Minna Groenning

Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status

Minna Groenning · Journal of Chemical Biology · 2009 · 638 citations · Full text

Proteinlipid Interaction, Biochemistry, Protein Folding +8

A Helical Structural Nucleus Is the Primary Elongating Unit of Insulin Amyloid Fibrils

Bente Vestergaard, Minna Groenning, Manfred Roessle et al. · PLoS Biology · 2007 · 254 citations · Full text

Protein Assembly, Helical Structural Nucleus, Molecular Biology +17

Study on the binding of Thioflavin T to β-sheet-rich and non-β-sheet cavities

Minna Groenning, Lars Olsen, Marco van de Weert et al. · Journal of Structural Biology · 2007 · 249 citations

Medicine, Thioflavin T, Non-β-sheet Cavities +2

Binding mode of Thioflavin T in insulin amyloid fibrils

Minna Groenning, Mathias Norrman, James M. Flink et al. · Journal of Structural Biology · 2007 · 236 citations

Proteinlipid Interaction, Biochemistry, Protein Folding +3

Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation

Vito Foderà, Fabio Librizzi, Minna Groenning et al. · The Journal of Physical Chemistry B · 2008 · 169 citations

Secondary Nucleation, Protein Assembly, Biochemistry +13