The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated
Benesch, J.L.P., Aquilina, J.A., Baldwin, A.J., Rekas, A., Stengel, F., Lindner, R., Basha, E., Devlin, G., Horwitz, J., Vierling, E., Carver, J.A. & Robinson, C.V.
Chem. Biol. (2010), 17, 1008-17
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Separating and visualising protein assemblies by means of preparative mass spectrometry and microscopy
Benesch, J.L.P., Ruotolo, B.T., Simmons, D.A., Barrera, N.P., Morgner, N., Wang, L., Saibil, H.R. & Robinson, C.V..
J. Struct. Biol. (2010), 172, 161-8
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Crystal structures of truncated αA and αB crystallins reveals structural mechanisms of polydispersity important for eye lens function
Laganowsky, A., Benesch, J.L.P., Landau, M., Ding, L., Sawaya, M.R., Cascio, D. Huang, Q., Robinson, C.V., Horwitz, J. & Eisenberg, D.
Protein Sci. (2010), 19, 1031-43
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Quaternary dynamics and plasticity underlie small heat shock protein chaperone function
Stengel, F., Baldwin, A.J., Painter, A.J., Jaya, N., Basha, E., Kay, L.E., Vierling, E., Robinson, C.V. & Benesch, J.L.P.
Proc. Natl. Acad. Sci. U.S.A. (2010), 107, 2007-12
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