Items where authors include "Hewitt, EW"

Export as [feed] Atom [feed] RSS
Jump to: Article
Number of items: 13.

Article

Chau, CC orcid.org/0000-0002-3134-6798, Hewitt, EW orcid.org/0000-0002-6238-6303 and Actis, P orcid.org/0000-0002-7146-1854 (2021) The role of macromolecular crowding in single-entity electrochemistry: Friend or foe? Current Opinion in Electrochemistry, 25. 100654. ISSN 2451-9103

Chau, CC orcid.org/0000-0002-3134-6798, Radford, SE orcid.org/0000-0002-3079-8039, Hewitt, EW orcid.org/0000-0002-6238-6303 et al. (1 more author) (2020) Macromolecular Crowding Enhances the Detection of DNA and Proteins by a Solid-State Nanopore. Nano Letters, 20 (7). pp. 5553-5561. ISSN 1530-6984

Karamanos, TK, Jackson, MP, Calabrese, AN et al. (6 more authors) (2019) Structural mapping of oligomeric intermediates in an amyloid assembly pathway. eLife, 8. e46574. ISSN 2050-084X

Iadanza, MG, Jackson, MP, Hewitt, EW orcid.org/0000-0002-6238-6303 et al. (2 more authors) (2018) A new era for understanding amyloid structures and disease. Nature Reviews Molecular Cell Biology, 19 (12). pp. 755-773. ISSN 1471-0072

Jackson, MP and Hewitt, EW orcid.org/0000-0002-6238-6303 (2017) Why are Functional Amyloids Non-Toxic in Humans? Biomolecules, 7 (4). 71. ISSN 2218-273X

Jackson, MP and Hewitt, EW orcid.org/0000-0002-6238-6303 (2016) Cellular proteostasis: degradation of misfolded proteins by lysosomes. Essays in Biochemistry, 60 (2). pp. 173-180. ISSN 0071-1365

Tipping, KW, Van Oosten-Hawle, P, Hewitt, EW et al. (1 more author) (2015) Amyloid fibres: inert end-stage aggregates or key players in disease? Trends in Biochemical Sciences, 40 (12). pp. 719-727. ISSN 0968-0004

Tipping, KW, Karamanos, TK orcid.org/0000-0003-2297-540X, Jakhria, T et al. (6 more authors) (2015) pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. Proceedings of the National Academy of Sciences, 112 (18). pp. 5691-5696. ISSN 0027-8424

Jakhria, T, Hellewell, AL, Porter, MY et al. (5 more authors) (2014) β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes. Journal of Biological Chemistry, 289 (52). 35781 - 35794. ISSN 0021-9258

Hellewell, AL, Foresti, O, Gover, N et al. (2 more authors) (2014) Analysis of Familial Hemophagocytic Lymphohistiocytosis type 4 (FHL-4) mutant proteins reveals that S-acylation is required for the function of syntaxin 11 in natural killer cells. PLoS One, 9 (6). ARTN e98900. ISSN 1932-6203

Sheynis, T, Friediger, A, Xue, W-F et al. (5 more authors) (2013) Aggregation modulators interfere with membrane interactions of β2-microglobulin fibrils. Biophysical Journal, 105 (3). 745 - 755. ISSN 0006-3495

Brend, MYP, Routledge, KE, Radford, SE et al. (1 more author) (2011) Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β 2-microglobulin monomer and fibrils. PLoS One, 6 (11). e27353. ISSN 1932-6203

Woods, LA, Platt, GW, Hellewell, AL et al. (4 more authors) (2011) Ligand binding to distinct states diverts aggregation of an amyloid-forming protein. Nature Chemical Biology, 7. 730 - 739. ISSN 1552-4469

This list was generated on Sat Apr 20 20:39:44 2024 BST.