Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Jordan M. Fletcher"'
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
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
The ability to dynamically control protein-protein interactions and localization of proteins is critical in synthetic biological systems. Here the authors develop a peptide-based molecular switch that regulates dimer formation and lipid membrane targ
Externí odkaz:
https://doaj.org/article/4376b19d20ae4edab075ab555f27de80
Autor:
Matthew J. Lee, Judith Mantell, Ian R. Brown, Jordan M. Fletcher, Paul Verkade, Richard W. Pickersgill, Derek N. Woolfson, Stefanie Frank, Martin J. Warren
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Bacterial microcompartments (BMCs) are protein-bound organelles encapsulating segments of metabolic pathways. Here the authors utilize specific de novo coiled-coil protein-protein interactions to display proteins on the outer or inner surface of BMCs
Externí odkaz:
https://doaj.org/article/c4588752a0774db5a65123c4b6546adb
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Fletcher, J M, Woolfson, D N & Schwille, P 2021, ' De novo design of a reversible phosphorylation-dependent switch for membrane targeting ', Nature Communications, vol. 12, no. 1, 1472 . https://doi.org/10.1038/s41467-021-21622-5
Nature Communications
Fletcher, J M, Woolfson, D N & Schwille, P 2021, ' De novo design of a reversible phosphorylation-dependent switch for membrane targeting ', Nature Communications, vol. 12, no. 1, 1472 . https://doi.org/10.1038/s41467-021-21622-5
Nature Communications
Modules that switch protein-protein interactions on and off are essential to develop synthetic biology; for example, to construct orthogonal signaling pathways, to control artificial protein structures dynamically, and for protein localization in cel
Autor:
Deborah K. Shoemark, Derek N. Woolfson, Richard B. Sessions, Tanniemola B. Liverpool, Majid Mosayebi, Noah Linden, Jordan M. Fletcher
Publikováno v:
Mosayebi, M, Shoemark, D K, Fletcher, J M, Sessions, R B, Linden, N, Woolfson, D N & Liverpool, T B 2017, ' Beyond icosahedral symmetry in packings of proteins in spherical shells ', Proceedings of the National Academy of Sciences of the United States of America, vol. 114, no. 34, pp. 9014-9019 . https://doi.org/10.1073/pnas.1706825114
The formation of quasi-spherical cages from protein building blocks is a remarkable self-assembly process in many natural systems, where a small number of elementary building blocks are assembled to build a highly symmetric icosahedral cage. In turn,
Autor:
Deborah K. Shoemark, Joseph L. Beesley, Colin M. Edge, Derek N. Woolfson, Dominic Alibhai, Judith Mantell, Jordan M. Fletcher, David G. Tew, Angela Bridges, Paul Verkade, Harriet E. V. Bray, James F. Ross, William M. Dawson, Richard B. Sessions, Lorna Hodgson
Publikováno v:
Ross, J F, Bridges, A, Fletcher, J M, Shoemark, D, Alibhai, D, Bray, H E V, Beesley, J L, Dawson, W M, Hodgson, L R, Mantell, J, Verkade, P, Edge, C M, Sessions, R B, Tew, D & Woolfson, D N 2017, ' Decorating Self-Assembled Peptide Cages with Proteins ', ACS Nano, vol. 11, no. 8, pp. 7901-7914 . https://doi.org/10.1021/acsnano.7b02368
An ability to organize and encapsulate multiple active proteins into defined objects and spaces at the nanoscale has potential applications in biotechnology, nanotechnology, and synthetic biology. Previously, we have described the design, assembly, a
Autor:
Derek N. Woolfson, Judith Mantell, Ian R. Brown, Stefanie Frank, Jordan M. Fletcher, Richard W. Pickersgill, Matthew J. Lee, Martin J. Warren, Paul Verkade
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Nature Communications
