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Inside Cover: Deamidation and Transamidation of Substance P by Tissue Transglutaminase Revealed by Electron‐Capture Dissociation Fourier Transform Mass Spectrometry (Chem. Eur. J. 2/2011)
Author(s) -
Fornelli Luca,
Schmid Adrien W.,
Grasso Luigino,
Vogel Horst,
Tsybin Yury O.
Publication year - 2011
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201190001
Subject(s) - deamidation , electron capture dissociation , mass spectrometry , dissociation (chemistry) , chemistry , fourier transform , cover (algebra) , fourier transform ion cyclotron resonance , analytical chemistry (journal) , chromatography , biochemistry , organic chemistry , enzyme , physics , mechanical engineering , quantum mechanics , engineering
Consensus sequence… … and specificity for deamidation and transamidation of peptides and proteins by tissue transglutaminase (tTGase) are of a particular interest for understanding neurodegenerative disorders. In their Full Paper on p. 486 ff. , Y. Tsybin et al. describe the application of electron‐capture dissociation high‐resolution mass spectrometry to reveal the sites of tTGase‐induced deamidation and transamidation on the neuropeptide substance P.