Selected Publications

Find all our publications here.

Selected relevant publications from previous work:

Korn SM, Ulshöfer C, Schneider T, Schlundt A. Structures and target RNA preferences of the multi-domain RNA-binding protein family of IGF2BPs: An overview. Review. Structure. 2021May 21 (online).

Available at: https://doi.org/10.1016/j.str.2021.05.001


Altincekic N, Korn SM, Qureshi NS, Dujardin M, Ninot-Pedrosa M, …, Böckmann A*, …, Schwalbe H*, …,  Hengesbach M*, Schlundt A*. Large-scale recombinant production of the SARS-CoV-2 proteome for high-throughput and structural biology applications.

Front Mol. Biosci. 2021 May 10 (online).

Available at: https://doi.org/10.3389/fmolb.2021.653148


Wang Y, Kirkpatrick J, Zur Lage S, Korn SM, Neißner K, Schwalbe H, Schlundt A, Carlomagno T. 1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein).

Biomol NMR Assign. 2021 Mar 26:1-9.

Available at: https://doi.org/10.1007/s12104-021-10019-6


F Dudás E, Puglisi R, Korn SM, Alfano C, Bellone ML, Piaz FD, Kelly G, Monaca E, Schlundt A, Schwalbe H, Pastore A. Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9.

Biomol NMR Assign. 2021 Mar 23:1-7.

Available at: https://doi.org/10.1007/s12104-021-10011-0


Korn SM, Lambertz R, Fürtig B, Hengesbach M, Löhr F, Richter C, Schwalbe H, Weigand JE, Wöhnert J, Schlundt A. 1H, 13C, and 15N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein.

Biomol NMR Assign. 2021 Apr;15(1):129-135.

Available at: https://doi.org/10.1007/s12104-020-09995-y


Korn SM, Dhamotharan K, Fürtig B, Hengesbach M, Löhr F, Qureshi NS, Richter C, Saxena K, Schwalbe H, Tants JN, Weigand JE, Wöhnert J, Schlundt A. 1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e.

Biomol NMR Assign. 2020 Oct;14(2):329-333.

Available at: https://doi.org/10.1007/s12104-020-09971-6


Wacker A, Weigand JE, Akabayov SR, Altincekic N, Bains JK, Banijamali E, Binas O, Castillo-Martinez J, Cetiner E, Ceylan B, Chiu LY, Davila-Calderon J, Dhamotharan K, Duchardt-Ferner E, Ferner J, Frydman L, Fürtig B, Gallego J, Grün JT, Hacker C, Haddad C, Hähnke M, Hengesbach M, Hiller F, Hohmann KF, Hymon D, de Jesus V, Jonker H, Keller H, Knezic B, Landgraf T, Löhr F, Luo L, Mertinkus KR, Muhs C, Novakovic M, Oxenfarth A, Palomino-Schätzlein M, Petzold K, Peter SA, Pyper DJ, Qureshi NS, Riad M, Richter C, Saxena K, Schamber T, Scherf T, Schlagnitweit J, Schlundt A, Schnieders R, Schwalbe H, Simba-Lahuasi A, Sreeramulu S, Stirnal E, Sudakov A, Tants JN, Tolbert BS, Vögele J, Weiß L, Wirmer-Bartoschek J, Wirtz Martin MA, Wöhnert J, Zetzsche H. Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy.

Nucl. Acid. Res. 2020 Dec 16;48(22):12415-12435.

Available at: https://doi.org/10.1093/nar/gkaa1013


Binas O, Tants JN, Peter S, Janowski R, Davydova E, Braun J, Niessing D,Schwalbe H, Weigand J*, Schlundt A*. Structural basis for the recognition of transiently structured AU-rich elements by Roquin.

Nucl. Acid. Res. 2020 Jul 27;48(13):7385-7403

Available at: https://doi.org/10.1093/nar/gkaa465


LingarajuM, Johnsen D, Schlundt A, Langer LM, Basquin J, Sattler M, Heick Jensen T, Falk S, Conti E. The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs.

