Výsledky vyhledávání - "S J, Tzartos"

Production of antibodies to alpha(181-192) peptides of neuronal nicotinic acetylcholine receptor coupled to protein carriers in different orientations

Autor: M V, Skok, O Yu, Lykhmus, S O, Bobrovnik, O V, Solodova, S J, Tzartos, T, Tsouloufis, R, Vanderesse, M, Marraud

Publikováno v: Ukrains'kyi biokhimichnyi zhurnal (1999 ). 74(4)

The antibodies to nicotinic acetylcholine receptor alpha(181-192) synthetic peptides were elicited in rabbits and mice using the peptides conjugated to protein carriers in different orientations, either through C-terminal Cys (S-conjugates), or throu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0a8ca6057e9d9803e3db55eafe8078e0
https://pubmed.ncbi.nlm.nih.gov/14964862

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Design, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptor

Autor: V, Theodorou, V, Tsikaris, M, Sakarellos-Daitsiotis, V, Avramopoulou, K, Kostelidou, S J, Tzartos, C, Sakarellos

Publikováno v: Biopolymers. 56(1)

Photoaffinity labeling is a powerful tool for the characterization of the molecular basis of ligand binding to acceptor molecules, which provides important insights for mapping the bimolecular interfaces. The autoimmune disease myasthenia gravis is c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::11632497944d9ed5c63970e42832cd98
https://pubmed.ncbi.nlm.nih.gov/11582576

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Severe congenital myasthenic syndrome due to homozygosity of the 1293insG epsilon-acetylcholine receptor subunit mutation

Autor: J P, Sieb, S, Kraner, B, Schrank, B, Reitter, T H, Goebel, S J, Tzartos, O K, Steinlein

Publikováno v: Annals of neurology. 48(3)

Recently, a congenital myasthenic syndrome (CMS) with end-plate acetylcholine receptor (AChR) deficiency due to missense mutations in the genes for the AChR subunit was described. The first observed patient with this CMS was heteroallelic for the two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::15fd461fbacbc4b48b134d4868a59f13
https://pubmed.ncbi.nlm.nih.gov/10976646

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The crystal structure of the Fab fragment of a rat monoclonal antibody against the main immunogenic region of the human muscle acetylcholine receptor

Autor: M, Kontou, D D, Leonidas, E H, Vatzaki, P, Tsantili, A, Mamalaki, N G, Oikonomakos, K R, Acharya, S J, Tzartos

Publikováno v: European journal of biochemistry. 267(8)

The crystal structure of the Fab fragment of a rat monoclonal antibody, number 192, with a very high affinity (Kd = 0.05 nM) for the main immunogenic region of the human muscle acetylcholine receptor (AChR), has been determined and refined to 2.4 A r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::17d4182e8f4614e7f339a1d645a0e60f
https://pubmed.ncbi.nlm.nih.gov/10759865

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Modulation of the anti-acetylcholine receptor response and experimental autoimmune myasthenia gravis by recombinant fragments of the acetylcholine receptor

Autor: D, Barchan, O, Asher, S J, Tzartos, S, Fuchs, M C, Souroujon

Publikováno v: European journal of immunology. 28(2)

Myasthenia gravis (MG) is a neuromuscular disorder of man caused by a humoral response to the acetylcholine receptor (AChR). Most of the antibodies in MG and in experimental autoimmune myasthenia gravis (EAMG) are directed to the extracellular portio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::67cee93a5347f09536c896ff748b6e70
https://pubmed.ncbi.nlm.nih.gov/9521072

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Cyclic lactam analogues containing the main immunogenic region of Torpedo acetylcholine receptor

Autor: E, Detsikas, V, Tsikaris, M, Sakarellos-Daitsiotis, C, Sakarellos, M T, Cung, M, Marraud, E, Vatzaki, S J, Tzartos

Publikováno v: Peptide research. 6(1)

The majority of autoantibodies against the nicotinic acetylcholine receptor (AChR) bind to an extracellular region of the AChR's alpha-subunit, named main immunogenic region (MIR), with the sequence W67-N-P-A-DY-G-G-I-K76 for the Torpedo californica

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e7c5dc0e6d540a609764a4886007ba0c
https://pubmed.ncbi.nlm.nih.gov/7679937

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The Ser-Arg-Tyr-Asp region of the major surface glycoprotein of Leishmania mimics the Arg-Gly-Asp-Ser cell attachment region of fibronectin

Autor: K P, Soteriadou, M S, Remoundos, M C, Katsikas, A K, Tzinia, V, Tsikaris, C, Sakarellos, S J, Tzartos

Publikováno v: The Journal of biological chemistry. 267(20)

The major surface glycoprotein of Leishmania, gp63, a fibronectin-like molecule, plays a key role in parasite-macrophage interaction. Binding of gp63 to macrophage receptors is inhibited by Arg-Gly-Asp-Ser (RGDS)-containing synthetic peptides of fibr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e528c2f483524d675367a366b6527901
https://pubmed.ncbi.nlm.nih.gov/1629196

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2D-NMR and molecular dynamics analysis of the Torpedo californica acetylcholine receptor alpha 67-76 fragment and of its [Ala76]-analogue

Autor: M T, Cung, V, Tsikaris, P, Demange, I, Papadouli, S J, Tzartos, C, Sakarellos, M, Marraud

Publikováno v: Peptide research. 5(1)

The alpha 67-76 fragment (Trp67-Asn68-Pro69-Ala70-Asp71-Tyr72 -Gly73-Gly74- Ile75-Lys76) of the Torpedo californica acetylcholine receptor (AChR) is selectively recognized by antibodies against the main immunogenic region of the AChR. The antibody bi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5eda4dd4132ac965ec73656a9a0d4c01
https://pubmed.ncbi.nlm.nih.gov/1623299

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