Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 2, Issue 3, Pages 182-190Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.M300027-MCP200
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- NCRR NIH HHS [RR01614] Funding Source: Medline
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The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification. The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach. We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry. J. Am. Soc. Mass Spectrom. 12, 1106-1113). In this Work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
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