Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors
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Title
Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors
Authors
Keywords
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Journal
Nature Chemistry
Volume 9, Issue 9, Pages 909-917
Publisher
Springer Nature
Online
2017-03-21
DOI
10.1038/nchem.2744
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Note: Only part of the references are listed.- Homogeneous Sulfopeptides and Sulfoproteins: Synthetic Approaches and Applications To Characterize the Effects of Tyrosine Sulfation on Biochemical Function
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- Crystal Structure of Thrombin in Complex with S-Variegin: Insights of a Novel Mechanism of Inhibition and Design of Tunable Thrombin Inhibitors
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- Leech-Derived Thrombin Inhibitors: From Structures to Mechanisms to Clinical Applications
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- Regulation of Chemokine Recognition by Site-Specific Tyrosine Sulfation of Receptor Peptides
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- Isolation, Cloning and Structural Characterisation of Boophilin, a Multifunctional Kunitz-Type Proteinase Inhibitor from the Cattle Tick
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