PubMed:22182687 / 677-1553 JSONTXT

{"project":"PubMed_Structured_Abstracts","denotations":[{"id":"T2","span":{"begin":0,"end":876},"obj":"RESULTS"}],"text":"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 of various widths. We also measure the two-photon action cross-section of Aβ40 labelled with Hilyte Fluor 488 and demonstrate that this tag is suitable for use with two-photon fluorescence techniques. Similarly, we find that Alexa Fluor 488 labelling of αS variant proteins near either the N or C terminus (position 9 or 130) does not interfere with the formation of amyloid and other types of αS fibrils. We also present TEM images of fibrils grown from αS C-terminally labelled with enhanced green fluorescent protein (EGFP). Near neutral pH, two types of αS-EGFP fibrils are observed via TEM, while denaturation of the EGFP tag leads to the formation of additional species."}

{"project":"Allie","denotations":[{"id":"SS1_22182687_6_0","span":{"begin":6,"end":38},"obj":"expanded"},{"id":"SS2_22182687_6_0","span":{"begin":40,"end":43},"obj":"abbr"},{"id":"SS1_22182687_9_0","span":{"begin":685,"end":719},"obj":"expanded"},{"id":"SS2_22182687_9_0","span":{"begin":721,"end":725},"obj":"abbr"}],"relations":[{"id":"AE1_22182687_6_0","pred":"abbreviatedTo","subj":"SS1_22182687_6_0","obj":"SS2_22182687_6_0"},{"id":"AE1_22182687_9_0","pred":"abbreviatedTo","subj":"SS1_22182687_9_0","obj":"SS2_22182687_9_0"}],"text":"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 of various widths. We also measure the two-photon action cross-section of Aβ40 labelled with Hilyte Fluor 488 and demonstrate that this tag is suitable for use with two-photon fluorescence techniques. Similarly, we find that Alexa Fluor 488 labelling of αS variant proteins near either the N or C terminus (position 9 or 130) does not interfere with the formation of amyloid and other types of αS fibrils. We also present TEM images of fibrils grown from αS C-terminally labelled with enhanced green fluorescent protein (EGFP). Near neutral pH, two types of αS-EGFP fibrils are observed via TEM, while denaturation of the EGFP tag leads to the formation of additional species."}