Author

E. Hachani

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· 1 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Organism:bacteria (other)· 1 Organism:E. coli· 1 Assay:fluorescence / live-cell microscopy· 1 Research Focus:protein folding & dynamics· 1 Organism:yeast· 1

Frequent Co-Authors

L. Schmitt· 3 shared A. Kedrov· 2 shared J. Reiners· 2 shared S. H. Smits· 2 shared A. Hoeppner· 1 shared A. Papadopoulos· 1 shared F. Kovacic· 1 shared H. Gohlke· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiophysics

L. Schmitt

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Probing macromolecular crowding at the lipid membrane interface with genetically-encoded sensors

M. Loewe, S. Haensch, E. Hachani, L. Schmitt, S. Weidtkamp-Peters, A. Kedrov

The paper develops a genetically-encoded fluorescence sensor to quantify macromolecular crowding at lipid membrane interfaces, finding that crowding effects depend on factors beyond molecular weight.

bioRxiv · May 1, 2023Biophysics

The periplasmic chaperone Skp prevents misfolding of the secretory lipase A from Pseudomonas aeruginosa

A. Papadopoulos, M. Busch, J. Reiners, E. Hachani, M. Baeumers, L. Schmitt, K.-E. Jaeger, F. Kovacic, S. H. Smits, A. Kedrov

This study shows that Skp prevents misfolding of lipase A in Pseudomonas aeruginosa and facilitates its activation by LipH, with two binding modes identified.

bioRxiv · Mar 1, 2022Biochemistry

A MademoiseLLE domain binding platform links the key RNA transporter to endosomes

S.-K. Devan, S. Schott-Verdugo, K. Muentjes, L. Bismar, J. Reiners, E. Hachani, L. Schmitt, A. Hoeppner, S. H. Smits, H. Gohlke, M. Feldbruegge

The paper identifies MLLE domains in Rrm4 as essential for endosomal attachment, revealing a hierarchical binding platform for mRNA transport.

bioRxiv · Oct 25, 2021Microbiology