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Institution

École normale supérieure de Cachan

EducationCachan, Île-de-France, France
About: École normale supérieure de Cachan is a education organization based out in Cachan, Île-de-France, France. It is known for research contribution in the topics: Decidability & Nonlinear system. The organization has 2717 authors who have published 5585 publications receiving 175925 citations.


Papers
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Journal ArticleDOI
TL;DR: Introducing the concepts of microfluidic and biochip systems based on recent progress in microfabrication techniques used to mimic liver tissue in vitro that allow liver chronic toxicity analysis in vitro on engineered tissues.

113 citations

Book ChapterDOI
01 Jan 1999
TL;DR: This report is based on a new property, called π-freeness, which allows the tracking of a reference trajectory in a way which bears some analogy with flat finite dimensional nonlinear systems.
Abstract: This is a report on recent works [1, 17, 19, 20, 21, 39, 40, 41, 43] on the control tracking of some infinite dimensional linear systems. It is based on a new property, called π-freeness, which allows the tracking of a reference trajectory in a way which bears some analogy with flat finite dimensional nonlinear systems (see [15, 16] and the references therein). Several examples are examined and simulations are provided.

113 citations

Journal ArticleDOI
TL;DR: In this article, the authors analyze the transfer pricing of multinational firms and find that intrafirm prices may systematically deviate from arm's-length prices for two motives: pricing to market and tax avoidance.
Abstract: This paper analyzes the transfer pricing of multinational firms. Intrafirm prices may systematically deviate from arm’s-length prices for two motives: pricing to market and tax avoidance. Using Fre...

113 citations

Journal ArticleDOI
TL;DR: The crystal structure of Mut101 in complex with IN is determined and it is shown that the compound binds to the LEDGF-binding pocket, promoting conformational changes of IN which explain at the atomic level the allosteric effect of the IN/LEDGF interaction inhibitor on IN functions.
Abstract: LEDGF/p75 (LEDGF) is the main cellular cofactor of HIV-1 integrase (IN). It acts as a tethering factor for IN, and targets the integration of HIV in actively transcribed gene regions of chromatin. A recently developed class of IN allosteric inhibitors can inhibit the LEDGF-IN interaction. We describe a new series of IN-LEDGF allosteric inhibitors, the most active of which is Mut101. We determined the crystal structure of Mut101 in complex with IN and showed that the compound binds to the LEDGF-binding pocket, promoting conformational changes of IN which explain at the atomic level the allosteric effect of the IN/LEDGF interaction inhibitor on IN functions. In vitro, Mut101 inhibited both IN-LEDGF interaction and IN strand transfer activity while enhancing IN-IN interaction. Time of addition experiments indicated that Mut101 behaved as an integration inhibitor. Mut101 was fully active on HIV-1 mutants resistant to INSTIs and other classes of anti-HIV drugs, indicative that this compound has a new mode of action. However, we found that Mut101 also displayed a more potent antiretroviral activity at a post-integration step. Infectivity of viral particles produced in presence of Mut101 was severely decreased. This latter effect also required the binding of the compound to the LEDGF-binding pocket. Mut101 has dual anti-HIV-1 activity, at integration and post-integration steps of the viral replication cycle, by binding to a unique target on IN (the LEDGF-binding pocket). The post-integration block of HIV-1 replication in virus-producer cells is the mechanism by which Mut101 is most active as an antiretroviral. To explain this difference between Mut101 antiretroviral activity at integration and post-integration stages, we propose the following model: LEDGF is a nuclear, chromatin-bound protein that is absent in the cytoplasm. Therefore, LEDGF can outcompete compound binding to IN in the nucleus of target cells lowering its antiretroviral activity at integration, but not in the cytoplasm where post-integration production of infectious viral particles takes place.

112 citations

Journal ArticleDOI
TL;DR: In this paper, a general and accurate approach to determine the no-load flux of field-excited flux-switching (FE-FS) machines is presented, based on magnetomotive force permeance theory.
Abstract: This paper presents a general and accurate approach to determine the no-load flux of field-excited flux-switching (FE-FS) machines. These structures are inherently difficult to model due to their doubly-slotted air gap. This analytical approach is based on magnetomotive force-permeance theory. The analytical model developed is extensively compared to field distribution obtained with 2-D finite element (2-D FE) simulations. The good agreement observed between analytical model and 2-D FE results emphasizes the interest of this general approach regarding the computation time. Hence, this analytical approach is suitable for optimization process in pre-sizing loop. Furthermore, based on the field model, classical electromagnetic performances can be derived, such as flux linkage and back-electromotive force (back-EMF) and also, unbalanced magnetic force. Once again, FE results validate the analytical prediction, allowing investigations on several stator-rotor combinations, or optimization of the back-EMF.

111 citations


Authors

Showing all 2722 results

NameH-indexPapersCitations
Shi Xue Dou122202874031
Olivier Hermine111102643779
John R. Reynolds10560750027
Shaul Mukamel95103040478
Tomás Torres8862528223
Ifor D. W. Samuel7460523151
Serge Abiteboul7327824576
Stéphane Roux6862719123
Zeger Debyser6740416531
Louis Nadjo6426412596
Praveen K. Thallapally6419012110
Andrew Travers6319313537
Shoji Takeuchi6369214704
Bineta Keita6327412053
Yves Mély6236813478
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20233
202222
202121
202029
201958
201879