Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates*

@inproceedings{BeckerPauly2011ProteomicAR,
  title={Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates*},
  author={Christoph Becker-Pauly and O. De La Barre and Oliver Schilling and Ulrich Auf dem Keller and Anke Ohler and Claudia Broder and Andr{\'e} Sch{\"u}tte and Reinhild Kappelhoff and Walter St{\"o}cker and Christopher M. Overall},
  booktitle={Molecular & cellular proteomics : MCP},
  year={2011}
}
Astacins are secreted and membrane-bound metalloproteases with clear associations to many important pathological and physiological processes. Yet with only a few substrates described their biological roles are enigmatic. Moreover, the lack of knowledge of astacin cleavage site specificities hampers assay and drug development. Using PICS (proteomic identification of protease cleavage site specificity) and TAILS (terminal amine isotopic labeling of substrates) degradomics approaches >3000… CONTINUE READING

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