Author

C. Marchand

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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Plant Biology· 2 Ecology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:Arabidopsis· 2 Research Focus:protein folding & dynamics· 2 Research Focus:ecology & biodiversity· 1 Assay:imaging· 1 Assay:protein structure· 1 Assay:proteomics· 1 Organism:zebrafish· 1

Frequent Co-Authors

G. Falini· 2 shared M. Zaffagnini· 2 shared P. Trost· 2 shared S. Fermani· 2 shared S. Lemaire· 2 shared A. Del Giudice· 1 shared A. Dubuc· 1 shared D. Genovese· 1 shared

Activity by Year

2019-2019 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

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2 shared papersPlant Biology

G. Falini

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3 papers

Recent·Most cited

Patterns of fish utilisation in a tropical Indo-Pacific mangrove-coral seascape, New Caledonia

A. Dubuc, N. Waltham, R. Baker, C. Marchand, M. Sheaves

This study examines fish utilization patterns in a mangrove-coral seascape using underwater video cameras, revealing differences in fish assemblages between mangrove edge and interior habitats.

bioRxiv · Mar 31, 2019Ecology

Arabidopsis and Chlamydomonas phosphoribulokinase crystal structures complete the redox structural proteome of the Calvin-Benson cycle

L. Gurrieri, A. Del Giudice, N. Demitri, G. Falini, N. V. Pavel, M. Zaffagnini, M. Polentarutti, P. Crozet, C. Marchand, J. Henri, P. Trost, S. Lemaire, F. Sparla, S. Fermani

This paper determines the crystal structures of phosphoribulokinase (PRK) from Arabidopsis and Chlamydomonas, revealing structural features related to TRX regulation in the Calvin-Benson cycle.

bioRxiv · Feb 18, 2019Plant Biology

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