Olivier Genest

发表

Protein rescue from aggregates by powerful molecular chaperone machines

S. Wickner, S. M. Doyle, Olivier Genest, 2013, Nature Reviews Molecular Cell Biology.

Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling.

J. Hoskins, S. Wickner, Olivier Genest, 2015, Journal of molecular biology.

Hsp90 Is Essential under Heat Stress in the Bacterium Shewanella oneidensis.

V. Méjean, Olivier Genest, F. Honoré, 2017, Cell reports.

Cold adaptation in the environmental bacterium Shewanella oneidensis is controlled by a J-domain co-chaperone protein network

D. Byrne, V. Méjean, Olivier Genest, 2019, Communications Biology.

Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation

J. Hoskins, D. Masison, S. Wickner, 2011, Proceedings of the National Academy of Sciences.

TorD, an Essential Chaperone for TorA Molybdoenzyme Maturation at High Temperature*

V. Méjean, M. Ilbert, C. Iobbi-Nivol, 2005, Journal of Biological Chemistry.

Protection of the general stress response σS factor by the CrsR regulator allows a rapid and efficient adaptation of Shewanella oneidensis

V. Méjean, C. Iobbi-Nivol, Olivier Genest, 2017, The Journal of Biological Chemistry.

Interplay between the Hsp90 Chaperone and the HslVU Protease To Regulate the Level of an Essential Protein in Shewanella oneidensis

V. Méjean, Olivier Genest, F. Honoré, 2019, mBio.

Multiple roles of TorD-like chaperones in the biogenesis of molybdoenzymes.

Olivier Genest, V. Méjean, Chantal Iobbi-Nivol, 2009, FEMS microbiology letters.

Dedicated Metallochaperone Connects Apoenzyme and Molybdenum Cofactor Biosynthesis Components*

V. Méjean, S. Leimkühler, W. Stöcklein, 2008, Journal of Biological Chemistry.

Chaperones in maturation of molybdoenzymes: Why specific is better than general?

O. Lemaire, V. Méjean, C. Iobbi-Nivol, 2017, Bioengineered.

Quality control of a molybdoenzyme by the Lon protease

V. Méjean, David Redelberger, M. Ilbert, 2013, FEBS letters.

YcdY Protein of Escherichia coli, an Atypical Member of the TorD Chaperone Family

V. Méjean, David Redelberger, S. Leimkühler, 2011, Journal of bacteriology.

Multiple rolesof TorD-like chaperones in thebiogenesis ofmolybdoenzymes

V. Méjean, C. Iobbi-Nivol, Olivier Genest, 2009 .

Chaperone protection of immature molybdoenzyme during molybdenum cofactor limitation.

L. Théraulaz, V. Méjean, C. Iobbi-Nivol, 2006, FEMS microbiology letters.

Signal peptide protection by specific chaperone.

V. Méjean, M. Ilbert, C. Iobbi-Nivol, 2006, Biochemical and biophysical research communications.

Copper Induces Protein Aggregation, a Toxic Process Compensated by Molecular Chaperones

D. Reichmann, U. Jakob, P. Genevaux, 2022, mBio.

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling

S. Wickner, Olivier Genest, S. Doyle, 2018, The Journal of Biological Chemistry.

Functional and physical interaction between yeast Hsp90 and Hsp70

J. Hoskins, D. Masison, S. Wickner, 2018, Proceedings of the National Academy of Sciences.

The Bacterial Hsp90 Chaperone: Cellular Functions and Mechanism of Action.

S. Wickner, Olivier Genest, Thu-Lan Lily Nguyen, 2021, Annual review of microbiology.

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.

D. Agard, J. Hoskins, D. Masison, 2013, Molecular cell.

The multiple facets of the Hsp90 machine

Olivier Genest, Laura J Blair, Mehdi Mollapour, 2019, Nature Structural & Molecular Biology.

The multiple facets of the Hsp90 machine

M. Mollapour, L. Blair, Olivier Genest, 2019, Nature Structural & Molecular Biology.

Cold adaptation in the environmental bacterium Shewanella oneidensis is controlled by a J-domain co-chaperone protein network

D. Byrne, V. Méjean, Olivier Genest, 2019, Communications Biology.

Uncoupling the Hsp90 and DnaK chaperone activities revealed the in vivo relevance of their collaboration in bacteria

D. Byrne, J. Nougayrède, É. Oswald, 2022, Proceedings of the National Academy of Sciences of the United States of America.

Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling

J. Hoskins, S. Wickner, Jodi L. Camberg, 2011, Proceedings of the National Academy of Sciences.

Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK.

J. Hoskins, S. Wickner, Olivier Genest, 2017, Journal of molecular biology.

Cold adaptation in the environmental bacterium Shewanella oneidensis is controlled by a J-domain co-chaperone protein network

D. Byrne, V. Méjean, Olivier Genest, 2019, Communications Biology.

The General Stress Response σS Is Regulated by a Partner Switch in the Gram-negative Bacterium Shewanella oneidensis*

M. Fons, C. Jourlin-Castelli, V. Méjean, 2016, The Journal of Biological Chemistry.

51 A region in the middle domain of E. coli Hsp90 is important for collaboration with DnaK

J. Hoskins, S. Wickner, Olivier Genest, 2015, Journal of biomolecular structure & dynamics.

Bacterial adaptation to cold: Conservation of a short J-domain co-chaperone and its protein partners in environmental proteobacteria.

D. Byrne, P. Arnoux, V. Méjean, 2023, Environmental microbiology.

Modulation of the RNA polymerase activity by AtcB, a protein associated with a DnaK chaperone network in Shewanella oneidensis.

V. Méjean, S. Dementin, M. Giudici-Orticoni, 2020, Biochemical and biophysical research communications.

Emerging fields in chaperone proteins: A French workshop.

A. Barducci, F. Ochsenbein, E. Mileo, 2018, Biochimie.

First Virtual International Congress on Cellular and Organismal Stress Responses, November 5–6, 2020

H. Kampinga, A. Edkins, A. Zhuravleva, 2021, Cell Stress and Chaperones.