H. Simader

Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes

Dietrich Suck, D. Suck, G. Simos, 2006, Nucleic acids research.

Dipeptidyl nitrile inhibitors of Cathepsin L.

S. Steinbacher, Matthew Grist, M. Augustin, 2009, Bioorganic & medicinal chemistry letters.

Molecular determinants of the yeast Arc1p-aminoacyl-tRNA synthetase complex assembly.

D. Suck, G. Panayotou, G. Simos, 2007, Journal of molecular biology.

Design of selective Cathepsin inhibitors.

S. Steinbacher, M. Augustin, Galith Karoutchi, 2009, Bioorganic & medicinal chemistry letters.

Microtubule-associated Protein 1S, a Short and Ubiquitously Expressed Member of the Microtubule-associated Protein 1 Family*

H. Simader, F. Propst, A. Trančíková, 2005, Journal of Biological Chemistry.

Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold.

D. Suck, H. Simader, M. Hothorn, 2006, Acta crystallographica. Section D, Biological crystallography.

Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs

Adam Round, Dietrich Suck, Dmitri Svergun, 2012, Nucleic acids research.

Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs

D. Suck, D. Svergun, C. Koehler, 2012, Nucleic acids research.

Expression, purification, crystallization and preliminary phasing of the heteromerization domain of the tRNA-export and aminoacylation cofactor Arc1p from yeast.

D. Suck, H. Simader, 2006, Acta crystallographica. Section F, Structural biology and crystallization communications.