Nat. Commun. 2019 Jul 29;10(1):3393.

Available at: https://doi.org/10.1038/s41467-019-11339-x

Schneider T, Hung LH, Aziz M, Wilmen A, Thaum S, Wagner J, Janowski R, Müller S, Hüttelmaier S, Niessing D, Sattler M, Schlundt A*, BindereifA*. Combinatorial recognition of clustered RNA elements by the multidomain RNA-binding protein IMP3.

Nat. Commun. 2019 May 22;10(1):2266.

Available at: https://doi.org/ 10.1038/s41467-019-09769-8

Essig K, Kronbeck N, Guimaraes JC, Lohs C, Schlundt A, Hoffmann A, Behrens G, Brenner S, Kowalska J, Lopez-Rodriguez C, Jemielity J, Holtmann H, Reiche K, Hackermüller J, Sattler M, Zavolan M, Heissmeyer V. Roquin targets mRNAs in a 3′-UTR-specific manner by different modes of regulation.

Nat. Commun. 2018 Sep 19;9(1):3810.

Available at: https://doi.org/10.1038/s41467-018-06184-3

Schlundt A, Buchner S, Janowski R, Heydenreich T, Heermann R, Lassak J, Geerlof A, Stehle R, Niessing D, Jung K, Sattler M. Structure-function analysis of the DNA-binding domain of a transmembrane transcriptional activator.

Sci. Rep. 2017 Apr 21; 1051.

Available at: https://doi.org/10.1038/s41598-017-01031-9

Schlundt A, Tants J, Sattler M. Integrated structural biology to unravel mechanisms of RNA-protein recognition. Review

Methods. 2017 Mar 16. pii: S1046-2023(17)30120-2.

Available at: https://doi.org/10.1016/j.ymeth.2017.03.015.

Edelmann FT, Schlundt A, Heym RG, Jenner A, Niedner A, Syed MI, Paillart J, Stehle R, Janowski R, Sattler M, Jansen R, Niessing D. Molecular architecture and dynamics of RNA recognition by an mRNA-transport complex.

Nat. Struct. Mol. Biol. 2017 Feb;24(2):152-161.

Available at: https://doi.org/10.1038/nsmb.3351

Schlundt A*, Niessing D, Heissmeyer V, Sattler M*. RNA recognition by Roquin in posttranscriptional gene regulation. Review.

Wiley Interdiscipl. Rev. RNA. 2016 Jul;7(4):455-69.

Available at: https://doi.org/10.1002/wrna.1333

Janowski R*, Heinz GA*, Schlundt A*, Wommelsdorf N, Brenner S, Gruber AR, Blank M, Buch T, Buhmann R, Zavolan M, Niessing D, Heissmeyer V, Sattler M. Roquin recognizes a non-canonical hexaloop structure in the 3'-UTR of Ox40.

Nat. Commun. 2016 Mar 24;7:11032.

Available at: https://doi.org/10.1038/ncomms11032

Buchner S, Schlundt A, Lassak J, Sattler M, Jung K. Structural and Functional Analysis of the Signal-Transducing Linker in the pH-Responsive One-Component System CadC of Escherichia coli.

J. Mol. Biol. 2015 Jul 31;427(15):2548-61.

Available at: https://doi.org/10.1016/j.jmb.2015.05.001

SchlundtA*, Heinz GA*, Janowski R*, Geerlof A, Stehle R, Heissmeyer V, Niessing D, Sattler M. Structural basis for RNA recognition in roquin-mediated post-transcriptional gene regulation.

Nat.Struct. Mol. Biol. 2014 Aug;21(8):671-8.

Available at: https://doi.org/10.1038/nsmb.2855

*equal contribution or corresponding authorship

Kontakt

Dr. Andreas Schlundt
Biozentrum, Campus Riedberg
Building N250, Room 101
Max-von-Laue-Str. 9
60438 Frankfurt am Main

T +49 69 798-29699
F +49 69 798-29527
E schlundt@bio.uni-frankfurt.de