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pro vyhledávání: '"Townsend-Nicholson A"'
Akademický článek
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Publikováno v:
Journal of personalized medicine. 12(10)
The G protein-coupled receptor (GPCR) Smoothened (Smo) is a central signal transducer of the Hedgehog (Hh) pathway which has been linked to diverse forms of tumours. Stimulated by advancements in structural and functional characterisation, the Smo re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8844aa9dc17c9eb7cbe7ccb7f0bf207f
https://pubmed.ncbi.nlm.nih.gov/36294790
https://pubmed.ncbi.nlm.nih.gov/36294790
Autor:
Stefania Monteleone, Dmitri G. Fedorov, Andrea Townsend-Nicholson, Michelle Southey, Michael Bodkin, Alexander Heifetz
Publikováno v:
Journal of chemical information and modeling. 62(16)
Protein-protein interactions (PPIs) are essential for the function of many proteins. Aberrant PPIs have the potential to lead to disease, making PPIs promising targets for drug discovery. There are over 64,000 PPIs in the human interactome reference
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::749e987fedc984e4013b9d707ddb6a9d
https://pubmed.ncbi.nlm.nih.gov/35939049
https://pubmed.ncbi.nlm.nih.gov/35939049
Akademický článek
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Akademický článek
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Publikováno v:
Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology. 50(5)
The final year of a biochemistry degree is usually a time to experience research. However, laboratory-based research projects were not possible during COVID-19. Instead, we used open datasets to provide computational research projects in metagenomics
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d8381b9451fac9bdcd0f62d38a3e398
https://pubmed.ncbi.nlm.nih.gov/35972192
https://pubmed.ncbi.nlm.nih.gov/35972192
Publikováno v:
Artificial Intelligence in Drug Design ISBN: 9781071617861
Drug-target residence time, the duration of binding at a given protein target, has been shown in some protein families to be more significant for conferring efficacy than binding affinity. To carry out efficient optimization of residence time in drug
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ae909e9bc2eb004d8dfb46df2ea6ac17
https://doi.org/10.1007/978-1-0716-1787-8_8
https://doi.org/10.1007/978-1-0716-1787-8_8
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2390
Drug-target residence time, the duration of binding at a given protein target, has been shown in some protein families to be more significant for conferring efficacy than binding affinity. To carry out efficient optimization of residence time in drug
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::482a84fb0fc8d8ec8525f9321cc09afc
https://pubmed.ncbi.nlm.nih.gov/34731470
https://pubmed.ncbi.nlm.nih.gov/34731470
Autor:
Tim James, Inaki Morao, Alexander Heifetz, Michelle Southey, Dmitri G. Fedorov, Michael J. Bodkin, Andrea Townsend-Nicholson, Peter V. Coveney, Kostas Papadopoulos
Publikováno v:
Recent Advances of the Fragment Molecular Orbital Method ISBN: 9789811592348
There has been a long history of fruitful cooperation between academia and the pharmaceutical industry, with the primary beneficiary of this interaction being, of course, the public. Since the middle of the last century, the drug discovery process ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3069b9b86aa98ae45522141208a01a85
https://doi.org/10.1007/978-981-15-9235-5_15
https://doi.org/10.1007/978-981-15-9235-5_15
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2114
Arrestin binding to G protein-coupled receptors (GPCRs) plays a vital role in receptor signaling. Recently, the crystal structure of rhodopsin bound to activated visual arrestin was resolved using XFEL (X-ray free electron laser). However, even with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a2ca74a5e9d15eb30ca61815c9828b14
https://pubmed.ncbi.nlm.nih.gov/32016894
https://pubmed.ncbi.nlm.nih.gov/32016894