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pro vyhledávání: '"Amara, Najette"'
Autor:
Amara, Najette
Les protéines sont synthétisées essentiellement à partir d'acides aminés L. Cependant, les acides aminés D sont naturellement présents dans notre organisme. Il existe plusieurs mécanismes de régulation pour limiter leur présence. Il peut y
Externí odkaz:
http://pastel.archives-ouvertes.fr/pastel-00622571
http://pastel.archives-ouvertes.fr/docs/00/62/25/71/PDF/these_finale.pdf
http://pastel.archives-ouvertes.fr/docs/00/62/25/71/PDF/these_finale.pdf
Publikováno v:
BMC Bioinformatics, Vol 9, Iss 1, p 148 (2008)
Abstract Background Protein structure prediction and computational protein design require efficient yet sufficiently accurate descriptions of aqueous solvent. We continue to evaluate the performance of the Coulomb/Accessible Surface Area (CASA) impli
Externí odkaz:
https://doaj.org/article/ec9182ad17d74788897f504625d47a3f
Autor:
Simonson, Thomas, Ye-Lehmann, Shixin, Palmai, Zoltan, Amara, Najette, Wydau-Dematteis, Sandra, Bigan, Erwan, Druart, Karen, Moch, Clara, Plateau, Pierre
Publikováno v:
Proteins: Structure, Function, and Genetics
Proteins: Structure, Function, and Genetics, Wiley, 2016, 84 (2), pp.240-253. ⟨10.1002/prot.24972⟩
Proteins: Structure, Function, and Genetics, Wiley, 2016, 84 (2), pp.240-253. ⟨10.1002/prot.24972⟩
International audience; D-Amino acids are largely excluded from protein synthesis, yet they are of great interest in biotechnology. Unnatural amino acids have been introduced into proteins using engineered aminoacyl-tRNA synthetases (aaRSs), and this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::b1cac5b613569d71fdcd7f4d3c16d755
https://hal-polytechnique.archives-ouvertes.fr/hal-01315193
https://hal-polytechnique.archives-ouvertes.fr/hal-01315193
Autor:
Polydorides, Savvas, Amara, Najette, Aubard, C., Plateau, P., Simonson, T., Archontis, Georgios Z.
Publikováno v:
Proteins-Structure, Function and Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, 2011, 79 (12), pp.3448-68. ⟨10.1002/prot.23042⟩
Proteins: Structure, Function and Bioinformatics
Proteins Struct.Funct.Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, 2011, 79 (12), pp.3448-68. ⟨10.1002/prot.23042⟩
Proteins: Structure, Function and Bioinformatics
Proteins Struct.Funct.Bioinformatics
Computational Protein Design (CPD) is a promising method for high throughput protein and ligand mutagenesis. Recently, we developed a CPD method that used a polar-hydrogen energy function for protein interactions and a Coulomb/Accessible Surface Area
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c58df0730662e6ca748e07cda3e3096
https://doi.org/10.1002/prot.23042
https://doi.org/10.1002/prot.23042
Autor:
Amara, Najette
Publikováno v:
Bio-Informatique, Biologie Systémique [q-bio.QM]. Ecole Polytechnique X, 2011. Français
Although most proteins are usually synthesized with L-amino acids, D-amino acids are present in organisms in their free states, included in shorts peptides and even in particular proteins. Introducing D-amino acids in proteins in a controlled way can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::127b7dfe44223d8794fcf1436fe1411e
https://pastel.archives-ouvertes.fr/pastel-00622571/document
https://pastel.archives-ouvertes.fr/pastel-00622571/document
Autor:
Simonson, T., Gaillard, T., Mignon, D., Schmidt Am Busch, M., Lopes, A., Amara, Najette, Polydorides, Savvas, Sedano, A., Druart, Karen, Archontis, Georgios Z.
Publikováno v:
Journal of Computational Chemistry
Journal of Computational Chemistry, Wiley, 2013, 34 (28), pp.2472-84. ⟨10.1002/jcc.23418⟩
J.Comput.Chem.
Journal of Computational Chemistry, Wiley, 2013, 34 (28), pp.2472-84. ⟨10.1002/jcc.23418⟩
J.Comput.Chem.
1 online ID: 1032 In: Journal of computational chemistry, Vol. 34, no. 28 ( 2013), p.2472-2484. Summary: Abstract We describe an automated procedure for protein design, implemented in a flexible software package, called Proteus. System setup and calc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::609e9d85da65f54a2523036d35ad9715
https://hal-polytechnique.archives-ouvertes.fr/hal-00868677
https://hal-polytechnique.archives-ouvertes.fr/hal-00868677
Akademický článek
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Publikováno v:
BMC Bioinformatics; 2008, Vol. 9, Special section p1-16, 16p, 1 Diagram, 8 Charts, 3 Graphs
Publikováno v:
In Biophysical Journal 31 January 2012 102(3) Supplement 1:114a-114a
Autor:
Simonson T; Department of Biology, Laboratoire De Biochimie (CNRS UMR7654), Ecole Polytechnique, Palaiseau, 91128, France., Ye-Lehmann S; Department of Biology, Ecole Normale Supérieure, Paris, France., Palmai Z; Department of Biology, Laboratoire De Biochimie (CNRS UMR7654), Ecole Polytechnique, Palaiseau, 91128, France., Amara N; Department of Biology, Laboratoire De Biochimie (CNRS UMR7654), Ecole Polytechnique, Palaiseau, 91128, France., Wydau-Dematteis S; Department of Biology, Laboratoire De Biochimie (CNRS UMR7654), Ecole Polytechnique, Palaiseau, 91128, France., Bigan E; Department of Biology, Laboratoire De Biochimie (CNRS UMR7654), Ecole Polytechnique, Palaiseau, 91128, France., Druart K; Department of Biology, Laboratoire De Biochimie (CNRS UMR7654), Ecole Polytechnique, Palaiseau, 91128, France., Moch C; Department of Biology, Laboratoire De Biochimie (CNRS UMR7654), Ecole Polytechnique, Palaiseau, 91128, France., Plateau P; Department of Biology, Laboratoire De Biochimie (CNRS UMR7654), Ecole Polytechnique, Palaiseau, 91128, France.
Publikováno v:
Proteins [Proteins] 2016 Feb; Vol. 84 (2), pp. 240-53. Date of Electronic Publication: 2016 Jan 07.