ADAMTS13 cleavage efficiency is altered by mutagenic and, to a lesser extent, polymorphic sequence changes in the A1 and A2 domains of von Willebrand factor

@article{Pruss2008ADAMTS13CE,
  title={ADAMTS13 cleavage efficiency is altered by mutagenic and, to a lesser extent, polymorphic sequence changes in the A1 and A2 domains of von Willebrand factor},
  author={C. Pruss and C. Notley and C. Hegadorn and L. O'Brien and D. Lillicrap},
  journal={British Journal of Haematology},
  year={2008},
  volume={143}
}
The multimeric plasma protein von Willebrand factor (VWF) is regulated in size by its protease, ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin type 1 motif, member 13). Y1605‐M1606 cleavage site mutations and single nucleotide polymorphisms (SNPs) in the VWF A1 and A2 domains were examined for alteration in ADAMTS13‐mediated cleavage of VWF. Recombinant human full‐length VWF (rVWF) was digested with recombinant human ADAMTS13 (rADAMTS13) using a dialysis membrane method with… Expand
Rearranging Exosites in Noncatalytic Domains Can Redirect the Substrate Specificity of ADAMTS Proteases*
The genetic basis of von Willebrand disease.
Shear-Induced Unfolding and Enzymatic Cleavage of Full-Length VWF Multimers.
...
1
2
3
...

References

SHOWING 1-10 OF 26 REFERENCES
Characterization of a core binding site for ADAMTS-13 in the A2 domain of von Willebrand factor
ADAMTS13 Substrate Recognition of von Willebrand Factor A2 Domain*
Impact of mutations in the von Willebrand factor A2 domain on ADAMTS13-dependent proteolysis.
Mapping the Glycoprotein Ib-binding Site in the von Willebrand Factor A1 Domain*
FRETS‐VWF73, a first fluorogenic substrate for ADAMTS13 assay
...
1
2
3
...