Author

G. Dimchev

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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Cell Biology· 6

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 4 Research Focus:cell type annotation· 4 Approach:experimental assay· 4 Assay:cryo-EM· 2 Research Focus:development & morphogenesis· 2 Assay:imaging· 2 Approach:microscopy & imaging analysis· 2 Organism:mouse· 2

Frequent Co-Authors

K. Rottner· 4 shared F. Faessler· 3 shared F. K. Schur· 3 shared B. Amiri· 2 shared J. Faix· 2 shared M. Falcke· 2 shared V. Dimchev· 2 shared V.-V. Hodirnau· 2 shared

Activity by Year

2020-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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4 shared papersCell Biology

K. Rottner

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Author profile →

6 papers

Recent·Most cited

ArpC5 isoforms regulate Arp2/3 complex-dependent protrusion through differential Ena/VASP positioning

F. Faessler, M. Javoor, J. Datler, H. Doering, F. Hofer, G. Dimchev, V.-V. Hodirnau, K. Rottner, F. K. Schur

The paper investigates how ArpC5 and ArpC5L isoforms regulate cell migration by affecting Arp2/3 complex function and Ena/VASP positioning, linking them to cancer progression.

bioRxiv · Jul 28, 2022Cell Biology

Computational toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET data

G. Dimchev, B. Amiri, F. Faessler, M. Falcke, F. K. Schur

The paper introduces a computational toolbox for semi-automated quantification of filament networks in cryo-ET data to analyze ultrastructural changes in actin filaments under different conditions.

bioRxiv · May 25, 2021Cell Biology

Induced Arp2/3 complex depletion increases FMNL2/3 formin expression and filopodia formation

V. Dimchev, I. Lahmann, S. A. Koestler, F. Kage, G. Dimchev, A. Steffen, T. E. Stradal, F. Vauti, H.-H. Arnold, K. Rottner

This study shows that acute Arp2/3 complex depletion increases FMNL2/3 formin expression and filopodia formation in fibroblasts, despite reduced actin turnover and impaired lamellipodia formation.

bioRxiv · Dec 3, 2020Cell Biology

Novel cryo-electron tomography structure of Arp2/3 complex in cells reveals mechanisms of branch formation

F. Faessler, G. Dimchev, V.-V. Hodirnau, W. Wan, F. K. Schur

The paper presents a cryo-electron tomography structure of the Arp2/3 complex in cells, revealing new insights into branch formation mechanisms.

bioRxiv · Aug 25, 2020Cell Biology

Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation

G. Dimchev, B. Amiri, A. C. Humphries, M. Schaks, V. Dimchev, T. E. B. Stradal, J. Faix, M. Krause, M. Way, M. Falcke, K. Rottner

This study shows that lamellipodin stabilizes protrusions and promotes adhesion formation, enhancing cell migration efficiency.

Journal of Cell Science · Apr 9, 2020Peer-reviewedCell Biology

Loss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion

J. Damiano-Guercio, L. Kurzawa, J. Mueller, M. Nemethova, G. Dimchev, T. Pokrant, S. Bruehmann, J. Linkner, L. Blanchoin, M. Sixt, K. Rottner, J. Faix

This study shows that Ena/VASP proteins promote cell migration by regulating lamellipodium architecture, actin dynamics, and integrin-dependent adhesion.

bioRxiv · Jan 27, 2020Cell Biology