ArticleMethods in molecular biology (Clifton, N.J.)2026
A Vortex-Shear-Based Assay for Cleavage of Multimeric VWF by ADAMTS13.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Proteolytic cleavage of von Willebrand factor (VWF) by ADAMTS13 is a critical regulatory mechanism that maintains hemostatic balance, which directly influences VWF platelet adhesive function. In circulation, VWF adopts a globular conformation that is resistant to proteolysis by ADAMTS13. Exposure to high shear stress, as seen in the small arteries and microvasculature, induces VWF unfolding, which exposes the cleavage site within the A2 domain and allows ADAMTS13 to cleave VWF at the Tyr1605-Met1606 bond. Conventional assays for cleavage of multimeric VWF by ADAMTS13 rely on unfolding of VWF by denaturants such as urea or guanidine-HCl. Our laboratory first developed the vortex-shear-based assay that applies a mechanical shear in a small test tube to induce VWF unfolding for ADAMTS13 cleavage. The assay allows us to assess the proteolytic activity of ADAMTS13 and its cofactor-dependent regulatory function under physiologically relevant conditions. This chapter provides a detailed protocol for performing the vortex-based assay for research purpose.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.