Entity

Time filter

Source Type

Nancy, France

Nancy is a city with a strong university tradition. The University of Lorraine was founded in 1572 by the Dukes of Lorraine. It gained year after year a longstanding renown in Science, Law, Humanities and Medecine. Its current student population is 55,000, the majority being in Nancy. This is almost one student for seven inhabitants. Some 6,000 international students study on various campus in Nancy. The University of Lorraine , often abbreviated in UL, is a grand établissement created on 1 January 2012 by the merger of Henri Poincaré, Nancy 2 and Paul Verlaine Universities, and the National Polytechnic Institute of Lorraine . The merger process started in 2009 with the creation of a "pôles de recherche et d'enseignement supérieur" or PRES.The university is divided into two university centers, one in Nancy and one in Metz . The University of Lorraine has over 52,000 students and offers 101 accredited research centers organized in 9 research areas and 8 doctoral colleges. Wikipedia.


Grant
Agency: Cordis | Branch: H2020 | Program: RIA | Phase: NMP-29-2015 | Award Amount: 8.00M | Year: 2016

A definitive conclusion about the dangers associated with human or animal exposure to a particular nanomaterial can currently be made upon complex and costly procedures including complete NM characterisation with consequent careful and well-controlled in vivo experiments. A significant progress in the ability of the robust nanotoxicity prediction can be achieved using modern approaches based on one hand on systems biology, on another hand on statistical and other computational methods of analysis. In this project, using a comprehensive self-consistent study, which includes in-vivo, in-vitro and in-silico research, we address main respiratory toxicity pathways for representative set of nanomaterials, identify the mechanistic key events of the pathways, and relate them to interactions at bionano interface via careful post-uptake nanoparticle characterisation and molecular modelling. This approach will allow us to formulate novel set of toxicological mechanism-aware end-points that can be assessed in by means of economic and straightforward tests. Using the exhaustive list of end-points and pathways for the selected nanomaterials and exposure routs, we will enable clear discrimination between different pathways and relate the toxicity pathway to the properties of the material via intelligent QSARs. If successful, this approach will allow grouping of materials based on their ability to produce the pathway-relevant key events, identification of properties of concern for new materials, and will help to reduce the need for blanket toxicity testing and animal testing in the future.


Lede J.,University of Lorraine
Journal of Analytical and Applied Pyrolysis | Year: 2012

Cellulose pyrolysis, studied since more than one century, has been the object of a great number of papers. Several related kinetic models have been established in large experimental conditions, from slow to fast pyrolysis. Unfortunately, no actual consensus is reached. The primary formation of intermediate species accompanied or not with phase change phenomena are amongst the main matters of concerns. The purpose of the present review is to report the controversies, well-established knowledges and unresolved questions concerning the existence and role of intermediate species (often called "active cellulose"). After a general discussion, a few research topics are suggested at the end of the paper. © 2012 Elsevier B.V. All rights reserved. Source


Rouhier N.,University of Lorraine
New Phytologist | Year: 2010

Glutaredoxins are small oxidoreductases structurally related to thioredoxins. They have two major proposed biochemical roles: the reduction of disulphide bonds and the binding of iron-sulphur clusters, both of which involve glutathione. The thiol-disulphide reductase activity regulates the activity of target proteins, either metabolic enzymes or transcription factors, and also helps to regenerate thiol-dependent antioxidant enzymes, namely thiol-peroxidases and methionine sulphoxide reductases, which are key players for the plant response to environmental constraints. In photosynthetic organisms, glutaredoxins are distributed into six classes. Glutaredoxins from class II can exist either as apoforms, which display deglutathionylation activity, or as holoforms, which bind labile [2Fe-2S] clusters and seem to be required for iron-sulphur cluster assembly. This latter role is supported by the ability of the hologlutaredoxins to rapidly and efficiently transfer their clusters to apo-proteins in vitro. It has been proposed that they can act either as scaffold proteins for the de novo synthesis of iron-sulphur clusters or as carrier proteins for the transfer and delivery of preassembled iron-sulphur clusters. © The Authors (2010). Journal compilation © New Phytologist Trust (2010). Source


Henard S.,University of Lorraine
Journal of acquired immune deficiency syndromes (1999) | Year: 2012

A mild but significant association between a decrease in the total community viral load (CVL) and a decrease in the number of new HIV diagnoses was observed between 2005 and 2010 in the population of northern and eastern France. This result suggests that CVL could be used as robust marker of the efficacy of the "Treatment as Prevention" strategy, and it may even be stronger if a large number of undiagnosed patients and early HIV infection cases indicated by extend screening are included in the CVL measurement. Source


Weissman K.J.,University of Lorraine
Nature Chemical Biology | Year: 2015

The modular polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) are among the largest and most complicated enzymes in nature. In these biosynthetic systems, independently folding protein domains, which are organized into units called 'modules', operate in assembly-line fashion to construct polymeric chains and tailor their functionalities. Products of PKSs and NRPSs include a number of blockbuster medicines, and this has motivated researchers to understand how they operate so that they can be modified by genetic engineering. Beginning in the 1990s, structural biology has provided a number of key insights. The emerging picture is one of remarkable dynamics and conformational programming in which the chemical states of individual catalytic domains are communicated to the others, configuring the modules for the next stage in the biosynthesis. This unexpected level of complexity most likely accounts for the low success rate of empirical genetic engineering experiments and suggests ways forward for productive megaenzyme synthetic biology. Source

Discover hidden collaborations