Characterization of annexin A1 glycan binding reveals binding to highly 
sulfated glycans with preference for highly sulfated heparan sulfate and heparin

Horlacher, T.; Noti, C.; de Paz, J. L.; Bindschädler, P.; Hecht, M. L.; Smith, D. F.; Fukuda, M. N.; Seeberger, Peter H.

doi:dx.doi.org/10.1021/bi101121a

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Characterization of annexin A1 glycan binding reveals binding to highly sulfated glycans with preference for highly sulfated heparan sulfate and heparin

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Horlacher, T.
Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Hecht, M. L.
Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Seeberger, Peter H.
Peter H. Seeberger - Vaccine Development, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Horlacher, T., Noti, C., de Paz, J. L., Bindschädler, P., Hecht, M. L., Smith, D. F., et al. (2011). Characterization of annexin A1 glycan binding reveals binding to highly sulfated glycans with preference for highly sulfated heparan sulfate and heparin. Biochemistry, 50(13), 2650-2659. doi:dx.doi.org/10.1021/bi101121a.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-4797-E

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