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Article citations


Brinkerhoff, C.J., Woold, P.J. and Linderman, J.J. (2004) Monte Carlo simulations of receptor dynamics: insights into cell signaling. Journal of Molecular Histology, 35, 667-677.

has been cited by the following article:

  • TITLE: Do membrane proteins cluster without binding between molecules?

    AUTHORS: Xin Wang, Toshihiko Fukamachi, Hiromi Saito, Hiroshi Kobayashi

    KEYWORDS: Cluster Formation; Monte Carlo Simulation; Self-Assembly; Immune Cells; Membrane Proteins

    JOURNAL NAME: Open Journal of Immunology, Vol.2 No.1, March 19, 2012

    ABSTRACT: Clustering is a basic event for the initiation of immune cell responses, and simulation analyses of clustering of membrane proteins have been performed. It was claimed that a cluster is formed by the self-assembly induced by protein dimerization with a high binding speed (Woolf and Linderman, Biophys. Chem. 104, 217-227, 2003). We examined the cluster formation with Monte Carlo simulation using two algorithms. The first was that simulation processes were divided into two substeps. All proteins were subjected to movement in the first substep, followed by reaction in the second substep. The second algorithm was that proteins were first selected to react and proteins which did not react were subjected to movement. The self-assembly induced by dimerization was simulated only with the second algorithm. In this algorithm, monomers dissociated from dimers do not move because these monomers are not selected for movement, and a large proportion of such monomers are selected to form dimers in the next step. The self-assembly was again simulated with the first algorithm containing the conditions that monomers dissociated from dimers did not move in the next movement substep. This algorithm seems to be far removed from natural conditions. Thus, it is inferred that the self-assembly induced by dimerization is unlikely in situ, and that some interaction between proteins is required for cluster formation. In contrast to algorithms in previous simulations, our results suggest that it is more appropriate that proteins move to the same direction for a while and reflect when the collision occurs.