L.B. Gee, V. Pelmenschikov, C. Mons, N. Mishra, H. Wang, Y. Yoda, K. Tamasaku, M.-P. Golinelli-Cohen, S. P. Cramer. NRVS and DFT of MitoNEET – Understanding the special vibrational structure of a [2Fe-2S] cluster with (Cys)3(His)1 ligation. Biochemistry (2021) 60, 2419-2424. DOI: 10.1021/acs.biochem.1c00252

E. Lebigot, M. Schiff, M.-P. Golinelli-Cohen. A review of Multiple Mitochondrial Dysfunction Syndromes, syndromes associated with defective Fe-S protein maturation. Biomedicines (2021) 9, 989. DOI: 10.3390/biomedicines9080989

R. Chanet, D. Baille, M. P. Golinelli-Cohen, S. Riquier, O. Guittet, M. Lepoivre, M. E. Huang, L. Vernis. (2021) Fe-S coordination defects in the replicative DNA polymerase delta cause deleterious DNA replication in vivo and subsequent DNA damage in the yeast Saccharomyces cerevisiae, G3 (Bethesda). DOI: 10.1093/g3journal/jkab124

A. Antoine, A. Bourouis, M. Winder Bottelli, M. Lepoivre. (2021) RREB1 integrates TGF-beta and RAS signals to drive cell-dependent epithelial-mesenchymal transition, Medecine sciences : M/S 37, 408-411. DOI: 10.1051/medsci/2021044

M. Salameh, S. Riquier, O. Guittet, M.-E. Huang, L. Vernis, M. Lepoivre, M.-P. Golinelli-Cohen, New insights of the NEET protein CISD2 reveals distinct features compared to its close mitochondrial homolog mitoNEET. Biomedicines (2021), 9, 384. DOI: 10.3390/biomedicines9040384.

B. Gaillard, C. Juarez-Krieguer, M.-P. Golinelli-Cohen. MDM2 favorise la mort cellulaire en affectant la bioénergétique mitochondriale. Médecine/Sciences (2021) 37, 397-399. https://doi.org/10.1051/medsci/2021040

P. Mounkoro, T. Michel, M.-P. Golinelli-Cohen, S. Blandin, E. Davioud-Charvet, B. Meunier. A role for the succinate dehydrogenase in the mode of action of the redox-active antimalarial drug, plasmodione. Free Rad. Biol. Med. (2021) 162, 533-541. DOI: 10.1016/j.freeradbiomed.2020.11.010.

Lebigot, M. Hully, L. Amazit, P. Gaignard, T. Michel, M. Rio, M. Lombès, P. Thérond, A. Boutron, M.-P. Golinelli-Cohen..Expanding the Phenotype of Mitochondrial Disease: Novel Pathogenic Variant in ISCA1 Leading to Instability of the Iron-Sulfur Cluster in the Protein. Mitochondrion, (2020) 52, 75-82. DOI: 10.1016/j.mito.2020.02.008.

A. Blanchard, C. Gora, M.-P. Golinelli-Cohen. La protéine Fe-S NfuA, un nouvel acteur essentiel dans la virulence de Pseudomonas aeruginosa. Médecine/Sciences (2020) 36, 174-176. DOI: 10.1051/medsci/2020018.

Levy, E., Jaffrezic, F., Laloe, D., Rezaei, H., Huang, M. E., Beringue, V., Martin, D. & Vernis, L. (2020). « PiQSARS: A pipeline for quantitative and statistical analyses of ratiometric fluorescent biosensors. » MethodsX. 7, 101034. https://www.ncbi.nlm.nih.gov/pubmed/32953466.

Cabrie, A., O. Guittet, R. Tomasini, P. Vincendeau and M. Lepoivre (2019). « Crosstalk between TAp73 and TGF-beta in fibroblast regulates iNOS expression and Nrf2-dependent gene transcription. » Free Radic Biol Med 134: 617-629 https://www.ncbi.nlm.nih.gov/pubmed/30753884.

El Banna, N., E. Hatem, A. Heneman-Masurel, T. Leger, D. Baille, L. Vernis, C. Garcia, S. Martineau, C. Dupuy, S. Vagner, J. M. Camadro and M. E. Huang (2019). « Redox modifications of cysteine-containing proteins, cell cycle arrest and translation inhibition: Involvement in vitamin C-induced breast cancer cell death. » Redox Biol 26: 101290 http://www.ncbi.nlm.nih.gov/pubmed/31412312.

Hatem, E., S. Azzi, N. El Banna, T. He, A. Heneman-Masurel, L. Vernis, D. Baille, V. Masson, F. Dingli, D. Loew, B. Azzarone, P. Eid, G. Baldacci and M. E. Huang (2019). « Auranofin/Vitamin C: A Novel Drug Combination Targeting Triple-Negative Breast Cancer. » J Natl Cancer Inst http://www.ncbi.nlm.nih.gov/pubmed/30462268.

Hippolyte, A. and L. Vernis (2019). « [D-enantiomeric peptides could be a new therapeutic approach in Alzheimer’s disease]. » Med Sci (Paris) 35(11): 897-900 https://www.ncbi.nlm.nih.gov/pubmed/31845883.

