Danny M. Hatters

Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II.

The structural basis for amyloid formation by plasma apolipoproteins: a review.

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

Apolipoprotein E4 forms a molten globule. A potential basis for its association with disease.

Cross-linking and amyloid formation by N- and C-terminal cysteine derivatives of human apolipoprotein C-II.

Sedimentation velocity analysis of flexible macromolecules: self-association and tangling of amyloid fibrils.

Phospholipid complexation and association with apolipoprotein C-II: insights from mass spectrometry.

The circularization of amyloid fibrils formed by apolipoprotein C-II.

Fibrillar amyloid protein present in atheroma activates CD36 signal transduction.

Engineering conformational destabilization into mouse apolipoprotein E. A model for a unique property of human apolipoprotein E4.

Modulation of apolipoprotein E structure by domain interaction: differences in lipid-bound and lipid-free forms.

Model of biologically active apolipoprotein E bound to dipalmitoylphosphatidylcholine.

Apolipoprotein E structure: insights into function.

Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils.

Protein misfolding inside cells: the case of huntingtin and Huntington's disease.

Insight on the molecular envelope of lipid-bound apolipoprotein E from electron paramagnetic resonance spectroscopy.

Conformational detection of prion protein with biarsenical labeling and FlAsH fluorescence.

VLDL lipolysis products increase VLDL fluidity and convert apolipoprotein E4 into a more expanded conformation.

Conformation sensors that distinguish monomeric proteins from oligomers in live cells.

Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool.

Sedimentation velocity analysis of amyloid oligomers and fibrils using fluorescence detection.

Diagnostics for amyloid fibril formation: where to begin?