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Correction
February 2002

Errors in Figures 1 and 5 and Accompanying Legends, for a Sentence in Legends to Figures 2 Through 4, and in Lead Author's Name in Affiliation Footnote

Arch Neurol. 2002;59(2):202. doi:10.1001/archneur.59.2.202

In the Original Contribution by Parvathy et al titled "Correlation Between Aβx-40–, Aβx-42–, and Aβx-43–Containing Amyloid Plaques and Cognitive Decline," published in the December issue of ARCHIVES (2001;58:2025-2032), Figure 1 and Figure 5 had errors in the body of the figure and its accompanying legend. We are reproducing the correct figures and legends here (Figure 1 and Figure 5). In the legends to Figures 1 through 5, the sentence that reads "AβC40, AβC42, and AβC43 are antibodies reactive to amyloid βx-40." should have read: "AβC40, AβC42, and AβC43 are antibodies reactive to amyloid βx-40, amyloid βx-42, and amyloid βx-43, respectively. In addition, the second mention of the lead author's name was misspelled in the affiliation footnote at the bottom left on page 2025. It should have read Dr Parvathy. The ARCHIVES regrets these errors.

Figure 1.
Characterization of antibodies. AβC40, AβC42, and AβC43 are antibodies reactive to amyloid βx-40, amyloid βx-42, and amyloid βx-43, respectively. Specificity of antibodies AβC40, AβC42, and AβC43 was determined by dot blotting (A), immunoblotting (B), and enzyme-linked immunosorbent assay (C). Synthetic Aβ1-40, Aβ1-42, or Aβ1-43 was either spotted on a nitrocellulose membrane (A) or electrophoresed on a Tris-tricine gel and transferred to a nitrocellulose membrane (B). The membranes were probed with the indicated antibodies and detected using horseradish peroxidase–conjugated secondary antibody with enhanced chemiluminescent reagent. In part C indicated amounts of synthetic Aβ1-40, Aβ1-42, and Aβ1-43 peptides were coated onto enzyme-linked immunosorbent assay plates and incubated with antibody. Bound antibody was detected using a calorimetric assay.

Characterization of antibodies. AβC40, AβC42, and AβC43 are antibodies reactive to amyloid βx-40, amyloid βx-42, and amyloid βx-43, respectively. Specificity of antibodies AβC40, AβC42, and AβC43 was determined by dot blotting (A), immunoblotting (B), and enzyme-linked immunosorbent assay (C). Synthetic Aβ1-40, Aβ1-42, or Aβ1-43 was either spotted on a nitrocellulose membrane (A) or electrophoresed on a Tris-tricine gel and transferred to a nitrocellulose membrane (B). The membranes were probed with the indicated antibodies and detected using horseradish peroxidase–conjugated secondary antibody with enhanced chemiluminescent reagent. In part C indicated amounts of synthetic Aβ1-40, Aβ1-42, and Aβ1-43 peptides were coated onto enzyme-linked immunosorbent assay plates and incubated with antibody. Bound antibody was detected using a calorimetric assay.

Figure 5.
Relative proportion of amyloid β (Aβ) plaque types. The number of cored and diffuse plaques in double-labeled sections stained with either AβC40 and AβC42 (A) or AβC42 and AβC43 (B) antibodies was determined and is given as a percentage of total plaques counted in each condition. In each condition, the number of plaques containing either 1 or 2 Aβ variants was determined. AβC40, AβC42, and AβC43 are antibodies reactive to amyloid βx-40, amyloid βx-42, and amyloid βx-43, respectively.

Relative proportion of amyloid β (Aβ) plaque types. The number of cored and diffuse plaques in double-labeled sections stained with either AβC40 and AβC42 (A) or AβC42 and AβC43 (B) antibodies was determined and is given as a percentage of total plaques counted in each condition. In each condition, the number of plaques containing either 1 or 2 Aβ variants was determined. AβC40, AβC42, and AβC43 are antibodies reactive to amyloid βx-40, amyloid βx-42, and amyloid βx-43, respectively.

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