Showing 1961 - 1970 of 2039 Items
Statement by Anonymous (Paula) collected by Erika Bjorum on October 9, 2018 [part 2]
Date: 2018-10-09
Creator: Anonymous (Paula)
Access: Open access
- Transcription of statement includes parts 1 and 2, recorded on October 5 and October 9, 2018. This statement was given privately.
Statement by Deborah Yarmal collected by Rachel George on November 19, 2013
Date: 2013-11-19
Creator: Deborah Yarmal
Access: Open access
Statement by Bruce Mallonee collected by Rachel George on November 21, 2014
Date: 2014-11-21
Creator: Bruce Mallonee
Access: Open access
Statement by Penthea Burns collected by Rachel George on November 18, 2014
Date: 2014-11-18
Creator: Penthea Burns
Access: Open access
Statement by Betty Joseph collected by Rachel George on April 23, 2015
Date: 2015-04-23
Creator: Betty Joseph
Access: Open access
Statement by Susan Burgess collected by Rachel George on June 26, 2014
Date: 2014-06-26
Creator: Susan Burgess
Access: Open access
Statement by Randi McKechnie collected by Joan Uraneck on December 15, 2014
Date: 2014-12-15
Creator: Randi McKechnie
Access: Open access
Statement by Fred Putnam collected by Marilyn Bronzi on November 18, 2014
Date: 2014-11-18
Creator: Fred Putnam
Access: Open access
Probing mucin-type O-linked glycosylation in living animals
Date: 2006-03-28
Creator: Danielle H. Dube
Jennifer A. Prescher
Chi M. Quang
Carolyn R. Bertozzi
Access: Open access
- Changes in O-linked protein glycosylation are known to correlate with disease states but are difficult to monitor in a physiological setting because of a lack of experimental tools. Here, we report a technique for rapid profiling of O-linked glycoproteins in living animals by metabolic labeling with N-azidoacetylgalactosamine (GalNAz) followed by Staudinger ligation with phosphine probes. After injection of mice with a peracetylated form of GalNAz, azide-labeled glycoproteins were observed in a variety of tissues, including liver, kidney, and heart, in serum, and on isolated splenocytes. B cell glycoproteins were robustly labeled with GalNAz but T cell glycoproteins were not, suggesting fundamental differences in glycosylation machinery or metabolism. Furthermore, GalNAz-labeled B cells could be selectively targeted with a phosphine probe by Staudinger ligation within the living animal. Metabolic labeling with GalNAz followed by Staudinger ligation provides a means for proteomic analysis of this posttranslational modification and for identifying O-linked glycoprotein fingerprints associated with disease. © 2006 by The National Academy of Sciences of the USA.
The Role of Social Media for Knowledge Sharing and Collaboration in Distributed Teams
Creator: Nicole Ellison
Matthew Weber
Access: Open access
- Abstract