Sawyer, EB; Grabowska, AD; Cortes, T; (2018) Translational regulation in mycobacteria and its implications for pathogenicity. Nucleic acids research. ISSN 0305-1048 DOI: https://doi.org/10.1093/nar/gky574

Yang, W; Willemse, J; Sawyer, EB; Lou, F; Gong, WB; Zhang, H; Gras, SL; Claessen, D; Perrett, S; (2017) The propensity of the bacterial rodlin protein RdlB to form amyloid fibrils determines its function in Streptomyces coelicolor. Scientific reports, 7. p. 13. ISSN 2045-2322 DOI: https://doi.org/10.1038/srep42867

Sawyer, EB; Edgeworth, JA; Thomas, C; Collinge, J; Jackson, GS; (2015) Preclinical detection of infectivity and disease-specific PrP in blood throughout the incubation period of prion disease. Scientific reports, 5. p. 17742. ISSN 2045-2322 DOI: https://doi.org/10.1038/srep17742

Hu, C; Chan, SI; Sawyer, EB; Yu, Y; Wang, J; (2014) Metalloprotein design using genetic code expansion. Chemical Society reviews, 43 (18). pp. 6498-510. ISSN 0306-0012 DOI: https://doi.org/10.1039/c4cs00018h Full text not available from this repository.

Zhou, XM; Entwistle, A; Zhang, H; Jackson, AP; Mason, TO; Shimanovich, U; Knowles, TP; Smith, AT; Sawyer, EB; Perrett, S; (2014) Self-Assembly of Amyloid Fibrils That Display Active Enzymes. ChemCatChem, 6 (7). pp. 1961-1968. ISSN 1867-3880 DOI: https://doi.org/10.1002/cctc.201402125 Full text not available from this repository.

Lin, YW; Sawyer, EB; Wang, J; (2013) Rational heme protein design: all roads lead to Rome. Chemistry, an Asian journal, 8 (11). pp. 2534-44. ISSN 1861-4728 DOI: https://doi.org/10.1002/asia.201300291 Full text not available from this repository.

Sawyer, EB; Gras, SL; (2013) Self-assembling nanomaterials: monitoring the formation of amyloid fibrils, with a focus on small-angle X-ray scattering. Methods in molecular biology (Clifton, NJ), 996. pp. 77-101. ISSN 1064-3745 DOI: https://doi.org/10.1007/978-1-62703-354-1_5 Full text not available from this repository.

Healy, J; Wong, K; Sawyer, EB; Roux, C; Domigan, L; Gras, SL; Sunde, M; Larsen, NG; Gerrard, J; Vasudevamurthy, M; (2012) Polymorphism and higher order structures of protein nanofibers from crude mixtures of fish lens crystallins: toward useful materials. Biopolymers, 97 (8). pp. 595-606. ISSN 0006-3525 DOI: https://doi.org/10.1002/bip.22045 Full text not available from this repository.

Sawyer, EB; Barker, PD; (2012) Continued surprises in the cytochrome c biogenesis story. Protein & cell, 3 (6). pp. 405-9. ISSN 1674-800X DOI: https://doi.org/10.1007/s13238-012-2912-x

Sawyer, EB; Claessen, D; Gras, SL; Perrett, S; (2012) Exploiting amyloid: how and why bacteria use cross-β fibrils. Biochemical Society transactions, 40 (4). pp. 728-34. ISSN 0300-5127 DOI: https://doi.org/10.1042/BST20120013 Full text not available from this repository.

Chen, LJ; Sawyer, EB; Perrett, S; (2011) The yeast prion protein Ure2: insights into the mechanism of amyloid formation. Biochemical Society transactions, 39 (5). pp. 1359-64. ISSN 0300-5127 DOI: https://doi.org/10.1042/BST0391359 Full text not available from this repository.

Sawyer, EB; Claessen, D; Haas, M; Hurgobin, B; Gras, SL; (2011) The assembly of individual chaplin peptides from Streptomyces coelicolor into functional amyloid fibrils. PloS one, 6 (4). e18839. ISSN 1932-6203 DOI: https://doi.org/10.1371/journal.pone.0018839

Sawyer, EB; Stephens, E; Ferguson, SJ; Allen, JW; Barker, PD; (2010) Aberrant attachment of heme to cytochrome by the Ccm system results in a cysteine persulfide linkage. Journal of the American Chemical Society, 132 (14). pp. 4974-5. ISSN 0002-7863 DOI: https://doi.org/10.1021/ja908241v Full text not available from this repository.

Allen, JW; Sawyer, EB; Ginger, ML; Barker, PD; Ferguson, SJ; (2009) Variant c-type cytochromes as probes of the substrate specificity of the E. coli cytochrome c maturation (Ccm) apparatus. The Biochemical journal, 419 (1). 177-84, 2 p following 184. ISSN 0264-6021 DOI: https://doi.org/10.1042/BJ20081999 Full text not available from this repository.