Southworth DR and Agard DA, “Client-loading conformation revealed in the cryo-EM structure of the human Hsp90:Hop molecular chaperone complex.” Molecular Cell, 2011 Jun 24;42(6): 771-81.
Krukenberg KA, Southworth DR, Street TO, Agard DA, “pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation." Journal of Molecular Biology. 2009 Jul 10; 390(2): pp 278-91.
Southworth DR and Agard DA, “Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.” Molecular Cell, 2008 Dec. 5; 32(5):631-40.
Shiau AK*, Harris SF*, Southworth DR and Agard, DA, “Structural analysis of a bacterial hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.” Cell, 2006 Oct 20; 127(2):329-40.
Cukras, AC*, Southworth, DR*, Brunelle, JL, Culver GM, and Green, R. “Ribosomal Proteins S12 and S13 Function as control elements for translocation of the mRNA:tRNA complex.” Molecular Cell, 2003 August; 12(2): 321-8.
Southworth, DR, Brunelle, JL, Green, R. “EF-G-independent translocation of the mRNA:tRNA complex is promoted by modification of the ribosome with thiol-Specific reagents.” Journal of Molecular Biology, 2002 December 6; 324 (4): 611-23.
