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Article

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

Doherty, CPA orcid.org/0000-0001-5685-4716, Young, LM, Karamanos, TK et al. (4 more authors) (2018) A peptide‐display protein scaffold to facilitate single molecule force studies of aggregation‐prone peptides. Protein Science, 27 (7). pp. 1205-1217. ISSN 0961-8368

Martin, EM, Jackson, MP, Gamerdinger, M et al. (6 more authors) (2018) Conformational flexibility within the nascent polypeptide–associated complex enables its interactions with structurally diverse client proteins. Journal of Biological Chemistry, 293 (22). pp. 8554-8568. ISSN 0021-9258

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

Iadanza, MG, Jackson, MP, Radford, SE et al. (1 more author) (2016) MpUL-multi: Software for Calculation of Amyloid Fibril Mass per Unit Length from TB-TEM Images. Scientific Reports, 6. 21078. ISSN 2045-2322

Saunders, JC, Young, LM, Mahood, RA et al. (7 more authors) (2016) An in vivo platform for identifying inhibitors of protein aggregation. Nature Chemical Biology, 12 (2). pp. 94-101. ISSN 1552-4450

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

This list was generated on Sat Sep 21 18:27:21 2019 BST.