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Linker regions and flexibility around the metalloprotease domain account for conformational activation of ADAMTS‐13
Authors:L. Deforche  E. Roose  A. Vandenbulcke  N. Vandeputte  H. B. Feys  T. A. Springer  L. Z. Mi  J. Muia  J. E. Sadler  K. Soejima  H. Rottensteiner  H. Deckmyn  S. F. De Meyer  K. Vanhoorelbeke
Affiliation:1. Laboratory for Thrombosis Research, IRF Life Sciences, KU Leuven Kulak, Kortrijk, Belgium;2. Transfusion Research Center, Belgian Red Cross Flanders, Gent, Belgium;3. Program in Cellular and Molecular Medicine, Boston Children's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA;4. Departments of Medicine, Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, MO, USA;5. Research Department 1, The Chemo‐Sero‐Therapeutic Research Institute, Kikuchi, Kumamoto, Japan;6. Baxter Innovations GmbH, Vienna, Austria
Abstract:
Keywords:ADAMTS‐13 protein, human  allosteric regulation  autoantibodies  protein conformation  von Willebrand factor
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