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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] | | [https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Proline-based trypsin inhibitors occupying the S1-S2-S1' region were identified by an HTS screening campaign. It was discovered that truncation of the P1' moiety and appropriate extension into the S4 region led to highly potent trypsin inhibitors with excellent selectivity against related serine proteases and a favorable hERG profile.
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| Trypsin inhibitors for the treatment of pancreatitis.,Brandl T, Simic O, Skaanderup PR, Namoto K, Berst F, Ehrhardt C, Schiering N, Mueller I, Woelcke J Bioorg Med Chem Lett. 2016 Jul 17. pii: S0960-894X(16)30742-9. doi:, 10.1016/j.bmcl.2016.07.029. PMID:27476144<ref>PMID:27476144</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5lh4" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Trypsin 3D structures|Trypsin 3D structures]] | | *[[Trypsin 3D structures|Trypsin 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
