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Johannes A. Eble

Institute of Physiological Chemistry and Pathobiochemistry

University of Münster

Waldeyerstrasse 15

48149

Germany

[email]@uni-muenster.de

Name/email consistency: high

 
 
 
 
 
 
 

Affiliations

  • Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Waldeyerstrasse 15, 48149, Germany. 2002 - 2006
  • Institut für Physiologische Chemie und Pathobiochemie, Waldeyerstrasse 15 and the Institut für Physikalische Chemie, Schlossplatz 7, Universität Münster, Germany. 2001
  • Dana Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA. 1998

References

  1. Integrins in cancer treatment. Eble, J.A., Haier, J. Curr. Cancer. Drug. Targets (2006) [Pubmed]
  2. Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-terminal domains. Eble, J.A., Kassner, A., Niland, S., Mörgelin, M., Grifka, J., Grässel, S. J. Biol. Chem. (2006) [Pubmed]
  3. Collagen-binding integrins as pharmaceutical targets. Eble, J.A. Curr. Pharm. Des. (2005) [Pubmed]
  4. Vipera lebetina venom contains two disintegrins inhibiting laminin-binding beta1 integrins. Eble, J.A., Bruckner, P., Mayer, U. J. Biol. Chem. (2003) [Pubmed]
  5. The alpha2beta1 integrin inhibitor rhodocetin binds to the A-domain of the integrin alpha2 subunit proximal to the collagen-binding site. Eble, J.A., Tuckwell, D.S. Biochem. J. (2003) [Pubmed]
  6. Rhodocetin antagonizes stromal tumor invasion in vitro and other alpha2beta1 integrin-mediated cell functions. Eble, J.A., Niland, S., Dennes, A., Schmidt-Hederich, A., Bruckner, P., Brunner, G. Matrix Biol. (2002) [Pubmed]
  7. alpha 2beta 1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen. Eble, J.A., Beermann, B., Hinz, H.J., Schmidt-Hederich, A. J. Biol. Chem. (2001) [Pubmed]
  8. The molecular basis of integrin-extracellular matrix interactions. Eble, J.A. Osteoarthr. Cartil. (2001) [Pubmed]
  9. Recombinant soluble human alpha 3 beta 1 integrin: purification, processing, regulation, and specific binding to laminin-5 and invasin in a mutually exclusive manner. Eble, J.A., Wucherpfennig, K.W., Gauthier, L., Dersch, P., Krukonis, E., Isberg, R.R., Hemler, M.E. Biochemistry (1998) [Pubmed]
 
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