Chaperones and protein disaggregation Saibil group, ISMB Birkbeck College London

	Structural basis of ubiquitin-independent PP1 complex disassembly by p97. van den Boom, J, Meyer, H & Saibil, HR (2022) BioRxiv https://biorxiv.org/cgi/content/short/2022.06.24.497491v1
	Cooperative amyloid fibre binding and disassembly by the Hsp70 disaggregase. J.G. Beton, J Monistrol, A Wentink, EC Johnston, AJ Roberts, B Bukau, BW Hoogenboom, HR Saibil (2022) EMBO J https://doi.org/10.15252/embj.2021110410
	Correlative light and electron microscopy suggests that mutant huntingtin dysregulates the endolysosomal pathway in presymptomatic Huntington's Disease. Zhou, Y, Peskett, TR, Landles, C, Warner, JB, Sathasivam, K, Smith, EJ, Chen, S, Wetzel R, Lashuel, HA, Bates, GP & Saibil, HR (2021) Acta Neuropathologica Commun. 9:70
	Two-step activation mechanism of the ClpB disaggregase for sequential substrate threading by the main ATPase motor. Deville, C, Franke, K, Mogk, A, Bukau, B & Saibil, HR (2019) Cell Reports 27, 3433-3446.
	A liquid to solid phase transition underlying pathological huntingtin exon1 aggregation. Peskett, TR, Rau, F, O’Driscoll, J, Patani, R, Saibil, HR (2018) Molec. Cell, https://doi.org/10.1016/j.molcel.2018.04.007
	Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase. Deville, C, Carroni, M, Franke, KB, Topf, M, Bukau, B, Mogk, A, & Saibil, HR (2017) Science Advances 3:e1701726.
	Human Hsp70 disaggregase reverses Parkinson's-linked alpha-synuclein amyloid fibrils. Gao, X, Carroni, M, Nussbaum-Krammer, C, Mogk, A Nillegoda, NB, Szlachcic, A, Guilbride, DL, Saibil, HR, Mayer MP & Bukau, B (2015) Mol. Cell 59, 781-793.
	Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Carroni, M, Kummer, E, Oguchi, Y, Wendler, P, Clare, DK, Sinning, I, Kopp, J, Mogk, A, Bukau, B & Saibil, HR (2014) eLife 3:e02481
	Chaperone machines for protein folding, unfolding and disaggregation. Saibil, HR (2013) Nature Rev. Mol. Cell. Biol. 14, 630-642.
	ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin. Clare, DK, Vasishtan, D, Stagg, S, Quispe, J, Farr, GW, Topf, M, Horwich, AL & Saibil, HR (2012) Cell 149, 113-123. Movies
	Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Malet, H, Canellas, F, Sawa, J, Yan, J, Thalassinos, K, Ehrmann, M, Clausen, T & Saibil, HR (2012) Nature Struct. Mol. Biol. 19, 152-157.
	Chaperonin complex with a newly folded substrate protein encapsulated in the folding chamber. Clare, DK, Bakkes, P van Heerikhuizen, H, van der Vies, SM, & Saibil, HR (2009) Nature 457, 107-111.
	Multiple states of a nucleotide-bound group 2 chaperonin. Clare, DK, Stagg, S, Quispe, J, Farr, GW, Horwich, AL & Saibil, HR (2008) Structure 16, 528-534,
	Topologies of a substrate protein bound to the chaperonin GroEL. Elad, N, Farr, GW, Clare, DK, Orlova, EV, Horwich, AL & Saibil, HR (2007) Mol. Cell 26, 415-426.
	Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. White, HE, Orlova, EV, Chen, S, Wang, L, Ignatiou, A, Gowen, B, Stromer, T, Franzmann, TM, Haslbeck, M, Buchner, J & Saibil, HR (2006) Structure14, 1197-1204.
	Allosteric signalling of ATP hydrolysis in GroEL-GroES complexes. Ranson, NA, Clare, DK, Farr, GW, Houldershaw, D, Horwich AL & Saibil, HR (2006) Nature Struct. Mol. Biol. 13, 147-152.
	A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation. Sewell, BT, Best, RB, Chen, S, Roseman, AM, Farr, GW, Horwich, AL & Saibil, HR (2004) Nature Struct. Mol. Biol. 11, 1128-1133.
	ATP-bound states of GroEL captured by cryo-electron microscopy, Ranson et al. (2001) Cell 107, 869-879.
	The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL, Roseman et al. (1996) Cell 87, 241-251. Movie of ATPase cycle
	Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy, Chen et al. (1994) Nature 371, 261-264.

Birkbeck EM group
Helen Saibil