Regular Article26S Proteasome Structure Revealed by Three-dimensional Electron Microscopy☆
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2015, International Review of Cell and Molecular BiologyCitation Excerpt :The gate of 20S CP remains closed by the N-termini of the α-subunits and it opens by the regulatory action of the 19S RP (Groll et al., 2000; Whitby et al., 2000); on the other hand it is not clear how oxidized proteins bind and enter into the 20S CP. Based on low-resolution electron microscopy analyses of isolated proteasomes, the 19S RP (or PA700) contains 20 subunits which are evolutionarily conserved and are organized into two subcomplexes, namely the base and the lid (da Fonseca and Morris, 2008; Glickman et al., 1998a; Ikai et al., 1991; Liu and Jacobson, 2013; Nickell et al., 2007; Peters et al., 1991; Walz et al., 1998). The base consists of six AAA-type ATPases (Rpt1-6) and three non-ATPase subunits, namely the Rpn1, Rpn2, and Rpn13 subunits (Glickman et al., 1998a; Jung and Grune, 2013; Walz et al., 1998; Tanaka, 2013).
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