Zobrazeno 1 - 10
of 151
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:
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:
Paul White, Samuel F. Haysom, Matthew G. Iadanza, Anna J. Higgins, Jonathan M. Machin, James M. Whitehouse, Jim E. Horne, Bob Schiffrin, Charlotte Carpenter-Platt, Antonio N. Calabrese, Kelly M. Storek, Steven T. Rutherford, David J. Brockwell, Neil A. Ranson, Sheena E. Radford
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
The folding of outer membrane proteins (OMPs) is catalyzed by the βbarrel assembly machinery (BAM). Here, structural and functional analyses of BAM stabilized in distinct conformations elucidate the roles of lateral gate opening and interactions of
Externí odkaz:
https://doaj.org/article/bf4f9d65548640299d6a3b164c8b8b9d
Autor:
Matthew G. Iadanza, Bob Schiffrin, Paul White, Matthew A. Watson, Jim E. Horne, Anna J. Higgins, Antonio N. Calabrese, David J. Brockwell, Roman Tuma, Antreas C. Kalli, Sheena E. Radford, Neil A. Ranson
Publikováno v:
Communications Biology, Vol 3, Iss 1, Pp 1-14 (2020)
With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs. They show that the β-barrel domain of BamA is in a ‘lateral open’ conformation, and that BA
Externí odkaz:
https://doaj.org/article/cc183779d41f4d5aabd191eaa4c934aa
Autor:
Antonio N. Calabrese, Bob Schiffrin, Matthew Watson, Theodoros K. Karamanos, Martin Walko, Julia R. Humes, Jim E. Horne, Paul White, Andrew J. Wilson, Antreas C. Kalli, Roman Tuma, Alison E. Ashcroft, David J. Brockwell, Sheena E. Radford
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show ho
Externí odkaz:
https://doaj.org/article/2047c9564bc341c98f0fa558c55a100a
Autor:
Jessica S. Ebo, Janet C. Saunders, Paul W. A. Devine, Alice M. Gordon, Amy S. Warwick, Bob Schiffrin, Stacey E. Chin, Elizabeth England, James D. Button, Christopher Lloyd, Nicholas J. Bond, Alison E. Ashcroft, Sheena E. Radford, David C. Lowe, David J. Brockwell
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Protein aggregation remains a significant challenge for manufacturing of protein biopharmaceuticals. Here, the authors demonstrate the use of directed evolution and an assay for in vivo innate protein aggregation-propensity to generate aggregation-re
Externí odkaz:
https://doaj.org/article/7cd4d27ccee2435a841e247a296e334c
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