Levy, E., N. El Banna, D. Baille, A. Heneman-Masurel, S. Truchet, H. Rezaei, M. E. Huang, V. Beringue, D. Martin and L. Vernis (2019). « Causative Links between Protein Aggregation and Oxidative Stress: A Review. » Int J Mol Sci 20(16) http://www.ncbi.nlm.nih.gov/pubmed/31405050.

Mounkoro, P., T. Michel, S. Blandin, M. P. Golinelli-Cohen, E. Davioud-Charvet and B. Meunier (2019). « Investigating the mode of action of the redox-active antimalarial drug plasmodione using the yeast model. » Free Radic Biol Med 141: 269-278 https://www.ncbi.nlm.nih.gov/pubmed/31238126.

Ferecatu, I., F. Canal, L. Fabbri, N. M. Mazure, C. Bouton and M. P. Golinelli-Cohen (2018). « Dysfunction in the mitochondrial Fe-S assembly machinery leads to formation of the chemoresistant truncated VDAC1 isoform without HIF-1alpha activation. » PLoS One 13(3): e0194782 https://www.ncbi.nlm.nih.gov/pubmed/29596470.

Guitton, J., M. Bekara and M. P. Golinelli-Cohen (2018). « Les protéines Fe-S Wbl, de nouvelles cibles thérapeutiques pour lutter contre la tuberculose. » Med Sci (Paris) 34(6-7): 612-614 https://www.medecinesciences.org/en/articles/medsci/full_html/2018/07/medsci180189s/medsci180189s.html.

Mons, C., T. Botzanowski, A. Nikolaev, P. Hellwig, S. Cianferani, E. Lescop, C. Bouton and M. P. Golinelli-Cohen (2018). « The H2O2-Resistant Fe-S Redox Switch MitoNEET Acts as a pH Sensor To Repair Stress-Damaged Fe-S Protein. » Biochemistry 57(38): 5616-5628 https://www.ncbi.nlm.nih.gov/pubmed/30204426.

Carreaux, A., S. De Champs De Saint-Léger, Y. Kouidri and M.-P. Golinelli-Cohen (2017). « Contrôle de la virulence de Salmonella enterica par la machinerie de biogenèse des centres Fe-S. » Med Sci (Paris) 33: 603-606 https://www.medecinesciences.org/en/articles/medsci/full_html/2017/06/medsci2017336-7p603/medsci2017336-7p603.html.

Golinelli-Cohen, M.-P. and C. Bouton (2017). « Fe-S Proteins Acting as Redox Switch: New Key Actors of Cellular Adaptive Responses. » Current Chemical Biology 11: 1-19 http://www.eurekaselect.com/node/151389/article.

Hatem, E., N. El Banna and M. E. Huang (2017). « Multifaceted Roles of Glutathione and Glutathione-Based Systems in Carcinogenesis and Anticancer Drug Resistance. » Antioxid Redox Signal 27(15): 1217-1234 https://www.ncbi.nlm.nih.gov/pubmed/28537430.

Lebigot, E., P. Gaignard, I. Dorboz, A. Slama, M. Rio, P. de Lonlay, B. Heron, F. Sabourdy, O. Boespflug-Tanguy, A. Cardoso, F. Habarou, C. Ottolenghi, P. Therond, C. Bouton, M. P. Golinelli-Cohen and A. Boutron (2017). « Impact of mutations within the [Fe-S] cluster or the lipoic acid biosynthesis pathways on mitochondrial protein expression profiles in fibroblasts from patients. » Mol Genet Metab 122(3): 85-94 https://www.ncbi.nlm.nih.gov/pubmed/28803783.

Mons, C., I. Ferecatu, S. Riquier, E. Lescop, C. Bouton and M. P. Golinelli-Cohen (2017). « Combined Biochemical, Biophysical, and Cellular Methods to Study Fe-S Cluster Transfer and Cytosolic Aconitase Repair by MitoNEET. » Methods Enzymol 595: 83-106 http://www.ncbi.nlm.nih.gov/pubmed/28882209.

Toledano, M. B. and M.-E. Huang (2017). « The Unfinished Puzzle of Glutathione Physiological Functions, an Old Molecule That Still Retains Many Enigmas. » Antioxidants & Redox Signaling 27(15): 1127-1129 https://pubmed.ncbi.nlm.nih.gov/28874053/.

Peuchant E, Bats ML, Moranvillier I, Lepoivre M, Guitton J, Wendum D, Lacombe ML, Moreau-Gaudry F, Boissan M, Dabernat S. (2017). « Metastasis suppressor NM23 limits oxidative stress in mammals by preventing activation of stress-activated protein kinases/JNKs through its nucleoside diphosphate kinase activity.  » FASEB J. 31(4):1531-1546. doi: 10.1096/fj.201600705R. Epub 2017 Jan 11. PMID: 28077425 10.1096/fj.201600705R

Vernis, L., N. El Banna, D. Baïlle, E. Hatem, A. Heneman and M.-E. Huang (2017). « Fe-S Clusters Emerging as Targets of Therapeutic Drugs. » Oxidative Medicine and Cellular Longevity 2017: 12 http://www.ncbi.nlm.nih.gov/pubmed/29445445.


Nrf2-dependent persistent oxidative stress results in stress-induced vulnerability to depression
Mol. Psychiatr., 2017, 22(pp.1701