Zobrazeno 1 - 10 of 163 pro vyhledávání: '"André Aubry"'
1
Molecular modelling, synthesis and biological evaluation of peptide inhibitors as anti-angiogenic agent targeting Neuropilin-1 for anticancer application
Autor: Amirah Mohd Gazzali, Habibah A. Wahab, Céline Frochot, Régis Vanderesse, Muriel Barberi-Heyob, Ezatul Ezleen Kamarulzaman, Cédric Boura, André Aubry, Omar bin Shawkataly
Publikováno v: Journal of Biomolecular Structure and Dynamics
Journal of Biomolecular Structure and Dynamics, Taylor & Francis: STM, Behavioural Science and Public Health Titles, 2017, 35 (1), pp.26-45. ⟨10.1080/07391102.2015.1131196⟩
Vascular endothelial growth factor (VEGF) and its co-receptor neuropilin-1 (NRP-1) are important targets of many pro-angiogenic factors. In this study, nine peptides were synthesized and evaluated for their molecular interaction with NRP-1 and compar
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f138bc61681ef25806dffa5a1917cf70
https://hal.archives-ouvertes.fr/hal-01309306
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2
Peptides from chiral Cα,α-disubstituted glycines. Synthesis and conformational analysis of homochiral (αMe) Leu / Ala model peptides
Autor: A. Dautant, Fernando Formaggio, M. Pantano, W. H. J. Boesten, Claudio Toniolo, André Aubry, Marco Crisma, Gian Maria Bonora, Hans E. Schoemaker, Johan Kamphuis, D. Bayeul
Publikováno v: Recueil des Travaux Chimiques des Pays-Bas. 113:29-34
Homochiral (αMe)Leu/Ala and Leu/Ala model peptides were synthesized by solution methods and fully characterized. A solution conformational analysis of the tripeptides was carried out using FT-IR absorption and 1H NMR. The crystal-state structure of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::99fb67d585f62f452896a3400f5ce3e8
https://doi.org/10.1002/recl.19941130104
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3
Crystal molecular structures of two tripeptides related to the sequence coding for N-glycosylation
Autor: Guy Boussard, Abdelilah Abbadi, Virginie Pichon-Pesme, Michel Marraud, André Aubry
Publikováno v: International Journal of Peptide and Protein Research. 32:175-182
The crystal structures of two tripeptides related to the sequence coding for N-glycosylation of peptides have been solved: Boc-Asn(Me)-Ala-Ser-OMe, 1, and Boc-Asn(Me)-Pro-Ser-NHMe, 2. Both molecules contain an “Asx-turn” characterized by a hydrog
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ff2537a8c7d0edca3f039a16afc31983
https://doi.org/10.1111/j.1399-3011.1988.tb00932.x
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4
N-Methyl peptides
Autor: Manh Thong Cung, Michel Marraud, B. Vitoux, André Aubry
Publikováno v: International Journal of Peptide and Protein Research. 27:617-632
The natural occurrence of N-methyl peptides in various plant metabolites has made N-methylation a subtle and attractive possible modification for structure-activity relationship studies of endogeneous peptides. However, little is known about the conf
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3edd1f6bbb01706a3c780071b53a435f
https://doi.org/10.1111/j.1399-3011.1986.tb01058.x
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5
Aza-peptides. III. Experimental structural analysis of aza-alanme and aza-asparagine-containing peptides
Autor: André Aubry, Guy Boussard, Michel Marraud, Frédéric André, André Vicherat
Publikováno v: The Journal of Peptide Research. 50:372-381
To determine the structural perturbations induced by the C alpha H-->N alpha exchange in aza-peptides, we have examined by 1H NMR and IR spectroscopy various derivatives of the aza-analogues of alanine, aspartic acid and asparagine in different organ
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b0843871d3468b70101c5b3434715a9
https://doi.org/10.1111/j.1399-3011.1997.tb01197.x
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6
Synthesis, crystal structure and molecular conformation of the tBuCO-D,L-Ala-Δz-Phe-NhiPr α,β-unsaturated dipeptide
Autor: Guy Boussard, Barbara Rzeszotarska, Michel Marraud, André Aubry, Grzegorz Pietrzynski
Publikováno v: International Journal of Peptide and Protein Research. 37:39-45
The crystal structure of the tBuCO-D,L-Ala-delta Z-Phe-NHiPr dipeptide has been solved by X-ray diffraction. The peptide crystallizes in monoclinic space group P2(1)/c with a = 13.445 (3) A, b = 35.088 (4) A, c = 14.755 (3) A, beta = 116.73 (1) degre
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::958d2d4f2ba4b2ffcf5110a4053d1478
https://doi.org/10.1111/j.1399-3011.1991.tb00731.x
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8
N-METHYL PEPTIDES
Autor: Michel Marraud, B. Vitoux, Guy Boussard, André Aubry
Publikováno v: International Journal of Peptide and Protein Research. 18:195-202
The model tripeptide tBuCO-L-Pro-Me-D-Ala-MHMe crystallizes in both anhydrous (1) and monohydrated (2) states: 1, monoclinic space group C2 with a = 20.030 (2) A, b = 5.836 (2) A, c = 14.958 (3) A and beta = 94.11 (1) degrees; 2, orthorhombic space g
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::11debdb04d9c880a9fd36ce73bbdbbae
https://doi.org/10.1111/j.1399-3011.1981.tb02057.x
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9
A β-turn-like conformation in 'reduced' peptides Crystal structures of two dipeptide analogs with Pro-GlyΨ[CH2-NH] sequence
Autor: Emmanuel J. Gomez, Michel Marraud, Larbi El Masdouri, André Aubry, Manh Thong Cung, Constantinos Sakarellos
Publikováno v: International Journal of Peptide and Protein Research. 31:420-428
The conformational properties of the “reduced” dipeptides tBuCO-Pro-GlyΨ[CH2-NH]NRR′(R = H, R = Et; R = R′= Me) greatly depend upon the neutral or protonated state of the “reduced” amide bond. Due to protonation, the quite flexible neutr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::702e723bb55b9668c7bbcbd5e3446f8b
https://doi.org/10.1111/j.1399-3011.1988.tb00051.x
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10
A Structural Analysis of the Catalytic Mechanism of Methionine Sulfoxide Reductase A from Neisseria meningitidis
Autor: Frédérique Favier, André Aubry, Brice Kauffmann, Fanomezana M. Ranaivoson, Guy Branlant, Mathias Antoine, Sandrine Boschi-Muller
Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2008, 377 (1), pp.268-280. ⟨10.1016/j.jmb.2008.01.021⟩
The methionine sulfoxide reductases (Msrs) are thioredoxin-dependent oxidoreductases that catalyse the reduction of the sulfoxide function of the oxidized methionine residues. These enzymes have been shown to regulate the life span of a wide range of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afe3d756dc69ae44c8629546075c2596
https://doi.org/10.1016/j.jmb.2008.01.021
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