Zobrazeno 1 - 10
of 166
pro vyhledávání: '"Alison E. Ashcroft"'
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:
Matthew G. Iadanza, Anna J. Higgins, Bob Schiffrin, Antonio N. Calabrese, David J. Brockwell, Alison E. Ashcroft, Sheena E. Radford, Neil A. Ranson
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
The β-barrel assembly machinery (BAM complex) is a key mediator of outer membrane protein biogenesis in Gram-negative bacteria. Here the authors report a cryo-EM structure of the intact BAM complex that suggests that lateral gate opening is a necess
Externí odkaz:
https://doaj.org/article/88d9b9184d62412599a6be4be362ef28
Publikováno v:
Beilstein Journal of Nanotechnology, Vol 4, Iss 1, Pp 429-440 (2013)
We examine how the different steric packing arrangements found in amyloid fibril polymorphs can modulate their mechanical properties using steered molecular dynamics simulations. Our calculations demonstrate that for fibrils containing structural def
Externí odkaz:
https://doaj.org/article/5071808072d9455896106f1d93e8206c
Autor:
Alison E Ashcroft, Frank Sobott
Over the last decade, the use of ion mobility separation in combination with mass spectrometry analysis has developed significantly. This technique adds a unique extra dimension enabling the in-depth analysis of a wide range of complex samples in the
Publikováno v:
Journal of the American Society for Mass Spectrometry. 32:1583-1592
NMR studies and X-ray crystallography have shown that the structures of the 99-residue amyloidogenic protein β2-microglobulin (β2m) and its more aggregation-prone variant, D76N, are indistinguishable, and hence, the reason for the striking differen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1673b360f70885712f022e6d71658e91
https://doi.org/10.1021/jasms.0c00438
https://doi.org/10.1021/jasms.0c00438
Autor:
Paul W. A. Devine, Elizabeth England, Nicholas J. Bond, David C. Lowe, Amy S. Warwick, James Button, Sheena E. Radford, Janet C. Saunders, Bob Schiffrin, Alison E. Ashcroft, Alice M. Gordon, Chris Lloyd, David J. Brockwell, Stacey E. Chin, Jessica S. Ebo
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Nature Communications
Nature Communications
Protein biopharmaceuticals are highly successful, but their utility is compromised by their propensity to aggregate during manufacture and storage. As aggregation can be triggered by non-native states, whose population is not necessarily related to t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96889bc4c8d3d6996481b717209e811e
https://doaj.org/article/7cd4d27ccee2435a841e247a296e334c
https://doaj.org/article/7cd4d27ccee2435a841e247a296e334c
Publikováno v:
Journal of the American Society for Mass Spectrometry. 31:553-564
As monoclonal antibodies (mAbs) rapidly emerge as a dominant class of therapeutics, so does the need for suitable analytical technologies to monitor for changes in protein higher order structure (HOS) of these biomolecules. Reference materials (RM) s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c0e786a8b5232172de6385673a673ff
https://doi.org/10.1021/jasms.9b00022
https://doi.org/10.1021/jasms.9b00022
Autor:
Z. Soloviev, E. De Lorenzi, Paul A. Dalby, Bradley B. Stocks, C. Burns, D. Cooper-Shepherd, Altin Sula, V. Wood, Kamila J. Pacholarz, E. Rodriguez, Perdita E. Barran, Kate Groves, Jonathan J. Phillips, L. Luckau, Bonnie A. Wallace, Konstantinos Thalassinos, R. Parakra, S. Hill, P. Vicedo, Raffaella Colombo, J. A. Ferguson, Ryan D. Davis, Alison E. Ashcroft, Adam Cryar, Rosie Upton, Hongyu Zhang, Lorna Ashton, O. Durrant, J.R. Ault, Milena Quaglia
Measurements of protein higher order structure (HOS) provide important information on stability, potency, efficacy, immunogenicity, and biosimilarity of biopharmaceuticals, with a significant number of techniques and methods available to perform thes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3e8ca47638ee630d9e7c7c1baab0db7
https://nrc-publications.canada.ca/eng/view/object/?id=d45a403f-088a-4d02-9c14-40c49ef4daaa
https://nrc-publications.canada.ca/eng/view/object/?id=d45a403f-088a-4d02-9c14-40c49ef4daaa
Autor:
Richard A. Norman, Julie A. Tucker, Malcolm Anderson, Helen S. Beeston, Tobias Klein, Alison E. Ashcroft, Geoffrey A. Holdgate
Publikováno v:
Rapid communications in mass spectrometry : RCMREFERENCES.
Rationale The protein kinase FGFR1 regulates cellular processes in human development. As over-activity of FGFR1 is implicated with cancer, effective inhibitors are in demand. Type I inhibitors, which bind to the active form of FGFR1, are less effecti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::524e5426716ee2e6b01163f83d7e97cc
https://pubmed.ncbi.nlm.nih.gov/34038603
https://pubmed.ncbi.nlm.nih.gov/34038603