S. Easterbrook-Smith

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The C1q receptor site on immunoglobulin G

D. Burton, R. Dwek, J. Novotný, 1980, Nature.

The formation of insoluble immune complexes between ovalbumin and anti-ovalbumin IgG occurs in at least two distinct phases dependent on reactant concentration and ionic strength.

J. Altin, N. N. Gorgani, S. Easterbrook-Smith, 1996, Biochimica et biophysica acta.

Solution conformations of 1‐anilinonaphthalene‐8‐sulphonate

R. Vandenberg, G. Mendz, S. Easterbrook-Smith, 1990 .

Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state.

J. Carver, M. Rybchyn, M. Wilson, 2000, Biochemistry.

Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins*

J. Carver, Mark R. Wilson, S. Easterbrook-Smith, 1999, The Journal of Biological Chemistry.

Comparison of the role of tyrosine residues in human IgG and rabbit IgG in binding of complement subcomponent C1q.

M. McCall, S. Easterbrook-Smith, 1989, The Biochemical journal.

Effects of clusterin overexpression on TNFalpha- and TGFbeta-mediated death of L929 cells.

M. Wilson, M. Tenniswood, S. Easterbrook-Smith, 1997, Biochemistry.

Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin.

Mark R. Wilson, G. Howlett, D. Hatters, 2002, European journal of biochemistry.

Binding of complement component C1q by rat adipocyte membranes.

S. Easterbrook-Smith, A. Comis, 1985, Molecular immunology.

Carbodiimide crosslinking of human C1q and rabbit IgG.

B. Wines, S. Easterbrook-Smith, 1990, Molecular immunology.

Pyruvate carboxylase: mechanism on the second partial reaction.

J. Wallace, P. Hudson, D. Keech, 1976, Archives of biochemistry and biophysics.

Binding of complement component C1q by spectrin.

S. Easterbrook-Smith, A. Comis, 1986, Biochimica et biophysica acta.

Enhancement of the binding of C1q to immune complexes by polyethylene glycol.

B. Wines, S. Easterbrook-Smith, 1988, Molecular immunology.

Conformational changes in C1q upon binding to IgG oligomers

R. Vandenberg, S. Easterbrook-Smith, 1986, FEBS letters.

Evidence for arginine residues in the immunoglobulin-binding sites of human Clq.

S. Easterbrook-Smith, A. Comis, 1985, Biochimica et biophysica acta.

The effects of cleavage of the inter-chain disulphide bonds of rabbit IgG on its ability to bind C1q.

S. Easterbrook-Smith, J. Sutton, J. Alden, 1984, Biochimica et biophysica acta.

Activation of the binding of C1q to immune complexes by zinc

S. Easterbrook-Smith, S.B. Easterbrook-Smith, 1983, FEBS letters.

Evidence for histidine residues in the immunoglobulin-binding site of human C1q

S. Easterbrook-Smith, 1983, Bioscience reports.

Clusterin enhances the formation of insoluble immune complexes.

M. Wilson, S. Easterbrook-Smith, P. Roeth, 1991, Biochemical and biophysical research communications.

A reexamination of the role of clusterin as a complement regulator.

M. Wilson, S. Easterbrook-Smith, D. Humphreys, 1999, Experimental cell research.

C1q is a nucleotide binding protein and is responsible for the ability of clusterin preparations to promote immune complex formation.

S. Easterbrook-Smith, P. Roeth, 1996, Biochimica et biophysica acta.

Effects of glycosylation on the structure and function of the extracellular chaperone clusterin.

Elise M. Stewart, S. Moestrup, J. Aquilina, 2007, Biochemistry.

Mobility and symmetry in the Fc and pFc' fragments as probed by 1H NMR.

R. Dwek, P. Závodszky, J. Boyd, 1979, Molecular immunology.

Apolipoprotein J (clusterin) induces cholesterol export from macrophage-foam cells: a potential anti-atherogenic function?

R. Dean, I. Gelissen, M. Wilson, 1997, The Biochemical journal.

Characterization of the heparin-binding properties of human clusterin.

G. Pankhurst, S. Easterbrook-Smith, C. Bennett, 1998, Biochemistry.

A dye-binding assay for measurement of the binding of Cu(II) to proteins.

