Neil J. Oldham, Ph.D

Affiliations: 
Chemistry University of Nottingham, Nottingham, England, United Kingdom 
Area:
Mass spectrometry
Website:
http://www.nottingham.ac.uk/chemistry/people/neil.oldham
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"Neil J Oldham"
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Publications

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Bellamy-Carter J, Oldham NJ. (2019) PepFoot: a software package for semi-automated processing of protein footprinting data. Journal of Proteome Research
Jenner M, Kosol S, Griffiths D, et al. (2018) Mechanism of intersubunit ketosynthase-dehydratase interaction in polyketide synthases. Nature Chemical Biology
Manzi L, Barrow AS, Scott D, et al. (2016) Carbene footprinting accurately maps binding sites in protein-ligand and protein-protein interactions. Nature Communications. 7: 13288
Soukarieh F, Nowicki MW, Bastide A, et al. (2016) Design of nucleotide-mimetic and non-nucleotide inhibitors of the translation initiation factor eIF4E: Synthesis, structural and functional characterisation. European Journal of Medicinal Chemistry. 124: 200-217
Scott D, Garner TP, Long J, et al. (2016) Mass spectrometry insights into a tandem ubiquitin-binding domain hybrid engineered for the selective recognition of unanchored polyubiquitin. Proteomics
Jenner M, Afonso JP, Kohlhaas C, et al. (2016) Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins. Chemical Communications (Cambridge, England)
Scott D, Layfield R, Oldham NJ. (2015) Structural insights into interactions between ubiquitin specific protease 5 and its polyubiquitin substrates by mass spectrometry and ion mobility spectrometry. Protein Science : a Publication of the Protein Society
Scott D, Layfield R, Oldham NJ. (2015) Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5. Proteomics
Jenner M, Afonso JP, Bailey HR, et al. (2015) Acyl-chain elongation drives ketosynthase substrate selectivity in trans-acyltransferase polyketide synthases. Angewandte Chemie (International Ed. in English). 54: 1817-21
Scott D, Oldham NJ, Strachan J, et al. (2015) Ubiquitin-binding domains: mechanisms of ubiquitin recognition and use as tools to investigate ubiquitin-modified proteomes. Proteomics. 15: 844-61
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