By George M. Rodgers
This accomplished quantity discusses the protease ADAMTS13, summarizing the present prestige of easy and medical study. The 9 authoritative chapters start with a old viewpoint via exploration of the biochemistry and structure-function relationships of ADAMTS13 in addition to its common functionality in hemostasis (cleavage of von Willebrand factor). rising examine issues for ADAMTS13 are lined, together with its capability position in angiogenesis and different points of cellphone biology. extra themes comprise laboratory assays for ADAMTS13, inherited ADAMTS13 deficiency, and purchased ADAMTS13 deficiency. A bankruptcy on comparable thrombotic microangiopathic (TMA) issues examines the variations among TMAs linked to ADAMTS13 deficiency and people now not linked to ADAMTS13 deficiency. a last bankruptcy reports the initial info on rising points of ADAMTS13, resembling the prestige of recombinant ADAMTS13 items and their strength utility.
Comprehensive in its exploration of the ADAMTS13 protease in disease, ADAMTS13: Biology and disorder is an important source for medical hematologists, transfusion drugs physicians, and researchers drawn to hemostasis, vascular biology, biochemistry, and metalloproteases.
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Additional resources for ADAMTS13: Biology and Disease
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43. Stupka N, Kintakas C, White JD, Fraser FW, Hanciu M, Aramaki-Hattori N, Martin S, Coles C, Collier F, Ward AC, Apte SS, McCulloch DR. Versican processing by a disintegrin-like and metalloproteinase domain with thrombospondin-1 repeats proteinases-5 and -15 facilitates myoblast fusion. J Biol Chem. 2013;288(3):1907–17. 429647. Epub 2012/12/13. 44. Gerhardt S, Hassall G, Hawtin P, McCall E, Flavell L, Minshull C, Hargreaves D, Ting A, Pauptit RA, Parker AE, Abbott WM. Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteinerich domains.