Literature for peptidase M12.208: ADAM8 peptidase

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2019
1. Schlomann,U., Dorzweiler,K., Nuti,E., Tuccinardi,T., Rossello,A. and Bartsch,J.W.
   Metalloprotease inhibitor profiles of human ADAM8 in vitro and in cell-based assays
   Biol Chem400, 801-810. PubMed  Europe PubMed DOI  I
2012
2. Hall,T., Shieh,H.S., Day,J.E., Caspers,N., Chrencik,J.E., Williams,J.M., Pegg,L.E., Pauley,A.M., Moon,A.F., Krahn,J.M., Fischer,D.H., Kiefer,J.R., Tomasselli,A.G. and Zack,M.D.
   Structure of human ADAM-8 catalytic domain complexed with batimastat
   Acta Crystallogr Sect F Struct Biol Cryst Commun68, 616-621. PubMed  Europe PubMed DOI  S  I
2007
3. Moss,M.L. and Rasmussen,F.H.
   Fluorescent substrates for the proteinases ADAM17, ADAM10, ADAM8, and ADAM12 useful for high-throughput inhibitor screening
   Anal Biochem366, 144-148. PubMed  Europe PubMed DOI  A  I
2004
4. [YEAR:16-4-2004]Naus,S., Richter,M., Wildeboer,D., Moss,M., Schachner,M. and Bartsch,J.W.
   Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death
   J Biol Chem279, 16083-16090. PubMed  Europe PubMed DOI  I
2002
5. [YEAR:13-12-2002]Schlomann,U., Wildeboer,D., Webster,A., Antropova,O., Zeuschner,D., Knight,C.G., Docherty,A.J., Lambert,M., Skelton,L., Jockusch,H. and Bartsch,J.W.
   The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion
   J Biol Chem277, 48210-48219. PubMed  Europe PubMed DOI  I