PubMed:22182687 / 0-876 JSONTXT

{"project":"PubMed_Structured_Abstracts","denotations":[{"id":"T1","span":{"begin":131,"end":667},"obj":"BACKGROUND"}],"text":"Transmission electron microscopy characterization of fluorescently labelled amyloid β 1-40 and α-synuclein aggregates.\nBACKGROUND: Fluorescent tags, including small organic molecules and fluorescent proteins, enable the localization of protein molecules in biomedical research experiments. However, the use of these labels may interfere with the formation of larger-scale protein structures such as amyloid aggregates. Therefore, we investigate the effects of some commonly used fluorescent tags on the morphologies of fibrils grown from the Alzheimer's disease-associated peptide Amyloid β 1-40 (Aβ40) and the Parkinson's disease-associated protein α-synuclein (αS).\nRESULTS: Using transmission electron microscopy (TEM), we verify that N-terminal labeling of Aβ40 with AMCA, TAMRA, and Hilyte-Fluor 488 tags does not prevent the formation of protofibrils and amyloid fibrils"}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":399,"end":406},"obj":"HP_0011034"},{"id":"T2","span":{"begin":542,"end":561},"obj":"HP_0002511"},{"id":"T3","span":{"begin":581,"end":588},"obj":"HP_0011034"},{"id":"T4","span":{"begin":611,"end":620},"obj":"HP_0001300"}],"text":"Transmission electron microscopy characterization of fluorescently labelled amyloid β 1-40 and α-synuclein aggregates.\nBACKGROUND: Fluorescent tags, including small organic molecules and fluorescent proteins, enable the localization of protein molecules in biomedical research experiments. However, the use of these labels may interfere with the formation of larger-scale protein structures such as amyloid aggregates. Therefore, we investigate the effects of some commonly used fluorescent tags on the morphologies of fibrils grown from the Alzheimer's disease-associated peptide Amyloid β 1-40 (Aβ40) and the Parkinson's disease-associated protein α-synuclein (αS).\nRESULTS: Using transmission electron microscopy (TEM), we verify that N-terminal labeling of Aβ40 with AMCA, TAMRA, and Hilyte-Fluor 488 tags does not prevent the formation of protofibrils and amyloid fibrils"}

{"project":"Allie","denotations":[{"id":"SS1_22182687_4_0","span":{"begin":581,"end":595},"obj":"expanded"},{"id":"SS2_22182687_4_0","span":{"begin":597,"end":601},"obj":"abbr"},{"id":"SS1_22182687_4_1","span":{"begin":650,"end":661},"obj":"expanded"},{"id":"SS2_22182687_4_1","span":{"begin":663,"end":665},"obj":"abbr"},{"id":"SS1_22182687_6_0","span":{"begin":683,"end":715},"obj":"expanded"},{"id":"SS2_22182687_6_0","span":{"begin":717,"end":720},"obj":"abbr"}],"relations":[{"id":"AE1_22182687_4_0","pred":"abbreviatedTo","subj":"SS1_22182687_4_0","obj":"SS2_22182687_4_0"},{"id":"AE1_22182687_4_1","pred":"abbreviatedTo","subj":"SS1_22182687_4_1","obj":"SS2_22182687_4_1"},{"id":"AE1_22182687_6_0","pred":"abbreviatedTo","subj":"SS1_22182687_6_0","obj":"SS2_22182687_6_0"}],"text":"Transmission electron microscopy characterization of fluorescently labelled amyloid β 1-40 and α-synuclein aggregates.\nBACKGROUND: Fluorescent tags, including small organic molecules and fluorescent proteins, enable the localization of protein molecules in biomedical research experiments. However, the use of these labels may interfere with the formation of larger-scale protein structures such as amyloid aggregates. Therefore, we investigate the effects of some commonly used fluorescent tags on the morphologies of fibrils grown from the Alzheimer's disease-associated peptide Amyloid β 1-40 (Aβ40) and the Parkinson's disease-associated protein α-synuclein (αS).\nRESULTS: Using transmission electron microscopy (TEM), we verify that N-terminal labeling of Aβ40 with AMCA, TAMRA, and Hilyte-Fluor 488 tags does not prevent the formation of protofibrils and amyloid fibrils"}