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