Davide Normanno | Centre National de la Recherche Scientifique / French National Centre for Scientific Research (original) (raw)

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Papers by Davide Normanno

SummaryCell fate depends on genetic, epigenetic and environmental inputs that are interconnected,... more SummaryCell fate depends on genetic, epigenetic and environmental inputs that are interconnected, making it difficult to disentangle their respective contributions to cell fate decisions1-3, and epigenetic reprogramming is a major contributor to tumor plasticity and adaptation4-6. Although cancer initiation and progression are generally associated with the accumulation of somatic mutations7,8, substantial epigenomic alterations underlie many aspects of tumorigenesis and cancer susceptibility9-18, suggesting that genetic mechanisms alone may not be sufficient to drive malignant transformations19-23. However, whether purely non-genetic reprogramming mechanisms are sufficient to initiate tumorigenesis irrespective of mutations is unknown. Here, we show that a transient perturbation of transcriptional silencing mediated by Polycomb-Group proteins is sufficient to induce an irreversible switch to a cancer cell fate inDrosophila. This is linked to the irreversible derepression of genes th...

Physical Review A, Nov 30, 2004

Microscopy Research and Technique, Nov 1, 2004

Single‐molecule techniques have propelled an impressive number of biophysical studies during the ... more Single‐molecule techniques have propelled an impressive number of biophysical studies during the last decade. From relatively simple video‐microscopy techniques, to sophisticated manipulation and detection apparata, single‐molecule techniques are capable of tracking the movements and the reaction trajectories of single enzymatic units. By observing microspheres attached to biomolecules it is possible to follow the motion of molecular motors, or to detect conformational “switching” induced by regulatory proteins. Micromanipulation tools like optical tweezers have been widely applied to understand the mechanisms of linear molecular motors, and have allowed the measurement of the elementary steps and the forces produced by several motor proteins, including myosin, kinesin, and dynein. New experimental assays based on magnetic or optical “wrenches,” which are able to apply and detect torques on rotary motors and biopolymers, are opening new possibilities in this field. Here, established and emerging magneto‐optical manipulation and video‐tracking techniques are reviewed, in the perspective of single molecular motors and regulatory proteins studies. Microsc. Res. Tech. 65:194–204, 2004. © 2005 Wiley‐Liss, Inc.

bioRxiv (Cold Spring Harbor Laboratory), Aug 13, 2021

Small, Jun 5, 2009

... 11 DE Staunton, ML Dustin, TA Springer, Nature 1989, 339, 61 64. ... 12 AR De Fougerolles, T... more ... 11 DE Staunton, ML Dustin, TA Springer, Nature 1989, 339, 61 64. ... 12 AR De Fougerolles, TA Springer, J. Exp. Med. 1992, 175, 185 190. ... 13 T. Schmidt, GJ Schutz, W. Baumgartner, HJ Gruber, H. Schindler, Proc. Natl. Acad. Sci. USA 1996, 93, 2926 2929. ...

Proceedings of the National Academy of Sciences of the United States of America, Jan 7, 2022

Life science alliance, Sep 27, 2021

Optics Letters, Oct 1, 2004

Laser beams have been demonstrated to be capable of exerting torque as well as forces on micropar... more Laser beams have been demonstrated to be capable of exerting torque as well as forces on microparticles. Using a custom magneto-optic manipulator, we directly measured the torque exerted by laser light on absorbing microspheres as a result of the transfer of spin angular momentum. A general method for measuring torque has been developed, and the experimental apparatus has shown a sensitivity of approximately 1 pN/nm.

Chemistry: A European Journal, Oct 31, 2022

One of the greatest current challenges in structural biology is to study protein dynamics over a ... more One of the greatest current challenges in structural biology is to study protein dynamics over a wide range of timescales in complex environments, such as the cell. Among magnetic resonances suitable for this approach, electron paramagnetic resonance spectroscopy coupled to site‐directed spin labeling (SDSL‐EPR) has emerged as a promising tool to study protein local dynamics and conformational ensembles. In this work, we exploit the sensitivity of nitroxide labels to report protein local dynamics at room temperature. We demonstrate that such studies can be performed while preserving both the integrity of the cells and the activity of the protein under investigation. Using this approach, we studied the structural dynamics of the chaperone NarJ in its natural host, Escherichia coli. We established that spin‐labeled NarJ is active inside the cell. We showed that the cellular medium affects NarJ structural dynamics in a site‐specific way, while the structural flexibility of the protein is maintained. Finally, we present and discuss data on the time‐resolved dynamics of NarJ in cellular context.