Article citationsMore>>

Y. Suzuki, T. Goetze, D. Stroebel, D. Balasuriya, S. Yoshimura, R. Henderson, et al., “Visualization of Structural Changes Accompanying Activation of N-Methyl-D-Aspartate (NMDA) Receptors Using Fast-Scan Atomic Force Microscopy Imaging,” The Journal of Biological Chemistry, Vol. 288, No. 2, 2013, pp. 778-784.
http://dx.doi.org/10.1074/jbc.M112.422311

has been cited by the following article:

• TITLE: AFM Investigation of the Organization of Actin Bundles Formed by Actin-Binding Proteins

  AUTHORS: Jamie L. Gilmore, Masahiro Kumeta, Kunio Takeyasu

  KEYWORDS: F-Actin; Caprice; α-Actinin

  JOURNAL NAME: Journal of Surface Engineered Materials and Advanced Technology, Vol.3 No.4A, October 22, 2013

  ABSTRACT: AFM is a powerful technique for revealing the morphological features of various biological systems at high resolution. However, one of the complications of AFM is that samples must be attached to a flat surface in order to obtain images. This often requires the development of specialized methods depending on the sample which is being used. In this study, we developed a novel technique to image actin bundles on the mica surface. Using this technique, we were able to image molecular assemblies of F-actin with two actin remodeling proteins: α-actinin and Caprice. High resolution AFM images of F-actin fibers and bundle organization depicted two different types of molecular assemblies: F-actin bundles forming an elongated “zipper” structure in the presence of α-actinin, and bundles forming a perpendicularly crossing the mesh structure in the presence of Caprice.