Erratum to: Mol Neurobiol

DOI 10.1007/s12035-014-8910-7

Figures 2c and 7c of the original articles unfortunately contain mistakes. The authors would like to correct these figures and are now elaborated as follows:

  1. (1)

    In Fig. 2c, the names of the two lanes should be swapped left–right. In the second line from the bottom of its caption, the word “left” should be “right.”

  2. (2)

    Aβ42-Q26 in Fig. 7c should be Aβ42-N27

Correct Figs. 2 and 7 are hereby published.

figure a

Fig. 2 Dot blot and Western blot analyses for the binding specificities of scFv AS to various Aβ42 species. Dots of Aβ42 monomers after incubation for an indicated period of time (0 and 30 min; 3, 6, 12, and 24 h) a or of Aβ42 monomers, oligomers, protofibrils, and fibrils b were probed with B4 and scFv AS, respectively, and then were detected with HRP-conjugated IgG and visualized with ECL chemiluminescence kit. Detection of scFv AS binding to various Aβ42 species ranging from Aβ42 monomers to fibrils by Western blot c. B4 served as positive controls [top row in a and b or right lane in c]. M monomers, O oligomers, P protofibrils, F fibrils

figure b

Fig. 7 Molecular docking model of Aβ42 monomer to scFv AS. a Ribbon display mode showing Aβ42 in dark black, scFv AS in light black. b Surface representation of the model. c Close-up view of VL-Ala174, Aβ42-Ser26, and Aβ42-Asn27 as those in b. d The hydrogen bonding interactions (dashed lines) between scFv AS and the N-terminal region (residues 1–15) of Aβ42 monomer. e The hydrophobic bonding interactions between scFv AS and the central region (residues 20–33) of Aβ42 monomer