University of Münster
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Kathrin Schlücking

No current affiliations available for this person. The person is no longer active at the university.

Publications

Protein fragment bimolecular fluorescence complementation analyses for the in vivo study of protein-protein interactions and cellular protein complex localizations
Waadt R., Schlücking K., Schroeder J.I., Kudla J. (2014)
In: Sanchez-Serrano, Jose; Salinas, Julio (eds.), Arabidopsis Protocols. unbekannt / n.a. / unknown.
Research article (book contribution)
Untersuchungen zur Funktion vakuolärer CBL- und NHX-Proteine und der Interaktion von CIPK- mit Rboh-Proteinen aus Arabidopsis thaliana
Schlücking, Kathrin (2013)
(kein Verlag angegeben).
Thesis (doctoral or post-doctoral)
The Calcineurin B-like calcium sensors CBL1 and CBL9 together with their interacting protein kinase CIPK26 regulate the Arabidopsis NADPH oxidase RBOHF.
Drerup MM, Schlücking K, Hashimoto K, Manishankar P, Steinhorst L, Kuchitsu K, Kudla J (2013)
In: Molecular Plant, 6(2).
Research article (journal)
A New β-Estradiol-Inducible Vector Set that Facilitates Easy Construction and Efficient Expression of Transgenes Reveals CBL3-Dependent Cytoplasm to Tonoplast Translocation of CIPK5.
Schlücking K, Edel KH, Köster P, Drerup MM, Eckert C, Steinhorst L, Waadt R, Batistic O, Kudla J (2013)
In: Molecular Plant, 6(6).
Research article (journal)
S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses.
Batistič O, Rehers M, Akerman A, Schlücking K, Steinhorst L, Yalovsky S, Kudla J (2012)
In: Cell Research, 22(7).
Research article (journal)
Show all publications

Doctorates

Untersuchungen zur Funktion vakuolärer CBL‐ und NHX‐Proteine und der Interaktion von CIPK‐ mit Rboh‐Proteinen aus Arabidopsis thaliana
Candidate: Schlücking, Kathrin | Supervisors: Kudla, Jörg; von Schaewen, Antje; Prüfer, Dirk
Period of time: 01/09/2008 - 12/07/2013
Doctoral examination procedure finished at: Doctoral examination procedure at University of Münster