Ontology highlight
ABSTRACT:
INSTRUMENT(S): Orbitrap Fusion Lumos, LTQ Orbitrap Velos, Q Exactive
ORGANISM(S): Homo Sapiens (human) Saccharomyces Cerevisiae (baker's Yeast)
SUBMITTER: Joshua Hamey
LAB HEAD: Marc R Wilkins
PROVIDER: PXD009515 | Pride | 2018-09-03
REPOSITORIES: Pride
Action | DRS | |||
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Datamanuallyanalysed.txt | Txt | |||
EF1A-ve_metassay_lysarg_1ul.dat | Other | |||
EF1A-ve_metassay_lysarg_1ul.mgf | Mgf | |||
EF1A-ve_metassay_lysarg_1ul.raw | Raw | |||
EF1A-ve_metassay_tryp_1ul.dat | Other |
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Hamey Joshua J JJ Separovich Ryan J RJ Wilkins Marc R MR
Journal of proteome research 20180906 10
Protein methyltransferases often recognize their substrates through linear sequence motifs. The determination of these motifs is critical to understand methyltransferase mechanism, function, and drug targeting. Here we describe MT-MAMS (methyltransferase motif analysis by mass spectrometry), a quantitative approach to characterize methyltransferase substrate recognition motifs. In MT-MAMS, peptide sets are synthesized which contain all amino acid substitutions at single positions within a templa ...[more]