Lee, M J, Mantell, J, Brown, I R, Fletcher, J M, Verkade, P, Pickersgill, R W, Woolfson, D N, Frank, S & Warren, M J 2018, ' De novo targeting to the cytoplasmic and luminal side of bacterial microcompartments ', Nature Communications, vol. 9, 3413 . https://doi.org/10.1038/s41467-018-05922-x
Nature Communications
Lee, M J, Mantell, J, Brown, I R, Fletcher, J M, Verkade, P, Pickersgill, R W, Woolfson, D N, Frank, S & Warren, M J 2018, ' De novo targeting to the cytoplasmic and luminal side of bacterial microcompartments ', Nature Communications, vol. 9, 3413 . https://doi.org/10.1038/s41467-018-05922-x
Bacterial microcompartments, BMCs, are proteinaceous organelles that encase a specific metabolic pathway within a semi-permeable protein shell. Short encapsulation peptides can direct cargo proteins to the lumen of the compartments. However, the fusi
Autor:
Gail J. Bartlett, Guto G. Rhys, Derek N. Woolfson, Katherine A. Horner, Jordan M. Fletcher, Andrew J. Wilson
Publikováno v:
Fletcher, J, Horner, K A, Bartlett, G, Rhys, G, Wilson, A J & Woolfson, D 2018, ' De novo coiled-coil peptides as scaffolds for disrupting protein-protein interactions ', Chemical Science . https://doi.org/10.1039/C8SC02643B
Protein–protein interactions (PPIs) play pivotal roles in the majority of biological processes. Therefore, improved approaches to target and disrupt PPIs would provide tools for chemical biology and leads for therapeutic development. PPIs with α-h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::705fb21c0d6fee9a1d1b5977295fba63
https://research-information.bris.ac.uk/ws/files/168050507/c8sc02643b1.pdf
https://research-information.bris.ac.uk/ws/files/168050507/c8sc02643b1.pdf
Autor:
Guto G. Rhys, Wei-Feng Xue, Johanna M. Galloway, Robert L. Harniman, Joseph L. Beesley, Judith Mantell, Derek N. Woolfson, Majid Mosayebi, Tanniemola B. Liverpool, Lorna Hodgson, Paul Verkade, Noah Linden, Laura Senior, Jennifer Coombs, Jordan M. Fletcher, Paul Curnow
Publikováno v:
Galloway, J M, Senior, L, Fletcher, J M, Beesley, J L, Hodgson, L R, Harniman, R L, Mantell, J M, Coombs, J, Rhys, G G, Xue, W-F, Mosayebi, M, Linden, N, Liverpool, T B, Curnow, P, Verkade, P & Woolfson, D N 2018, ' Bioinspired Silicification Reveals Structural Detail in Self-Assembled Peptide Cages ', ACS Nano, vol. 12, no. 2, pp. 1420–1432 . https://doi.org/10.1021/acsnano.7b07785
ACS Nano
ACS Nano
Understanding how molecules in self-assembled soft-matter nanostructures are organized is essential for improving the design of next-generation nanomaterials. Imaging these assemblies can be challenging and usually requires processing, e.g. staining
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d4adb2ef9dbc878edcc93d35427cb2d
https://hdl.handle.net/1983/597ff710-325f-4d82-ac3f-003afee7dba4
https://hdl.handle.net/1983/597ff710-325f-4d82-ac3f-003afee7dba4
Autor:
Matthew J. Lee, Ian R. Brown, Paul Verkade, Derek N. Woolfson, Judith Mantell, Jordan M. Fletcher, Dominic Alibhai, Stefanie Frank, Lorna Hodgson, Martin J. Warren, Wei-Feng Xue
Publikováno v:
Lee, M J, Mantell, J, Hodgson, L, Alibhai, D, Fletcher, J M, Brown, I R, Frank, S, Xue, W F, Verkade, P, Woolfson, D N & Warren, M J 2018, ' Engineered synthetic scaffolds for organizing proteins within bacterial cytoplasms ', Nature Chemical Biology, vol. 14, no. 2, pp. 142-147 . https://doi.org/10.1038/nchembio.2535
We have developed a system for producing a supramolecular scaffold that permeates the entire Escherichia coli cytoplasm. This cytoscaffold is constructed from a three-component system comprising a bacterial microcompartment shell protein and two comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::864fbf50b45ca9fd768344819e866b25
https://research-information.bris.ac.uk/en/publications/e8d2ced0-196e-43a1-a84e-16b0a4e0292b
https://research-information.bris.ac.uk/en/publications/e8d2ced0-196e-43a1-a84e-16b0a4e0292b