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Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.
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- Angewandte Chemie, 2017, v. 129, n. 26, p. 7618, doi. 10.1002/ange.201701761
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Polymorphismus von Amyloidfibrillen in vivo.
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- Angewandte Chemie, 2016, v. 128, n. 15, p. 4903, doi. 10.1002/ange.201511524
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Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.
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- Angewandte Chemie International Edition, 2017, v. 56, n. 26, p. 7510, doi. 10.1002/anie.201701761
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- Article
Polymorphism of Amyloid Fibrils In Vivo.
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- Angewandte Chemie International Edition, 2016, v. 55, n. 15, p. 4822, doi. 10.1002/anie.201511524
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- Article
Diversity in Functional Organization of Class I and Class II Biotin Protein Ligase.
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- PLoS ONE, 2011, v. 6, n. 3, p. 1, doi. 10.1371/journal.pone.0016850
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Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis.
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- Nature Communications, 2019, v. 10, n. 1, p. 1, doi. 10.1038/s41467-019-09032-0
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- Article
Physical basis of amyloid fibril polymorphism.
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- Nature Communications, 2018, v. 9, n. 1, p. 1, doi. 10.1038/s41467-018-03164-5
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- Article
Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril.
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- Biomolecular NMR Assignments, 2021, v. 15, n. 1, p. 9, doi. 10.1007/s12104-020-09975-2
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Synthesis and variable temperature electrical conductivity studies of highly ordered TiO<sub>2</sub> nanotubes.
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- Journal of Materials Science, 2009, v. 44, n. 17, p. 4613, doi. 10.1007/s10853-009-3703-5
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