Lorna Wilkinson-White, S. Easterbrook-Smith, 2008, Journal of inorganic biochemistry.

The presence of histidine residues at or near the C1q binding site of rabbit immunoglobulin G.

M. McCall, S. Easterbrook-Smith, 1987, Biochimica et biophysica acta.

Pyruvate carboxylase: affinity labelling of the magnesium adenosine triphosphate binding site.

J. Wallace, D. Keech, S. Easterbrook-Smith, 1976, European journal of biochemistry.

RHP is antigenically related to factor H and binds to the globular heads of C1q.

M. Wilson, B. Wines, S. Easterbrook-Smith, 1992, Molecular immunology.

The atypical velocity response by pyruvate carboxylase to increasing concentrations of acetyl-coenzyme A.

J. Wallace, D. Keech, S. Easterbrook-Smith, 1979, The Biochemical journal.

The role of Fc:Fc interactions in insoluble immune complex formation and complement activation.

R. Vandenberg, S. Easterbrook-Smith, J. Alden, 1988, Molecular immunology.

Clusterin is a secreted mammalian chaperone.

M. Wilson, S. Easterbrook-Smith, M. Wilson, 2000, Trends in biochemical sciences.

Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off‐folding pathway

J. Carver, Mark R. Wilson, T. Treweek, 2002, FEBS letters.

Evidence that clusterin has discrete chaperone and ligand binding sites.

J. Lakins, J. Carver, Mark R. Wilson, 2002, Biochemistry.

Inhibition of serum complement haemolytic activity by lipid vesicles containing phosphatidylserine

S. Easterbrook-Smith, A. Comis, 1986, FEBS letters.

Clusterin binds by a multivalent mechanism to the Fc and Fab regions of IgG.

M. Wilson, S. Easterbrook-Smith, Mark R. Wilson, 1992, Biochimica et biophysica acta.

The Fab/c fragment of IgG produced by cleavage at cyanocysteine residues.

B. Wines, S. Easterbrook-Smith, 1991, Molecular immunology.

Mildly Acidic pH Activates the Extracellular Molecular Chaperone Clusterin*

J. Carver, M. Rybchyn, Mark R. Wilson, 2002, The Journal of Biological Chemistry.

Single-step purification of immunoglobulin M on C1q-Sepharose.

S. Easterbrook-Smith, R. Raison, A. Nethery, 1990, Journal of immunological methods.

Analysis of the inhibition of C1q binding to aggregated immunoglobulin.

S. Easterbrook-Smith, M. R. van Schravendijk, M. V. van Schravendijk, 1985, Molecular immunology.

The isolation of a globular fragment of rabbit immunoglobulin G probably corresponding to the intact C gamma 2 homology region.

R. Dwek, P. Závodszky, S. Easterbrook-Smith, 1979, Molecular immunology.

Serum Albumin Prevents Protein Aggregation and Amyloid Formation and Retains Chaperone-like Activity in the Presence of Physiological Ligands

A. Nunez, M. Sunde, S. Easterbrook-Smith, 2012, The Journal of Biological Chemistry.

The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin.

M. Rybchyn, Mark R. Wilson, J. Yerbury, 2005, Biochemistry.

Structural basis of recognition in the immune response.

R. Dwek, P. Závodszky, P. Gettins, 1978, Biochemical Society transactions.

Activation of the classical complement pathway by BioRex-70.

R. Vandenberg, S. Easterbrook-Smith, 1987, Immunology letters.

Characterization of the binding of Cu(II) and Zn(II) to transthyretin: effects on amyloid formation.

Lorna Wilkinson-White, S. Easterbrook-Smith, 2007, Biochemistry.

Proton-n.m.r. study of interaction of myelin basic protein with a monoclonal antibody.

W. Moore, G. Mendz, D. Linthicum, 1985, The Biochemical journal.

C1q binding to mitochondria: a possible artefact?

S. Easterbrook-Smith, A. Comis, Alfio Comis, 1985, FEBS letters.

pH-dependent changes in the in vitro ligand-binding properties and structure of human clusterin.

J. Wilce, G. Pankhurst, S. Easterbrook-Smith, 2000, Biochemistry.

Clusterin is a secreted mammalian chaperone.

S. Easterbrook-Smith, M. Wilson, 2000, Trends in biochemical sciences.