Conformational studies of a benzodiazepine-like peptide in SDS micelles by circular dichroism,1H NMR and molecular dynamics simulation

Autor: Michel Marraud, Régis Vanderesse, Céline Frochot, Manh Thong Cung, Piotr Orlewski, Laurent Miclo, Jean-Luc Gaillard, Marc Lecouvey

Publikováno v: Letters in Peptide Science. 4:359-364

The conformation of a benzodiazepine-like decapeptide corresponding to the YLGYLEQLLR fragment of a casein has been examined in a sodium dodecyl sulfate micellar medium using circular dichroism, two-dimensional1H NMR spectroscopy and restrained molec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::092a1dcd969fe484b9d9d1cb46e57569
https://doi.org/10.1007/bf02442900

Solution structure of an SRYD-containing sequence (250?257) of the fibronectin-like Leishmania gp63 protein by restrained molecular dynamics

Autor: Vassilios Tsikaris, Maria Sakarellos-Daitsiotis, Manh Thong Cung, Piotr Orlewski, Constantinos Sakarellos, Ketty Soteriadou, Michel Marraud

Publikováno v: Letters in Peptide Science. 3:317-326

The IASRYDQL synthetic octapeptide (250-257) of the Leishmania major surface glycoprotein gp63 efficiently inhibits parasite attachment to the macrophage receptors in in vitro experiments, and the SRYD-containing tetrapeptide mimics antigenically and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64fdc149266f83af3b3f0ebb518a2425
https://doi.org/10.1007/bf00127666

Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76] MIR analogue: A molecular dynamics simulation from two-dimensional NMR data

Autor: Constantinos Sakarellos, Maria Sakarellos-Daitsiotis, Michel Marraud, Vassilios Tsikaris, Socrates J. Tzartos, Piotr Orlewski, Efstratia H. Vatzaki, Manh-Thong Cung

Publikováno v: Biopolymers. 40:419-432

Monoclonal antibodies against the main immunogenic region (MIR) of the muscle acetylcholine receptor (AChR) are capable of inducing experimental myasthenia gravis (MG) in animals. The epitope of these antibodies has been localized between residues 67

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7498149c4544ae7bc5a17a52ab79191c
https://doi.org/10.1002/(sici)1097-0282(1996)40:5<419::aid-bip1>3.0.co

The third-dimensional structure of the complex between an Fv antibody fragment and an analogue of the main immunogenic region of the acetylcholine receptor: A combined two-dimensional NMR, homology, and molecular modeling approach

Autor: Michel Marraud, Jens Kleinjung, Vassilios Tsikaris, Marie-Christine Petit, Constantinos Sakarellos, Piotr Orlewski, Manh-Thong Cung, Maria Sakarellos-Daitsiotis, Socrates J. Tzartos, Avgi Mamalaki

Publikováno v: Biopolymers / Biopolymers (Biospectroscopy); Biopolymers (Pept Sci ); Biopolymers (Peptide Sci ); Biopolymers (Pept Sci); Biopolymers
Biopolymers / Biopolymers (Biospectroscopy); Biopolymers (Pept Sci ); Biopolymers (Peptide Sci ); Biopolymers (Pept Sci); Biopolymers, 2000, 53 (2), pp.113-28. ⟨10.1002/(SICI)1097-0282(200002)53:23.0.CO;2-J⟩

Binding of autoantibodies to the acetylcholine receptor (AChR) plays a major role in the autoimmune disease Myasthenia gravis (MG). In this paper, we propose a structure model of a putative immunocomplex that gives rise to the reduction of functional

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::502b92e23db20499f466cdf097ae9401
http://olympias.lib.uoi.gr/jspui/handle/123456789/9711

Solution structures of the fibronectin-like Leishmania gp63 SRYD-containing sequence in the free and antibody-bound states - Transferred NOE and molecular dynamics studies

Autor: Michel Marraud, Constantinos Sakarellos, Georgia Konidou, Vassilios Tsikaris, Piotr Orlewski, Maria Sakarellos-Daitsiotis, Manh Thong Cung, Athina K. Tzinia, Marie-Christine Petit, Ketty Soteriadou

Publikováno v: European Journal of Biochemistry
European Journal of Biochemistry, Wiley, 1998, 253 (1), pp.184-93. ⟨10.1046/j.1432-1327.1998.2530184.x⟩

The anti-SRYD monoclonal antibody (mAbSRYD) raised against the IASRYDQL synthetic octapeptide, the 250-257 sequence of the Leishmania major surface glycoprotein gp63 recognizes both SRYD-containing peptides and the whole cognate major surface protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5024181c28b0a695b7c2f432433b130
http://olympias.lib.uoi.gr/jspui/handle/123456789/9204