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pro vyhledávání: '"Ashcroft, AE"'
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=core_ac_uk__::7570edb3040d17d294dd076ae5ca9224
Understanding the structural mechanism by which proteins and peptides aggregate is crucial given the role of fibrillar aggregates in debilitating amyloid diseases and bioinspired materials. Yet, this is a major challenge given assembly involves multi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::355bdf0069518dc154250436e02232c4
https://eprints.whiterose.ac.uk/145685/5/eaav8216.full.pdf
https://eprints.whiterose.ac.uk/145685/5/eaav8216.full.pdf
Hydrogen deuterium exchange (HDX) coupled to mass spectrometry (MS) is a well-established technique employed in the field of structural MS to probe the solvent accessibility, dynamics and hydrogen bonding of backbone amides in proteins. By contrast,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::4625fbe590e794de8099655ff2b7e6b8
https://eprints.whiterose.ac.uk/135582/7/10.1007_s13361-018-2067-y.pdf
https://eprints.whiterose.ac.uk/135582/7/10.1007_s13361-018-2067-y.pdf
Autor:
Martin, EM, Jackson, MP, Gamerdinger, M, Gense, K, Karamanos, TK, Humes, JR, Deuerling, E, Ashcroft, AE, Radford, SE
Publikováno v:
The Journal of Biological Chemistry
As newly synthesized polypeptides emerge from the ribosome, it is crucial that they fold correctly. To prevent premature aggregation, nascent chains interact with chaperones that facilitate folding or prevent misfolding until protein synthesis is com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::29b9478a4f16529351ef5de097310b5a
Autor:
Schiffrin, R, Calabrese, AN, Higgins, AJ, Humes, JR, Ashcroft, AE, Kalli, AC, Brockwell, DJ, Radford, SE
The biogenesis of outer-membrane proteins (OMPs) in gram-negative bacteria involves delivery by periplasmic chaperones to the β-barrel assembly machinery (BAM), which catalyzes OMP insertion into the outer membrane. Here, we examine the effects of m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::dd76bd8f3bc8cf27b9838822067ef891
https://eprints.whiterose.ac.uk/121155/22/1-s2.0-S002228361730445X-main.pdf
https://eprints.whiterose.ac.uk/121155/22/1-s2.0-S002228361730445X-main.pdf
Autor:
Calabrese, AN, Jackson, SM, Jones, LN, Beckstein, O, Heinkel, F, Gsponer, J, Sharples, D, Sans, M, Kokkinidou, M, Pearson, AR, Radford, SE, Ashcroft, AE, Henderson, PJF
Cys accessibility and quantitative intact mass spectrometry (MS) analyses have been devised to study the topological transitions of Mhp1, the membrane protein for sodium-linked transport of hydantoins from Microbacterium liquefaciens. Mhp1 has been c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::2a8bc36508119ad8d093a07644d46b90
https://eprints.whiterose.ac.uk/119336/6/acs.analchem.pdf
https://eprints.whiterose.ac.uk/119336/6/acs.analchem.pdf
Although amyloid assembly in vitro is commonly investigated using single protein sequences, fibril formation in vivo can be more heterogeneous, involving co-assembly of proteins of different length, sequence and/or post-translational modifications. E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::22b0fe3e25843cfa9cb8cd5240f6348d
https://eprints.whiterose.ac.uk/116895/7/c7sc00620a.pdf
https://eprints.whiterose.ac.uk/116895/7/c7sc00620a.pdf
Autor:
Schiffrin, B, Calabrese, AN, Devine, PWA, Harris, SA, Ashcroft, AE, Brockwell, DJ, Radford, SE
The trimeric chaperone Skp sequesters outer-membrane proteins (OMPs) within a hydrophobic cage, thereby preventing their aggregation during transport across the periplasm in Gram-negative bacteria. Here, we studied the interaction between Escherichia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::36ef1df3c9693f0df4be838430e9b484
https://eprints.whiterose.ac.uk/101494/1/finalpaper.pdf
https://eprints.whiterose.ac.uk/101494/1/finalpaper.pdf
The chaperonin GroEL binds folding intermediates of four-disulfidehen lysozyme transiently within its central cavity. Using stopped flow fluorescence we show that GroEL binds early intermediates in folding and accelerates the slow kinetic phase that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::574f74231565697c6fe40c0781b9e3c5
https://ora.ox.ac.uk/objects/uuid:7a796c7b-91b8-488d-b3ab-f0d89ddc5df4
https://ora.ox.ac.uk/objects/uuid:7a796c7b-91b8-488d-b3ab-f0d89ddc5df4
ESI-IMS-MS: A method for rapid analysis of protein aggregation and its inhibition by small molecules
Electrospray ionisation-ion mobility spectrometry-mass spectrometry (ESI-IMS-MS) is a powerful method for the study of conformational changes in protein complexes, including oligomeric species populated during protein self-aggregation into amyloid fi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::54e48a8d6a40ffe06868864a0e4be098
https://eprints.whiterose.ac.uk/91940/8/RadfordESI-IMS-MSamethodforrapidanalysis.pdf
https://eprints.whiterose.ac.uk/91940/8/RadfordESI-IMS-MSamethodforrapidanalysis.pdf