Author

G. Venturoli

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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Biophysics· 1 Physiology· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Organism:Arabidopsis· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:development & morphogenesis· 1 Research Focus:host-pathogen & immune response· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

M. Malferrari· 3 shared A. S. Holehouse· 2 shared E. W. Martin· 2 shared F. Francia· 2 shared F. Yu· 2 shared S. Biswas· 2 shared S. KC· 2 shared S. Sukenik· 2 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersPhysiology

M. Malferrari

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Labile assembly of a tardigrade protein induces biostasis

S. Sanchez-Martinez, K. Nguyen, S. Biswas, V. Nicholson, A. V. Romanyuk, J. F. Ramirez, S. KC, A. Akter, C. Childs, E. T. Usher, G. M. Ginell, F. Yu, E. Gollub, M. Malferrari, F. Francia, , T. C. Boothby

This study identifies a mechanism by which tardigrade CAHS D proteins form gels to protect cells during desiccation, showing that gelation reduces molecular motion and metabolic activity, with reversible effects.

bioRxiv · Jun 30, 2023Physiology

Tardigrade CAHS Proteins Act as Molecular Swiss Army Knives to Mediate Desiccation Tolerance Through Multiple Mechanisms

C. S. Hesgrove, K. H. Nguyen, S. Biswas, C. A. Childs, S. KC, B. X. Medina, V. Alvarado, S. Sukenik, F. Yu, M. Malferrari, F. Francia, G. Venturoli, E. W. Martin, A. S. Holehouse, T. C. Boothby

This study identifies CAHS D as a tardigrade protein that protects against desiccation through multiple mechanisms involving water coordination and slowed molecular motion.

bioRxiv · Aug 16, 2021 · PreprintBiophysics

Glutathionylation primes soluble GAPDH for late collapse into insoluble aggregates

M. Zaffagnini, C. Marchand, M. Malferrari, S. Murail, S. Bonacchi, D. Genovese, M. Montalti, G. Venturoli, G. Falini, M. Baaden, S. Lemaire, S. Fermani, P. Trost

This study shows that glutathionylation of AtGAPC1 in Arabidopsis primes it for aggregation, leading to insoluble, inactive protein chains.

bioRxiv · Feb 15, 2019Plant Biology