Author

S. Heber

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· 2 Cell Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell type annotation· 3 Organism:Drosophila· 3 Assay:metagenomics· 2 Research Focus:cell signaling & trafficking· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1 Organism:yeast· 1

Frequent Co-Authors

A. Ephrussi· 3 shared D. Niessing· 2 shared I. Gaspar· 2 shared M. A. McClintock· 2 shared S. L. Bullock· 2 shared A. Niedner· 1 shared B. Simon· 1 shared J. Günther· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiochemistry

A. Ephrussi

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4 papers

Recent·Most cited

A consensus motif in ASH1 and further transcripts unifies several RNA motifs required for interaction with the She2p/She3p transport machinery and mRNA localization in yeast

M. Seiler, A. Niedner, S. Heber, M. Feldbruegge, R.-P. Jansen, D. Niessing, K. Zarnack

The paper identifies a consensus motif for She2p/3p recognition sites in yeast RNA, showing that spatial arrangement of sequence features is more important than sequence order for function.

bioRxiv · Mar 10, 2024 · PreprintCell Biology

Tropomyosin 1-I/C co-ordinates kinesin-1 and dynein motors during oskar mRNA transport

S. Heber, M. A. McClintock, B. Simon, J. Hennig, S. L. Bullock, A. Ephrussi

This study shows Tm1-I/C coordinates kinesin-1 and dynein during oskar mRNA transport by inhibiting kinesin-1 until it is needed in the oocyte.

bioRxiv · Oct 26, 2022 · PreprintBiochemistry

An RNA-based feed-forward mechanism ensures motor switching in oskar mRNA transport

I. Gaspar, L. J. Phea, M. A. McClintock, S. Heber, S. L. Bullock, A. Ephrussi

The paper shows that Staufen and Egl interact to switch motor proteins during oskar mRNA transport in Drosophila oocytes, enabling proper localization.

bioRxiv · Apr 24, 2021 · PreprintCell Biology

Staufen2 mediated RNA recognition and localization requires combinatorial action of multiple domains

S. Heber, I. Gaspar, J.-N. Tants, J. Günther, S. M. Fernandez Moya, R. Janowski, A. Ephrussi, M. Sattler, D. Niessing

This study shows that dsRBDs 1-2 of mStau2 are essential for mRNA recognition and function, as demonstrated by rescue experiments in Drosophila oocytes.

bioRxiv · Feb 1, 2019Biochemistry