Massively parallel enzyme kinetics reveals the substrate recognition landscape of the metalloprotease ADAMTS13.

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第一作者： Colin A,Kretz

第一单位： Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109;

作者： Colin A,Kretz ^[1] ; Manhong,Dai ^[2] ; Onuralp,Soylemez ^[3] ; Andrew,Yee ^[1] ; Karl C,Desch ^[4] ; David,Siemieniak ^[5] ; Kärt,Tomberg ^[6] ; Fyodor A,Kondrashov ^[7] ; Fan,Meng ^[2] ; David,Ginsburg ^[8]

作者单位： Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109; ^[1] Department of Psychiatry and Molecular and Behavioral Neuroscience Institute, University of Michigan, Ann Arbor, MI 48109; ^[2] Bioinformatics and Genomics Programme, Centre for Genomic Regulation, Barcelona, Spain 08003; Universitat Pompeu Fabra, Barcelona, Spain 08003; ^[3] Department of Pediatrics, University of Michigan Medical School, Ann Arbor, MI 48109; ^[4] Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109; Howard Hughes Medical Institute, Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109; ^[5] Department of Human Genetics, University of Michigan Medical School, Ann Arbor, MI 48109; ^[6] Bioinformatics and Genomics Programme, Centre for Genomic Regulation, Barcelona, Spain 08003; Universitat Pompeu Fabra, Barcelona, Spain 08003; Institució Catalana de Recerca i Estudis Avançats, Barcelona, Spain 08003; ^[7] Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109; Department of Pediatrics, University of Michigan Medical School, Ann Arbor, MI 48109; Howard Hughes Medical Institute, Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109; Department of Human Genetics, University of Michigan Medical School, Ann Arbor, MI 48109; Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109 ginsburg@umich.edu. ^[8]

关键词 ADAMTS13 high-throughput sequencing phage display protease von Willebrand factor