizawa, Tianyu Zhang, Simon J Waddell, Joanna Bacon, Cleopatra Neagoie, John S. Fossey, Luke J. Alderwick.
Tuberculosis (TB) is the leading cause of global morbidity and mortality resulting from infectious disease, with over 10 million new cases and 1.5 million deaths in 2019. This global emergency is exacerbated by the emergence of multi-drug-resistant M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::66e23350ab3888c21d9c850dce9078a6
https://doi.org/10.1101/2020.09.03.281170
https://doi.org/10.1101/2020.09.03.281170