Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10536785 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2015 | 6 Pages |
Abstract
These data indicate that the FXArg386 is involved in FIXa/FVIIIa-mediated FX activation and help in elucidating the bleeding tendency associated with the FX386Cys in a rare FX deficiency case. Taking advantage of the unpaired cysteine, the rFX386Cys mutant may be efficiently targeted by thiol-specific ligands and represent a valuable tool to study FX structure-function relationships both in vitro and in vivo.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
M. Baroni, G. Pavani, M. Pinotti, A. Branchini, F. Bernardi, R.M. Camire,