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Issue DateTitleAuthor(s)
2016-01-25Combination of Ambiguous and Unambiguous Data in the Restraint-driven Docking of Flexible Peptides with HADDOCK: The Binding of the Spider Toxin PcTx1 to the Acid Sensing Ion Channel (ASIC) 1a.Deplazes, E; Davies, J; Bonvin, AMJJ; King, GF; Mark, AE
2019-09-25Experimental and theoretical tools to elucidate the binding mechanisms of solid-binding peptides.Bansal, R; Care, A; Lord, MS; Walsh, TR; Sunna, A
2013-04-12Breast Cancer-Derived Microparticles Display Tissue Selectivity in the Transfer of Resistance Proteins to CellsJaiswal, R; Luk, F; Dalla, PV; Grau, GER; Bebawy, M
2017-02-22Structural basis for the hijacking of endosomal sorting nexin proteins by Chlamydia trachomatisPaul, B; Kim, HS; Kerr, MC; Huston, WM; Teasdale, RD; Collins, BM
2015-01-01MHJ-0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniaeJarocki, VM; Santos, J; Tacchi, JL; Raymond, BBA; Deutscher, AT; Jenkins, C; Padula, MP; Djordjevic, SP
2017-03-14Staged heterogeneity learning to identify conformational B-cell epitopes from antigen sequencesRen, J; Song, J; Ellis, J; Li, J
2011-11-01Isoforms of the heteropteran Nezara viridula ecdysone receptor: Protein characterisation, RH5992 insecticide binding and homology modellingTohidi-Esfahani, D; Lawrence, MC; Graham, LD; Hannan, GN; Simpson, AM; Hill, RJ
2012-11-01A helminth cathelicidin-like protein suppresses antigen processing and presentation in macrophages via inhibition of lysosomal vATPaseRobinson, MW; Alvarado, R; To, J; Hutchinson, AT; Dowdell, SN; Lund, M; Turnbull, L; Whitchurch, CB; O'Brien, BA; Dalton, JP; Donnelly, S
2014-06-06Cilium Adhesin P216 (MHJ-0493) is a target of ectodomain shedding and aminopeptidase activity on the surface of mycoplasma hyopneumoniaeTacchi, JL; Raymond, BBA; Jarocki, VM; Berry, IJ; Padula, MP; Djordjevic, SP
2010-08-01The VQ motif protein IKU1 regulates endosperm growth and seed size in ArabidopsisWang, A; Garcia, D; Zhang, H; Feng, K; Chaudhury, A; Berger, F; Peacock, WJ; Dennis, ES; Luo, M
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