Zobrazeno 1 - 10
of 105
pro vyhledávání: '"William M, Dawson"'
Autor:
William M. Dawson, Kathryn L. Shelley, Jordan M. Fletcher, D. Arne Scott, Lucia Lombardi, Guto G. Rhys, Tania J. LaGambina, Ulrike Obst, Antony J. Burton, Jessica A. Cross, George Davies, Freddie J. O. Martin, Francis J. Wiseman, R. Leo Brady, David Tew, Christopher W. Wood, Derek N. Woolfson
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Differential sensing aims to mimic senses such as taste and smell through the use of synthetic receptors. Here, the authors show that arrays of de novo designed peptide assemblies can be used as sensor components to distinguish various analytes and c
Externí odkaz:
https://doaj.org/article/a820f403adc549ffa2b3bf2e841354ca
Autor:
William M. Dawson, Eric J. M. Lang, Guto G. Rhys, Kathryn L. Shelley, Christopher Williams, R. Leo Brady, Matthew P. Crump, Adrian J. Mulholland, Derek N. Woolfson
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
So far most of the de novo designed proteins are for single states only. Here, the authors present the de novo design and crystal structure determination of a coiled-coil peptide that assembles into multiple, distinct conformational states under the
Externí odkaz:
https://doaj.org/article/da6fbe49cbb74470820dc44739bd5079
Autor:
Guto G. Rhys, Jessica A. Cross, William M. Dawson, Harry F. Thompson, Sooruban Shanmugaratnam, Nigel J. Savery, Mark P. Dodding, Birte Höcker, Derek N. Woolfson
Publikováno v:
Rhys, G G, Cross, J A, Dawson, W M, Thompson, H F, Shanmugaratnam, S, Savery, N J, Dodding, M P, Höcker, B & Woolfson, D N 2022, ' De novo designed peptides for cellular delivery and subcellular localisation ', Nature Chemical Biology, vol. 18, no. 9, pp. 999-1004 . https://doi.org/10.1038/s41589-022-01076-6
Nature Chemical Biology
Nature Chemical Biology
Increasingly, it is possible to design peptide and protein assemblies de novo from first principles or computationally. This approach provides new routes to functional synthetic polypeptides, including designs to target and bind proteins of interest.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2b0851f64b0b8cc4cf7ea344139af74
https://doi.org/10.1038/s41589-022-01076-6
https://doi.org/10.1038/s41589-022-01076-6
Autor:
Kozhinjampara R. Mahendran, William M. Dawson, Mark I. Wallace, Jason T. Sengel, Adrian J. Mulholland, William F. DeGrado, Hagan Bayley, Lijun Liu, R. Leo Brady, Eric J. M. Lang, Ai Niitsu, Alistair J. Scott, Derek N. Woolfson, Marco Mravic, Andrew R. Thomson, Huong T. Kratochvil
Publikováno v:
Scott, A J, Niitsu, A, Lang, E J M, Dawson, W M, Brady, R L, Mulholland, A J & Woolfson, D N 2021, ' Constructing ion channels from water-soluble α-helical barrels ', Nature Chemistry, vol. 13, no. 7, pp. 643-650 . https://doi.org/10.1038/s41557-021-00688-0
The design of peptides that assemble in membranes to form functional ion channels is challenging. Specifically, hydrophobic interactions must be designed between the peptides and at the peptide–lipid interfaces simultaneously. Here, we take a multi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37756b89f736b22f8a11bd297b48bcde
https://doi.org/10.1038/s41557-021-00688-0
https://doi.org/10.1038/s41557-021-00688-0
Autor:
Guto G. Rhys, William M. Dawson, Derek N. Woolfson, Freddie J. O. Martin, R. Leo Brady, Kathryn L Shelley
Publikováno v:
Dawson, W M, Martin, F J O, Rhys, G G, Shelley, K L, Brady, R L & Woolfson, D N 2021, ' Coiled coils 9-to-5 : rational de novo design of α-helical barrels with tunable oligomeric states ', Chemical Science, vol. 12, no. 20, pp. 6923-6928 . https://doi.org/10.1039/d1sc00460c
The rational design of linear peptides that assemble controllably and predictably in water is challenging. Short sequences must encode unique target structures and avoid alternative states. However, the non-covalent forces that stabilize and discrimi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::939f1f7d1bd526a6bd01378f9c86571c
