Author

C. Blancard

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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Microbiology· 3 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Assay:proteomics· 2 Organism:bacteria (other)· 1 Organism:fungi (other)· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

B. Salin· 4 shared A. Daskalov· 2 shared E. Tetaud· 2 shared M. Rojo· 2 shared S. Duvezin-Caubet· 2 shared S. J. Saupe· 2 shared T. Bardin· 2 shared V. Coustou· 2 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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4 shared papersMicrobiology

B. Salin

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

A member of a new dynamin superfamily modulates mitochondrial membrane branching in Trypanosoma brucei

C. A. Morel, C. Asencio, D. Moreira, C. Blancard, B. Salin, E. Gontier, S. Duvezin-Caubet, M. Rojo, F. Bringaud, E. Tetaud

The paper identifies a novel dynamin superfamily protein in Trypanosoma brucei that modulates mitochondrial membrane branching through GTPase-dependent mechanisms.

bioRxiv · Jun 28, 2023 · PreprintMicrobiology

TMEM70 forms oligomeric scaffolds within mitochondrial cristae promoting in situ assembly of mammalian ATP synthase proton channel

H. Bahri, J. Buratto, M. Rojo, J. P. Dompierre, B. Salin, C. Blancard, S. Cuvellier, M. Rose, A. Ben Ammar Elgaaied, E. Tetaud, J.-P. di Rago, A. Devin, S. Duvezin-Caubet

This study shows TMEM70 forms oligomers that scaffold the assembly of the ATP synthase c-ring within mitochondrial cristae.

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · Apr 1, 2021Peer-reviewedCell Biology

Partial prion cross-seeding between fungal and mammalian amyloid signaling motifs

T. Bardin, A. Daskalov, S. Barrouilhet, A. Granger-Farbos, B. Salin, C. Blancard, S. J. Saupe, V. Coustou

The paper identifies a third amyloid signaling pathway in Podospora anserina involving a PP-motif that forms prions and partially cross-seeds with human RHIM prions, suggesting evolutionary conservation of amyloid-based cell-death mechanisms.

bioRxiv · Jul 22, 2020Microbiology

Identification of NLR-associated amyloid signaling motifs in filamentous bacteria

W. Dyrka, V. Coustou, A. Daskalov, A. Lends, T. Bardin, M. Berbon, B. Kauffmann, C. Blancard, B. Salin, A. Loquet, S. J. Saupe

The paper identifies bacterial amyloid signaling motifs related to fungal and mammalian motifs and shows they form prion-like structures in fungi and in vitro.

bioRxiv · Jan 6, 2020 · PreprintMicrobiology