Identification of GlcNAcylation sites of peptides and α-crystallin using Q-TOF mass spectrometry-Reference-Cited by-同舟云学术

Identification of GlcNAcylation sites of peptides and α-crystallin using Q-TOF mass spectrometry

Published:2001-10-01 Issue:10 Volume:12 Page:1106-1113
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Chalkley Robert J.¹,Burlingame A. L.¹²³

Affiliation:

1. Ludwig Institute for Cancer Research, University College Branch of Cell and Molecular Biology, Royal Free and University College Medical School, London, UK

2. Department of Pharmaceutical Chemistry, Mass Spectrometry Facility, University of California San Francisco, 94143-0446, San Francisco, CA, USA

3. Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California, USA

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1016/S1044-0305%2801%2900295-1

Reference27 articles.

1. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.

2. O-Glycosylation of Nuclear and Cytoplasmic Proteins: Regulation Analogous to Phosphorylation?

3. DYNAMIC O-LINKED GLYCOSYLATION OF NUCLEAR AND CYTOSKELETAL PROTEINS

4. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase.

5. Dynamic Glycosylation of Nuclear and Cytosolic Proteins

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