Shear-Dependent Interactions of von Willebrand Factor with Factor VIII and Protease ADAMTS 13 Demonstrated at a Single Molecule Level by Atomic Force Microscopy-Reference-Cited by-同舟云学术

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Shear-Dependent Interactions of von Willebrand Factor with Factor VIII and Protease ADAMTS 13 Demonstrated at a Single Molecule Level by Atomic Force Microscopy

Published:2015-09-30 Issue:20 Volume:87 Page:10299-10305
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Bonazza Klaus¹,Rottensteiner Hanspeter²,Schrenk Gerald²,Frank Johannes³,Allmaier Günter¹,Turecek Peter L.²,Scheiflinger Friedrich²,Friedbacher Gernot¹

Affiliation:

1. Institute of Chemical Technologies and Analytics, Vienna University of Technology, Getreidemarkt 9/164, A-1060 Vienna, Austria

2. Baxalta Innovations, Industriestrasse 67, A-1221 Vienna, Austria

3. Central Machine Shop of the Faculty Technical Chemistry, Vienna University of Technology, Getreidemarkt 9/174, A-1060 Vienna, Austria

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.5b02078

Reference34 articles.

1. von Willebrand factor: the old, the new and the unknown

2. Blood-clotting-inspired reversible polymer–colloid composite assembly in flow

3. The Life Cycle of Coagulation Factor VIII in View of Its Structure and Function

4. von Willebrand factor, Jedi knight of the bloodstream

5. Shear-dependent changes in the three-dimensional structure of human von Willebrand factor

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1. Cryptic Extensibility in von Willebrand Factor Revealed by Molecular Nanodissection;International Journal of Molecular Sciences;2024-07-02

2. An Automated pre-Dilution Setup for Von Willebrand Factor Activity Assays;BIO-PROTOCOL;2024

3. Biological activity of a new recombinant human coagulation factor VIII and its efficacy in a small animal model;Biochemical and Biophysical Research Communications;2023-01

4. Structural hierarchy of mechanical extensibility in human von Willebrand factor multimers;Protein Science;2022-12-29

5. Recombinant factor VIII protein aggregation and adsorption at the liquid-solid interface;Journal of Colloid and Interface Science;2022-12

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