Sophie Jackson

Research interests

Publications

• Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity

  ACS Chemical Biology · 2018 · 10.1021/acschembio.7b01039

• Factors affecting the physical stability (aggregation) of peptide therapeutics

  Interface Focus · 2017 · 10.1098/rsfs.2017.0030

• How to fold intricately: using theory and experiments to unravel the properties of knotted proteins

  Current Opinion in Structural Biology · 2016 · 10.1016/j.sbi.2016.10.002

• Molecular knots in biology and chemistry

  Journal of Physics Condensed Matter · 2015 · 10.1088/0953-8984/27/35/354101

• Hsp70 Forms Antiparallel Dimers Stabilized by Post-translational Modifications to Position Clients for Transfer to Hsp90

  Cell Reports · 2015 · 10.1016/j.celrep.2015.03.063

• Hsp90 Inhibits α-Synuclein Aggregation by Interacting with Soluble Oligomers

  Journal of Molecular Biology · 2013 · 10.1016/j.jmb.2013.08.006

• Hsp90: Structure and Function

  Topics in current chemistry · 2012 · 10.1007/128_2012_356

• Ubiquitin chain conformation regulates recognition and activity of interacting proteins

  Nature · 2012 · 10.1038/nature11722

• Knot formation in newly translated proteins is spontaneous and accelerated by chaperonins

  Nature Chemical Biology · 2011 · 10.1038/nchembio.742

• Structures and folding pathways of topologically knotted proteins

  Journal of Physics Condensed Matter · 2010 · 10.1088/0953-8984/23/3/033101

• Structural Studies on the Co-chaperone Hop and Its Complexes with Hsp90

  Journal of Molecular Biology · 2008 · 10.1016/j.jmb.2008.02.013

• Protein folding: Defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins

  Protein Science · 2005 · 10.1110/ps.041205405

• Folding Studies on a Knotted Protein

  Journal of Molecular Biology · 2005 · 10.1016/j.jmb.2004.12.055

• Ubiquitin folds through a highly polarized transition state

  Protein Engineering Design and Selection · 2005 · 10.1093/protein/gzi025

• The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins

  Journal of Molecular Biology · 2005 · 10.1016/j.jmb.2005.11.085

• The folding and design of repeat proteins: reaching a consensus

  Current Opinion in Structural Biology · 2003 · 10.1016/s0959-440x(03)00105-2

• Stimulation of the weak ATPase activity of human Hsp90 by a client protein 1 1Edited by G. von Heijne

  Journal of Molecular Biology · 2002 · 10.1006/jmbi.2001.5245

• Mapping the Interactions Present in the Transition State for Unfolding/Folding of FKBP12

  Journal of Molecular Biology · 1999 · 10.1006/jmbi.1999.2942

• How do small single-domain proteins fold?

  Folding and Design · 1998 · https://doi.org/10.1016/s1359-0278(98)00033-9

• Movement of the position of the transition state in protein folding

  Biochemistry · 1995 · 10.1021/bi00041a047

• Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.

  Proceedings of the National Academy of Sciences · 1994 · 10.1073/pnas.91.22.10422

• Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis

  Biochemistry · 1993 · 10.1021/bi00093a002

• Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2

  Biochemistry · 1993 · 10.1021/bi00093a001

• Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding

  Biochemistry · 1991 · 10.1021/bi00107a011

• Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition

  Biochemistry · 1991 · https://doi.org/10.1021/bi00107a010

Current projects

No projects listed.