Human protein aging: modification and crosslinking through dehydroalanine and dehydrobutyrine intermediates
Article first published online: 19 NOV 2013
© 2013 The Authors. Aging Cell published by the Anatomical Society and John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 13, Issue 2, pages 226–234, April 2014
Total views since publication: 484
How to Cite
Wang, Z., Lyons, B., Truscott, R. J. W. and Schey, K. L. (2014), Human protein aging: modification and crosslinking through dehydroalanine and dehydrobutyrine intermediates. Aging Cell, 13: 226–234. doi: 10.1111/acel.12164
- Issue published online: 11 MAR 2014
- Article first published online: 19 NOV 2013
- Accepted manuscript online: 17 OCT 2013 10:41AM EST
- Manuscript Accepted: 12 SEP 2013
- NIH. Grant Number: EY013462
- Vanderbilt Vision Research Center. Grant Number: P30 EY008126
- Vanderbilt Mass Spectrometry Research Center
- NHMRC. Grant Number: 1008667
Fig. S1 Selected ion chromatograms and tandem mass spectra of GSH-modified lens crystallin peptides.
Fig. S2 NMR spectra of synthetic peptides and reaction products.
Fig. S3 In vitro formation of glutathionylated AQP0 peptides.
Fig. S4 Extent of GSH modification on αB-crystallin S59 in combined water-soluble and urea-soluble fractions in distinct lens regions measured by MRM.
Fig. S5 Tandem mass spectra of crosslinked peptides identified in a cataract lens nucleus.
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