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N-linked glycan stabilization of the VWF A2 domain
by Christopher J. Lynch, and David A. Lane
Blood
Volume 127(13):1711-1718
March 31, 2016
©2016 by American Society of Hematology
Structure and manipulation of the VWF A2 domain N-linked glycans.
Christopher J. Lynch, and David A. Lane Blood
2016;127:1711-1718
©2016 by American Society of Hematology
N-linked glycosylation stabilizes the VWF A2 domain through the N1574-GlcNAc linkage.
Christopher J. Lynch, and David A. Lane Blood
2016;127:1711-1718
©2016 by American Society of Hematology
Solution competition assay of ADAMTS13 with VWF A2 domain glycan variants.
Christopher J. Lynch, and David A. Lane Blood
2016;127:1711-1718
©2016 by American Society of Hematology
N1574-GlcNAc intradomain interactions.
Christopher J. Lynch, and David A. Lane Blood
2016;127:1711-1718
©2016 by American Society of Hematology
Functional role of Y1544 in A2 domain stability and ADAMTS13 interaction.
Christopher J. Lynch, and David A. Lane Blood
2016;127:1711-1718
©2016 by American Society of Hematology
Proteolysis of glycan variants of the VWF A2 domain and FLVWF. (A) The VWF A2 variants (2 µM)
WT, N1574Q, GnT−/−, EndoH, and Y1544D/N1574Q and ADAMTS13 (20 nM) were separately
preincubated with 20 mM Tris (pH7.9), 150 mM NaCl, 5 mM CaCl2 and 2 M urea for at...
Christopher J. Lynch, and David A. Lane Blood
2016;127:1711-1718
©2016 by American Society of Hematology
Relationship between VWF A2 domain thermostability and ADAMTS13 binding.
Christopher J. Lynch, and David A. Lane Blood
2016;127:1711-1718
©2016 by American Society of Hematology
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