https://doi.org/10.1039/d1sc00460c
https://doi.org/10.1039/d1sc00460c
Autor:
Tetsushi Kataura, Elsje G Otten, Yoana Rabanal‐Ruiz, Elias Adriaenssens, Francesca Urselli, Filippo Scialo, Lanyu Fan, Graham R Smith, William M Dawson, Xingxiang Chen, Wyatt W Yue, Agnieszka K Bronowska, Bernadette Carroll, Sascha Martens, Michael Lazarou, Viktor I Korolchuk
Mitophagy, the elimination of mitochondria via the autophagy-lysosome pathway, is essential for the maintenance of cellular homeostasis. The best characterised mitophagy pathway is mediated by stabilisation of the protein kinase PINK1 and recruitment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d56ceed8916832358c51cd75384593b4
https://hdl.handle.net/11591/485468
https://hdl.handle.net/11591/485468
Autor:
Guto G, Rhys, Jessica A, Cross, William M, Dawson, Harry F, Thompson, Sooruban, Shanmugaratnam, Nigel J, Savery, Mark P, Dodding, Birte, Höcker, Derek N, Woolfson
Publikováno v:
Nature chemical biology. 18(9)
Increasingly, it is possible to design peptide and protein assemblies de novo from first principles or computationally. This approach provides new routes to functional synthetic polypeptides, including designs to target and bind proteins of interest.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::17fbd9340059c631067d1b6fc909d8e6
https://pubmed.ncbi.nlm.nih.gov/35836017
https://pubmed.ncbi.nlm.nih.gov/35836017
Autor:
Christopher Williams, William M. Dawson, Adrian J. Mulholland, Matthew P. Crump, R. Leo Brady, Eric J. M. Lang, Kathryn L Shelley, Guto G. Rhys, Derek N. Woolfson
Publikováno v:
Nature Communications
Dawson, W M, Lang, E J M, Rhys, G G, Shelley, K L, Williams, C, Brady, R L, Crump, M P, Mulholland, A J & Woolfson, D N 2021, ' Structural resolution of switchable states of a de novo peptide assembly ', Nature Communications, vol. 12, no. 1, 1530 (2020) . https://doi.org/10.1038/s41467-021-21851-8
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Dawson, W M, Lang, E J M, Rhys, G G, Shelley, K L, Williams, C, Brady, R L, Crump, M P, Mulholland, A J & Woolfson, D N 2021, ' Structural resolution of switchable states of a de novo peptide assembly ', Nature Communications, vol. 12, no. 1, 1530 (2020) . https://doi.org/10.1038/s41467-021-21851-8
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
De novo protein design is advancing rapidly. However, most designs are for single states. Here we report a de novo designed peptide that forms multiple α-helical-bundle states that are accessible and interconvertible under the same conditions. Usual
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4412c9b6d818e92335594445134d1004
http://europepmc.org/articles/PMC7943578
http://europepmc.org/articles/PMC7943578
Autor:
William M, Dawson, Freddie J O, Martin, Guto G, Rhys, Kathryn L, Shelley, R Leo, Brady, Derek N, Woolfson
Publikováno v:
Chemical Science
The rational design of linear peptides that assemble controllably and predictably in water is challenging. Short sequences must encode unique target structures and avoid alternative states. However, the non-covalent forces that stabilize and discrimi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9912a759cb517f015177aa33c997d95e
https://pubmed.ncbi.nlm.nih.gov/34745518
https://pubmed.ncbi.nlm.nih.gov/34745518
Autor:
William M. Dawson, Freddie J. O. Martin, Derek N. Woolfson, Kathryn L Shelley, Guto G. Rhys, R. Leo Brady
The rational design of linear peptides that assemble controllably and predictably in water is challenging. Sequences must encode unique target structures and avoid alternative states. However, the stabilizing and discriminating non-covalent forces av
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::166d59cbb2f381b7920e69a53824066c
https://doi.org/10.1101/2021.01.20.427391
https://doi.org/10.1101/2021.01.20.427391