Zobrazeno 1 - 10
of 573
pro vyhledávání: '"Alan R, Fersht"'
Publikováno v:
Protein Sci
The Rel proteins of the NF-κB complex comprise one of the most investigated transcription factor families, forming a variety of hetero- or homodimers. Nevertheless, very little is known about the fundamental kinetics of NF-κB complex assembly, or t
Autor:
Giovanni Settanni, Rhiannon N. Jones, John Spencer, Raysa Khan Tareque, Andreas Krämer, Andreas C. Joerger, Xiaomin Ni, Alan R. Fersht, Matthias R. Bauer
Publikováno v:
ACS Chemical Biology
We have previously shown that the thermolabile, cavity-creating p53 cancer mutant Y220C can be reactivated by small-molecule stabilizers. In our ongoing efforts to unearth druggable variants of the p53 mutome, we have now analyzed the effects of othe
Autor:
Alexandr Nasedkin, Moreno Marcellini, Tomasz L Religa, Stefan M Freund, Andreas Menzel, Alan R Fersht, Per Jemth, David van der Spoel, Jan Davidsson
Publikováno v:
PLoS ONE, Vol 10, Iss 5, p e0125662 (2015)
The folding and unfolding of protein domains is an apparently cooperative process, but transient intermediates have been detected in some cases. Such (un)folding intermediates are challenging to investigate structurally as they are typically not long
Externí odkaz:
https://doaj.org/article/0c69037db4244bb1b1a87aca2faf107d
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e47889 (2012)
Most proteins have not evolved for maximal thermal stability. Some are only marginally stable, as for example, the DNA-binding domains of p53 and its homologs, whose kinetic and thermodynamic stabilities are strongly correlated. Here, we applied high
Externí odkaz:
https://doaj.org/article/106edf49e9e24e7ea443bfe3b492e26a
Autor:
William M. Gallagher, Stephen F. Madden, Darran P. O'Connor, Norma O'Donovan, Matthias R. Bauer, Alan R. Fersht, John Crown, Naoise C Synnott, Michael J. Duffy, Alyson Murray, Rut Klinger
Publikováno v:
Cancer Letters. 414:99-106
The identification of a targeted therapy for patients with triple-negative breast cancer (TNBC) is one of the most urgent needs in breast cancer therapeutics. The p53 gene is mutated in approximately 80% of patients with TNBC, and is a potential ther
Autor:
D. Horil Roy, Alan R. Fersht, Matthias G. J. Baud, Andreas C. Joerger, Matthias R. Bauer, Ketan J. Patel, Felix A. Dingler, L. Verduci
Publikováno v:
European Journal of Medicinal Chemistry
Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the development of novel anticancer therapeutics. The oncogenic p53 mutation Y220C, which accounts for
Autor:
Alan R. Fersht
Publikováno v:
Journal of Molecular Biology. 433:167088
I outline how over my career as a protein scientist Machine Learning has impacted my area of science and one of my pastimes, chess, where there are some interesting parallels. In 1968, modelling of three-dimensional structures was initiated based on
Autor:
Andreas C. Joerger, Bradley Springett, Alan R. Fersht, Felix A. Dingler, Lorena Verduci, Matthias R. Bauer, Ketan J. Patel, Rhiannon N. Jones, John Spencer, Raysa Khan Tareque
Publikováno v:
Future Medicinal Chemistry
Future Med Chem
Future Med Chem
Aim: The p53 cancer mutation Y220C creates a conformationally unstable protein with a unique elongated\ud surface crevice that can be targeted by molecular chaperones. We report the structure-guided optimization\ud of the carbazole-based stabilizer P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d6730cd1f62e5fc2066d75c60511b9f
Autor:
Alessandra Bisio, Bartolomeo Bosco, Helena Ramos, Flávio Reis, Carla Cristina Marques de Oliveira, Alberto Inga, Maria Inês Almeida, Célia Gomes, Silvano Piazza, Maria M. M. Santos, Lucília Domingues, Lucília Saraiva, Liliana Raimundo, Matthias R. Bauer, Alan R. Fersht, Sara Gomes, Joana Soares, Nair Nazareth, Joao Paulo Bras, Joana B. Loureiro, Valentina Barcherini
Publikováno v:
Cancers, Vol 11, Iss 8, p 1151 (2019)
Cancers
Cancers; Volume 11; Issue 8; Pages: 1151
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Cancers
Cancers; Volume 11; Issue 8; Pages: 1151
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Half of human cancers harbor TP53 mutations that render p53 inactive as a tumor suppressor. In these cancers, reactivation of mutant p53 (mutp53) through restoration of wild-type-like function constitutes a valuable anticancer therapeutic strategy. I
Publikováno v:
Protein Engineering Design and Selection. 29:377-390
The p53 tumor suppressor protein performs a critical role in stimulating apoptosis and cell cycle arrest in response to oncogenic stress. The function of p53 can be compromised by mutation, leading to increased risk of cancer; approximately 50% of ca