المؤلفون: Mariusz Jaremko, Markus Zweckstetter, Stefan Becker, Charles D. Schwieters, Hai-Young Kim, Min-Kyu Cho, Karin Giller, Łukasz Jaremko

المصدر: Nature chemical biology 9(4), 264-270 (2013). doi:10.1038/nchembio.1181
Nature Chemical Biology

مصطلحات موضوعية: Models, Molecular, DNA, Bacterial, genetics [Cytotoxins], Protein Denaturation, Protein Folding, chemistry [Bacterial Proteins], metabolism [Bacterial Proteins], metabolism [Recombinant Proteins], chemistry [Recombinant Proteins], Dimer, chemistry [Cytotoxins], Molecular Conformation, Repressor, genetics [Enterococcus faecalis], Plasma protein binding, Article, Dissociation (chemistry), chemistry.chemical_compound, Bacterial Proteins, genetics [DNA, Bacterial], ddc:570, Enterococcus faecalis, Escherichia coli, Denaturation (biochemistry), Promoter Regions, Genetic, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Protein Unfolding, Binding Sites, Cytotoxins, genetics [Escherichia coli], metabolism [DNA, Bacterial], Cell Biology, Nuclear magnetic resonance spectroscopy, metabolism [Cytotoxins], Recombinant Proteins, Cold Temperature, chemistry [DNA, Bacterial], genetics [Recombinant Proteins], Crystallography, chemistry, Unfolded protein response, Protein folding, metabolism [Enterococcus faecalis], Protein Multimerization, genetics [Bacterial Proteins], Protein Binding

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f298120e59800a81f3faebc8a7b80b19Test
https://doi.org/10.1038/nchembio.1181Test

المؤلفون: Nampally Sreenivasachary, Paolo Paganetti, Valérie Giriens, Luitgard Nagel-Steger, Markus Zweckstetter, Oskar Adolfsson, Andreas Muhs, Heiko Kroth, Maria Pihlgren, Andrea Pfeifer, Thomas Schrader, Sophie Lohmann, Yvan Varisco, Asad Jan, Nasrollah Rezaei-Ghaleh, María Pilar López-Deber, Annalisa Ansaloni, Hilal A. Lashuel, Wolfgang Froestl, Dieter Willbold

المصدر: Journal of Biological Chemistry
The journal of biological chemistry 287(41), 34786-34800 (2012). doi:10.1074/jbc.M112.357665
Kroth, H, Ansaloni, A, Varisco, Y, Jan, A, Sreenivasachary, N, Rezaei-Ghaleh, N, Giriens, V, Lohmann, S, López-Deber, M P, Adolfsson, O, Pihlgren, M, Paganetti, P, Froestl, W, Nagel-Steger, L, Willbold, D, Schrader, T, Zweckstetter, M, Pfeifer, A, Lashuel, H A & Muhs, A 2012, ' Discovery and structure activity relationship of small molecule inhibitors of toxic β-amyloid-42 fibril formation ', The Journal of biological chemistry, vol. 287, no. 41, pp. 34786-800 . https://doi.org/10.1074/jbc.M112.357665Test

مصطلحات موضوعية: 3-aminopyrazole, antagonists & inhibitors [Amyloid beta-Peptides], antagonists & inhibitors [Cytotoxins], antagonists & inhibitors [Peptide Fragments], Chemie, chemistry [Cytotoxins], Protein aggregation, Biochemistry, Protein Structure, Secondary, Hydrophobic effect, Structure-Activity Relationship, Protein structure, Cell Line, Tumor, mental disorders, Journal Article, Humans, Structure–activity relationship, Molecular Biology, chemistry.chemical_classification, Amyloid beta-Peptides, Cytotoxins, Chemistry, Research Support, Non-U.S. Gov't, In vitro toxicology, Molecular Bases of Disease, Hydrogen Bonding, Cell Biology, amyloid beta-protein (1-42), Small molecule, Peptide Fragments, Amino acid, chemistry [Peptide Fragments], ddc:540, chemistry [Pyrazoles], Pyrazoles, chemistry [Amyloid beta-Peptides], Hydrophobic and Hydrophilic Interactions, Linker

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الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4f1d6b8bb6eb1e9cd8d68fd89416ac0Test
https://hdl.handle.net/11858/00-001M-0000-000E-7305-311858/00-001M-0000-000E-7304-511858/00-001M-0000-000E-7300-DTest