Author

G. Rivas

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 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 6 Approach:experimental assay· 6 Organism:E. coli· 4 Research Focus:cell type annotation· 2 Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:development & morphogenesis· 1 Assay:electronic health records· 1

Frequent Co-Authors

C. Alfonso· 4 shared M. Sobrinos-Sanguino· 3 shared A. Merino-Salomon· 2 shared B. Monterroso· 2 shared M. A. Robles-Ramos· 2 shared M. Jimenez· 2 shared P. Schwille· 2 shared S. Zorrilla· 2 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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4 shared papersBiochemistry

C. Alfonso

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution

A. Merino-Salomon, J. Schneider, L. Babl, J.-H. Krohn, M. Sobrinos-Sanguino, T. Schäfer, J. R. Luque-Ortega, C. Alfonso, M. Jimenez, M. Jasnin, P. Schwille, G. Rivas

This study shows ZapD crosslinks FtsZ filaments into toroidal structures, revealing how crosslinking density and geometry enable Z ring formation in bacteria.

bioRxiv · Jan 12, 2023Biochemistry

Assembly of bacterial cell division protein FtsZ into dynamic biomolecular condensates

M. A. Robles-Ramos, S. Zorrilla, C. Alfonso, W. Margolin, G. Rivas, B. Monterroso

This study shows FtsZ can form dynamic biomolecular condensates independently of SlmA, suggesting a broader role for phase separation in bacterial cell division.

bioRxiv · Aug 27, 2020Biochemistry

Bidirectional FtsZ filament treadmilling transforms lipid membranes via torsional stress

D. A. Ramirez-Diaz, A. Merino-Salomon, F. Meyer, M. Heymann, G. Rivas, M. Bramkamp, P. Schwille

This study shows FtsZ filaments generate forces via bidirectional treadmilling, causing lipid membrane deformation and constriction in vitro.

bioRxiv · Jun 12, 2020 · PreprintBiophysics

FtsZ assembles the bacterial cell division machinery by a diffusion-and-capture mechanism

N. Baranova, P. Radler, V. M. Hernandez-Rocamora, C. Alfonso, M. Lopez-Pelegrin, G. Rivas, W. Vollmer, M. Loose

The paper shows FtsZ treadmilling recruits divisome proteins via diffusion-and-capture, explaining how the Z-ring dynamically assembles the bacterial cell division machinery.

bioRxiv · Dec 3, 2018Biochemistry

The bacterial DNA binding protein MatP involved in linking the nucleoid terminal domain to the divisome at midcell interacts with lipid membranes

B. Monterroso, S. Zorrilla, M. Sobrinos-Sanguino, M. A. Robles-Ramos, C. Alfonso, B. Söderström, N. Y. Meiresonne, J. Verheul, T. den Blaauwen, G. Rivas

The paper shows MatP interacts with lipid membranes in E. coli during cell division, suggesting lipid binding modulates its localization and function without requiring DNA.

bioRxiv · Sep 27, 2018Biochemistry

Escherichia coli ZipA organizes FtsZ polymers into dynamic ring-like protofilament structures

W. Margolin, M. Krupka, M. Sobrinos-Sanguino, M. Jimenez, G. Rivas

This paper shows ZipA does not reduce FtsZ dynamics by bundling but instead allows dynamic FtsZ vortices at low surface densities on lipid membranes.

bioRxiv · May 14, 2018Microbiology