The molecular arrangement of membrane-bound annexin A2-S100A10 tetramer as revealed by scanning force microscopy

2004 | journal article; research paper. A publication with affiliation to the University of Göttingen.

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​The molecular arrangement of membrane-bound annexin A2-S100A10 tetramer as revealed by scanning force microscopy​
Menke, M.; Ross, M.; Gerke, V. & Steinem, C. ​ (2004) 
ChemBioChem, 5(7) pp. 1003​-1006​.​ DOI: https://doi.org/10.1002/cbic.200400004 

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Authors
Menke, Manuela; Ross, Michaela; Gerke, Volker; Steinem, Claudia 
Abstract
The first step in membrane aggregation mediated by the annexin A2-S100A10 heterotetrameric complex (annexin A2t) has been unraveled by in situ scanning force microscopy. It has been shown unambiguously that annexin A2t binds to solid-supported lipid bilayers simultaneously with both annexin A2 subunits.
Issue Date
2004
Journal
ChemBioChem 
ISSN
1439-4227
Language
English

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