Výsledky vyhledávání - "Fischer, Marcel J."

New drug-strategies to tackle viral-host interactions for the treatment of influenza virus infections

Autor: van de Wakker, Simonides I, Fischer, Marcel J E, Oosting, Ronald S, Pharmacology, Chemical Biology and Drug Discovery, Afd Chemical Biology and Drug Discovery

Publikováno v: European Journal of Pharmacology, 809, 178. Elsevier

The influenza virus (IV) is a highly contagious virus causing seasonal global outbreaks affecting annually up to 20% of the world's population and leading to 250,000-500,000 deaths worldwide. Current vaccines have variable effectiveness, and, in part

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bf12ba03c896279f5c2870c20ea9989
https://pubmed.ncbi.nlm.nih.gov/28533172

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Tissue-type plasminogen activator binds to Aβ and AIAPP amyloid fibrils with multiple domains.

Autor: Beringer, Dennis X.¹ (AUTHOR), Fischer, Marcel J. E.² (AUTHOR), Meeldijk, Johannes D.³ (AUTHOR), van Donselaar, Elly G.⁴ (AUTHOR), de Mol, Nico J.² (AUTHOR), Kroon-Batenburg, Loes M. J.¹ (AUTHOR) L.M.J.Kroon-Batenburg@uu.nl

Publikováno v: Amyloid. Jun2013, Vol. 20 Issue 2, p113-121. 9p.

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Surface Plasmon Resonance Thermodynamic and Kinetic Analysis as a Strategic Tool in Drug Design. Distinct Ways for Phosphopeptides to Plug into Src- and Grb2 SH2 Domains

Autor: de Mol, Nico J, Dekker, Frank J, Broutin, Isabel, Fischer, Marcel J E, Liskamp, Rob M J, Dekker, Frank

Publikováno v: Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 2005, 48 (3), pp.753-763. ⟨10.1021/jm049359e⟩
Journal of Medicinal Chemistry, 48(3), 753-763. AMER CHEMICAL SOC

Thermodynamic and kinetic studies of biomolecular interactions give insight into specificity of molecular recognition processes and advance rational drug design. Binding of phosphotyrosine (pY)-containing peptides to Src- and Grb2-SH2 domains was inv

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3347395a687da5d6f503ac6b9a5b2d29
https://hal.archives-ouvertes.fr/hal-02520004

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Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands

Autor: Arnusch, Christopher J., André, Sabine, Valentini, Paola, Lensch, Martin, Russwurm, Roland, Siebert, Hans-Christian, Fischer, Marcel J. E., Gabius, Hans-Joachim, Pieters, Roland J., Dep Farmaceutische wetenschappen, Afd Chemical Biology and Drug Discovery

Publikováno v: Bioorganic and Medicinal Chemistry Letters, 14(6), 1437. Elsevier

A library of pentapeptides containing the sequence -Y-X-Y- based on rational design was screened with six different lectins. Sequences were identified that modulate galectin binding to its natural carbohydrate ligand. SPR showed inhibition values 2-3

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53842c1002064c73454404f843cc47b4
https://dspace.library.uu.nl/handle/1874/387299

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Cyclic phosphopeptides for interference with Grb2 SH2 domain signal transduction prepared by ring-closing metathesis and phosphorylation

Autor: Dekker, Frank J, de Mol, Nico J, Fischer, Marcel J E, Kemmink, Johan, Liskamp, Rob M J, Dekker, Frank

Publikováno v: Organic & Biomolecular Chemistry, 1(19), 3297-303. ROYAL SOC CHEMISTRY

Cyclic phosphopeptides were prepared using ring-closing metathesis followed by phosphorylation. These cyclic phosphopeptides were designed to interact with the SH2 domain of Grb2, which is a signal transduction protein of importance as a target for a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::2dbd86d3b6b91314eb463b2d57ed351d
https://research.rug.nl/en/publications/26f05a45-a00f-423c-b416-48541692c4ba

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Amino propynyl benzoic acid building block in rigid spacers of divalent ligands binding to the Syk SH2 domains with equally high affinity as the natural ligand

Autor: Dekker, Frank J, de Mol, Nico J, Fischer, Marcel J E, Liskamp, Rob M J, Dekker, Frank

Publikováno v: Bioorganic & Medicinal Chemistry Letters, 13(7), 1241-4. American Chemical Society

The construction of rigid spacers composed of amino propynyl benzoic acid building blocks is described. These spacers were used to link two phosphopeptide ligand sites towards obtaining divalent ligands with a high affinity for Syk tandem SH2 domains

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::6ffaae626c349b1fc60c53638efc33b8
https://research.rug.nl/en/publications/1e6ccb38-7399-4bb1-aab2-26d90171c8e6

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