S
Silvia Zorrilla
Researcher at Spanish National Research Council
Publications - 51
Citations - 1231
Silvia Zorrilla is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: FtsZ & Nucleoid. The author has an hindex of 19, co-authored 48 publications receiving 1061 citations. Previous affiliations of Silvia Zorrilla include French Institute of Health and Medical Research & University of Montpellier.
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Journal ArticleDOI
Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly.
Germán Rivas,Asunción López,Jesús Mingorance,Marı́a José Ferrándiz,Silvia Zorrilla,Allen P. Minton,Miguel Vicente,José Manuel Andreu +7 more
TL;DR: It is proposed that these FtsZ oligomers and the polymers formed under assembly conditions share a similar axial interaction between monomers (like in the case of tubulin, the eukaryotic homolog of Ftsz).
Journal ArticleDOI
Molecular basis for group-specific activation of the virulence regulator PlcR by PapR heptapeptides.
Laurent Bouillaut,S. Perchat,Stefan T. Arold,Silvia Zorrilla,L. Slamti,Céline Henry,M. Gohar,Nathalie Declerck,Didier Lereclus +8 more
TL;DR: It is shown that the in vivo active form of PapR is the C-terminal heptapeptide of the precursor, and not the pentapeptides, as previously suggested.
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Bacterial FtsZ protein forms phase‐separated condensates with its nucleoid‐associated inhibitor SlmA
Begoña Monterroso,Silvia Zorrilla,Marta Sobrinos-Sanguino,Miguel Ángel Robles-Ramos,Marina López-Álvarez,William Margolin,Christine D. Keating,Germán Rivas +7 more
TL;DR: It is demonstrated that FtsZ can form crowding‐induced condensates, reminiscent of those observed for eukaryotic proteins, suggesting that phase separation may also play a functional role in the spatiotemporal organization of essential bacterial processes.
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Translational and rotational motions of proteins in a protein crowded environment
TL;DR: A method to estimate local apparent viscosities for the tracer translational and rotational diffusion directly from the bulk viscosity of the concentrated protein solutions is proposed.
Journal ArticleDOI
Protein self-association in crowded protein solutions: a time-resolved fluorescence polarization study
TL;DR: Time‐resolved fluorescence polarization methods described here are expected to be of general applicability to the detection and quantification of crowding effects in a variety of macromolecules of biological relevance.