H. Singh and R. H. Ashley, “Redox Regulation of CLIC1 by Cysteine Residues Associated with the Putative Chan- nel Pore,” Biophysical Journal, Vol. 90, No. 5, 2006, pp. 1628-1638. doi:10.1529/biophysj.105.072678

has been cited by the following article:

• TITLE: Soluble Structure of CLIC and S100 Proteins Investigated by Atomic Force Microscopy

  AUTHORS: Stella M. Valenzuela, Mark Berkahn, Alexander Porkovich, Thuan Huynh, Jesse Goyette, Donald K. Martin, Carolyn L. Geczy

  KEYWORDS: CLIC Proteins, S100 Proteins, Atomic Force Microscopy

  JOURNAL NAME: Journal of Biomaterials and Nanobiotechnology, Vol.2 No.1, January 27, 2011

  ABSTRACT: The ability to visualise proteins in their native environment and discern information regarding stoichiometry is of critical importance when studying protein interactions and function. We have used liquid cell atomic force microscopy (AFM) to visualise proteins in their native state in buffer and have determined their molecular volumes. The human proteins S100A8, S100A9, S100A12 and CLIC1 were used in this investigation. The effect of oxidation on the protein structure of CLIC1 was also investigated and we found that CLIC1 multimerisation could be discerned by AFM, which supports similar findings by other methods. We have found good correlation between the molecular volumes measured by AFM and the calculated volumes of the individual proteins. This method allows for the study of single soluble proteins under physiological conditions and could potentially be extended to study the structure of these proteins when located within a membrane environment.