ADAMTS13: Biology and Disease - download pdf or read online

By George M. Rodgers

ISBN-10: 3319087169

ISBN-13: 9783319087160

ISBN-10: 3319087177

ISBN-13: 9783319087177

This accomplished quantity discusses the protease ADAMTS13, summarizing the present prestige of uncomplicated and medical study. The 9 authoritative chapters commence with a historic viewpoint through exploration of the biochemistry and structure-function relationships of ADAMTS13 in addition to its general functionality in hemostasis (cleavage of von Willebrand factor). rising learn issues for ADAMTS13 are lined, together with its capability function in angiogenesis and different facets of mobilephone biology. extra subject matters comprise laboratory assays for ADAMTS13, inherited ADAMTS13 deficiency, and purchased ADAMTS13 deficiency. A bankruptcy on similar thrombotic microangiopathic (TMA) issues examines the variations among TMAs linked to ADAMTS13 deficiency and people no longer linked to ADAMTS13 deficiency. a last bankruptcy reports the initial details on rising facets of ADAMTS13, equivalent to the prestige of recombinant ADAMTS13 items and their power 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 attracted to hemostasis, vascular biology, biochemistry, and metalloproteases.

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Extra resources for ADAMTS13: Biology and Disease

Example text

Rao C, Foernzler D, Loftus SK, Liu S, McPherson JD, Jungers KA, Apte SS, Pavan WJ, Beier DR. A defect in a novel ADAMTS family member is the cause of the belted whitespotting mutation. Development. 2003;130(19):4665–72. Silver DL, Hou L, Somerville R, Young ME, Apte SS, Pavan WJ. The secreted metalloprotease ADAMTS20 is required for melanoblast survival. PLoS Genet. 2008;4(2):1–15. Rodriguez-Manzaneque JC, Westling J, Thai SN, Luque A, Knauper V, Murphy G, Sandy JD, Iruela-Arispe ML. ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors.

Mosyak L, Georgiadis K, Shane T, Svenson K, Hebert T, McDonagh T, Mackie S, Olland S, Lin L, Zhong X, Kriz R, Reifenberg EL, Collins-Racie LA, Corcoran C, Freeman B, Zollner R, Marvell T, Vera M, Sum PE, Lavallie ER, Stahl M, Somers W. Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5. Protein Sci. 2008;17(1): 16–21. 46. Shieh HS, Mathis KJ, Williams JM, Hills RL, Wiese JF, Benson TE, Kiefer JR, Marino MH, Carroll JN, Leone JW, Malfait AM, Arner EC, Tortorella MD, Tomasselli A.

A typical furin processing site (Arg-Xaa-Arg/Lys-Arg) is present in all ADAMTS proteases but ADAMTS10 at the junction of the propeptide and catalytic module. ADAMTS10 has a suboptimal (Gly-Leu-Lys-Arg) site at the propeptide–catalytic module junction, but contains additional consensus sites within the propeptide [42]. Whereas propeptide excision was not required for activity of ADAMTS9 and ADAMTS13 [23, 24], it is essential for activity of ADAMTS1, ADAMTS4, ADAMTS5, and ADAMTS15 [38–40, 43]. A structure of the ADAMTS13 catalytic domain is presently unavailable.

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ADAMTS13: Biology and Disease by George M. Rodgers


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