Françoise Rousseau-Hans

ORCID: 0000-0002-0382-6815
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About
Contact & Profiles
Research Areas
  • Education, sociology, and vocational training
  • Cultural Insights and Digital Impacts
  • Photosynthetic Processes and Mechanisms
  • RNA and protein synthesis mechanisms
  • scientometrics and bibliometrics research
  • Competitive and Knowledge Intelligence
  • Algal biology and biofuel production
  • Enzyme Structure and Function
  • Social Sciences and Governance
  • Protein Structure and Dynamics
  • Healthcare Systems and Practices
  • International Development and Aid
  • Bioinformatics and Genomic Networks
  • Bacterial Identification and Susceptibility Testing
  • Genomics and Phylogenetic Studies
  • Religion, Society, and Development
  • Social Policies and Family
  • Conferences and Exhibitions Management
  • Natural Language Processing Techniques
  • Molecular Biology Techniques and Applications
  • Academic Publishing and Open Access
  • Cancer Research and Treatments
  • Machine Learning in Bioinformatics
  • Health, Medicine and Society
  • Electrochemical sensors and biosensors

Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2005-2023

CEA Cadarache
2023

CEA Grenoble
2023

CEA Paris-Saclay - Etablissement de Saclay
2023

CEA Paris-Saclay
2023

Université d'Évry Val-d'Essonne
2021

Société Française de Cardiologie
2020

Agency for Science, Technology and Research
2011

Vrije Universiteit Brussel
2001-2006

Vlaams Instituut voor Biotechnologie
2001

FoldX is an empirical force field that was developed for the rapid evaluation of effect mutations on stability, folding and dynamics proteins nucleic acids. The core functionality FoldX, namely calculation free energy a macromolecule based its high-resolution 3D structure, now publicly available through web server at http://foldx.embl.de/. current release allows stability protein, positions protons prediction water bridges, metal binding sites analysis complex formation. Alanine scanning,...

10.1093/nar/gki387 article EN cc-by-nc Nucleic Acids Research 2005-06-26

Single nucleotide variants (SNVs) are, together with copy number variation, the primary source of variation in human genome and are associated phenotypic such as altered response to drug treatment susceptibility disease. Linking structural effects non-synonymous SNVs functional outcomes is a major issue bioinformatics. The SNPeffect database (http://snpeffect.switchlab.org) uses sequence- structure-based bioinformatics tools predict effect protein-coding on phenotype proteins. It integrates...

10.1093/nar/gkr996 article EN cc-by-nc Nucleic Acids Research 2011-11-10

We have developed a web tool, PupaSuite, for the selection of single nucleotide polymorphisms (SNPs) with potential phenotypic effect, specifically oriented to help in design large-scale genotyping projects. PupaSuite uses collection data on SNPs from heterogeneous sources and large number pre-calculated predictions offer flexible intuitive interface selecting an optimal set SNPs. It improves functionality PupaSNP PupasView programs implements new facilities such as analysis user's derive...

10.1093/nar/gkl071 article EN cc-by-nc Nucleic Acids Research 2006-07-01

p13suc1 has two native states, a monomer and domain-swapped dimer. We show that their folding pathways are connected by the denatured state, which introduces kinetic barrier between dimer under conditions. The is lowered conditions speed up unfolding, thereby allowing, to our knowledge for first time, quantitative dissection of energetics domain swapping. monomer–dimer equilibrium controlled conserved prolines in hinge loop connects exchanging domains. These residues exploit backbone strain...

10.1073/pnas.101542098 article EN Proceedings of the National Academy of Sciences 2001-05-08

We describe here the complete amino acid sequence of photosystem I subunit IV from Synechocystis 6803. The molecular mass 8.0 kDa is lower than in higher plants and Chlamydomonas , due to lack a characteristic, proline‐rich, N‐terminal sequence. remaining exhibits good conservation, with hydrophilic strongly basic N‐tenninal head followed by two hydrophobic domains. There no possibility classical membrane‐spanning alpha helices. This component likely be one most stroma accessible subunits I.

10.1016/0014-5793(90)80113-w article EN FEBS Letters 1990-01-29

12 Ar ( abes ) ques N°103 OCTOBRE

10.35562/arabesques.2719 article CA cc-by-nd Arabesques 2021-10-01
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