Author

E. Wahle

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:multiome· 4 Research Focus:chromatin & epigenetic regulation· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Organism:Drosophila· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

C. Ihling· 3 shared A. Sinz· 2 shared C. Rammelt· 2 shared A. Graber· 1 shared C. Temme· 1 shared C. Tueting· 1 shared C. Tüting· 1 shared E. Conti· 1 shared

Activity by Year

2017-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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3 shared papersBiochemistry

C. Ihling

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4 papers

Recent·Most cited

RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system

F. Pekovic, C. Rammelt, J. Kubikova, J. Metz, M. Jeske, E. Wahle

This study reconstitutes the Drosophila Smaug-dependent deadenylation of nanos mRNA in vitro, showing Smaug's role in recruiting CCR4-NOT complexes and identifying key subunits and interactions involved.

bioRxiv · May 11, 2022Biochemistry

Reconstitution of 3'-processing of mammalian pre-mRNA reveals a central role of RBBP6

M. Schmidt, F. Kluge, F. Sandmeir, U. Kühn, P. Schäfer, C. Tüting, C. Ihling, E. Conti, E. Wahle

The paper reconstitutes the 3'-processing of mammalian pre-mRNA and identifies essential and stimulatory proteins, highlighting RBBP6's role in activating CPSF73.

bioRxiv · Nov 2, 2021 · PreprintBiochemistry

Reconstitution of mammalian Cleavage Factor II involved in 3’ processing of mRNA precursors

P. Schaefer, C. Tueting, L. Schoenemann, U. Kuehn, T. Treiber, N. Treiber, C. Ihling, A. Graber, W. Keller, G. Meister, A. Sinz, E. Wahle

This study reconstitutes mammalian Cleavage Factor II as a heterodimer of hPcf11 and hClp1, showing its activity in RNA cleavage and RNA binding preferences.

bioRxiv · Aug 16, 2018Biochemistry

Translational Repression Of The Drosophila nanos mRNA Involves The RNA Helicase Belle And RNA Coating By Me31B And Trailer hitch

M. Gotze, J. Dufourt, C. Ihling, C. Rammelt, S. Pierson, N. Sambrani, C. Temme, A. Sinz, M. Simonelig, E. Wahle

The paper identifies Belle as a novel component of the SRE-dependent repressor complex that contributes to translational repression of nanos mRNA in Drosophila.

bioRxiv · May 24, 2017Biochemistry