Zobrazeno 1 - 10
of 104
pro vyhledávání: '"David J Brockwell"'
Autor:
Bob Schiffrin, Joel A. Crossley, Martin Walko, Jonathan M. Machin, G. Nasir Khan, Iain W. Manfield, Andrew J. Wilson, David J. Brockwell, Tomas Fessl, Antonio N. Calabrese, Sheena E. Radford, Anastasia Zhuravleva
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract The ATP-independent chaperone SurA protects unfolded outer membrane proteins (OMPs) from aggregation in the periplasm of Gram-negative bacteria, and delivers them to the β-barrel assembly machinery (BAM) for folding into the outer membrane
Externí odkaz:
https://doaj.org/article/b8ce23fd6b774989b970d0af57f9265e
Autor:
Oliver E Farrance, Eleanore Hann, Renata Kaminska, Nicholas G Housden, Sasha R Derrington, Colin Kleanthous, Sheena E Radford, David J Brockwell
Publikováno v:
PLoS Biology, Vol 11, Iss 2, p e1001489 (2013)
Colicins are protein antibiotics synthesised by Escherichia coli strains to target and kill related bacteria. To prevent host suicide, colicins are inactivated by binding to immunity proteins. Despite their high avidity (K(d) ≈ fM, lifetime ≈ 4 d
Externí odkaz:
https://doaj.org/article/971c0dd9777f4a4593fa9ceffca2a088
Autor:
Matt D. G. Hughes, Sophie Cussons, Benjamin S. Hanson, Kalila R. Cook, Tímea Feller, Najet Mahmoudi, Daniel L. Baker, Robert Ariëns, David A. Head, David J. Brockwell, Lorna Dougan
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-11 (2023)
Abstract Fibrous networks constructed from high aspect ratio protein building blocks are ubiquitous in nature. Despite this ubiquity, the functional advantage of such building blocks over globular proteins is not understood. To answer this question,
Externí odkaz:
https://doaj.org/article/75078bc47eed4e7291592f100c7a7a87
Autor:
Sabine M. Ulamec, Roberto Maya-Martinez, Emily J. Byrd, Katherine M. Dewison, Yong Xu, Leon F. Willis, Frank Sobott, George R. Heath, Patricija van Oosten Hawle, Vladimir L. Buchman, Sheena E. Radford, David J. Brockwell
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
The authors of this work characterize the effect of amino acid substitution on α-synuclein (α-Syn) aggregation. Residues 38 and 42 (in addition to 39) within the P1 region of α-Syn affect amyloid formation. The effect of substitution at position 3
Externí odkaz:
https://doaj.org/article/795dea3b15b941688aa5f281361c1332
Autor:
Bob Schiffrin, Jonathan M. Machin, Theodoros K. Karamanos, Anastasia Zhuravleva, David J. Brockwell, Sheena E. Radford, Antonio N. Calabrese
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-15 (2022)
Interaction of the outer membrane protein (OMP) chaperone SurA and the OMP folding catalyst BAM results in changes in the conformational ensembles of both species, suggesting a mechanism for delivery of OMPs to BAM in Gram-negative bacteria.
Externí odkaz:
https://doaj.org/article/49dc31e55c1c4e7abc6e6cd217e49c7b
Autor:
Christa P. Brown, Matt D. G. Hughes, Najet Mahmoudi, David J. Brockwell, P. Louise Coletta, Sally Peyman, Stephen D. Evans, Lorna Dougan
Publikováno v:
Biomaterials Science. 11:2726-2737
Globular folded proteins are powerful building blocks to create biomaterials with mechanical robustness and inherent biological functionality.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::43d7f81e392abf9001511f5c6162d326
https://doi.org/10.1039/d2bm01918c
https://doi.org/10.1039/d2bm01918c
Publikováno v:
Soft Matter. 19:3167-3178
Through a multi-modal rheology approach, we show that muscle-inspired hydrogels exhibit a surprising diversity of viscoelastic response from power-law rheology at low strains to stiffening and energy dissipation at high strains.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::21e2255869fa8ad33a21e3b676c42994
https://doi.org/10.1039/d2sm01225a
https://doi.org/10.1039/d2sm01225a
Publikováno v:
BMC Biology, Vol 15, Iss 1, Pp 1-16 (2017)
Abstract The cell envelope is essential for the survival of Gram-negative bacteria. This specialised membrane is densely packed with outer membrane proteins (OMPs), which perform a variety of functions. How OMPs fold into this crowded environment rem
Externí odkaz:
https://doaj.org/article/3309b024449e486aa6a7133983fb97f8
Publikováno v:
Trends in Chemistry. 4:378-391
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b6c1d83736eec3295bc3ae3118e2f587
https://doi.org/10.1016/j.trechm.2022.02.004
https://doi.org/10.1016/j.trechm.2022.02.004
Autor:
Matt D. G. Hughes, Lorna Dougan, Benjamin S. Hanson, Najet Mahmoudi, Sophie Cussons, David J. Brockwell
Publikováno v:
ACS Nano
Hierarchical assemblies of proteins exhibit a wide-range of material properties that are exploited both in nature and by artificially by humankind. However, little is understood about the importance of protein unfolding on the network assembly, sever
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe0effd1981642b0a6201d34de922ba5
https://doi.org/10.1021/acsnano.1c00353
https://doi.org/10.1021/acsnano.1c00353