Macromolecular Self-Assembly of Amyloid Fibrils

Solution Conditions Affect the Ability of the K30D Mutation to Prevent Amyloid Fibril Formation by Apolipoprotein C-II: Insights from Experiments and Theoretical Simulations

Y Mao, N Todorova, CO Zlatic, PR Gooley, MDW Griffin, GJ Howlett, I Yarovsky

2016-07-12

Apolipoproteins form amphipathic helical structures that bind lipid surfaces. Paradoxically, lipid-free apolipoproteins display a ..

Hydrogen/Deuterium Exchange and Molecular Dynamics Analysis of Amyloid Fibrils Formed by a D69K Charge-Pair Mutant of Human Apolipoprotein C-II

Y Mao, CO Zlatic, MDW Griffin, GJ Howlett, N Todorova, I Yarovsky, PR Gooley

2015-08-11

Plasma apolipoproteins form amphipathic α helices in lipid environments but in the lipid-free state show a high propensity to form..

Charge and charge-pair mutations alter the rate of assembly and structural properties of apolipoprotein C-II amyloid fibrils

Y Mao, CL Teoh, S Yang, CO Zlatic, ZK Rosenes, PR Gooley, GJ Howlett, MDW Griffin

2015-02-17

The misfolding, aggregation, and accumulation of proteins as amyloid fibrils is a defining characteristic of several debilitating ..

Sedimentation Velocity Analysis of the Size Distribution of Amyloid Oligomers and Fibrils

YF Mok, GJ Howlett, MDW Griffin

2015-01-01

Amyloid fibrils result from the self-assembly of proteins into large aggregates with fibrillar morphology and common structural fe..

Avoiding the oligomeric state: αB-crystallin inhibits fragmentation and induces dissociation of apolipoprotein C-II amyloid fibrils

KJ Binger, H Ecroyd, S Yang, JA Carver, GJ Howlett, MDW Griffin

2013-03-01

The in vivo aggregation of proteins into amyloid fibrils suggests that cellular mechanisms that normally prevent or reverse this a..

Shear flow induced changes in apolipoprotein C-II conformation and amyloid fibril formation

CL Teoh, IB Bekard, P Asimakis, MDW Griffin, TM Ryan, DE Dunstan, GJ Howlett

2011-05-17

The misfolding and self-assembly of proteins into amyloid fibrils that occur in several debilitating diseases are affected by a va..

Sedimentation velocity analysis of amyloid oligomers and fibrils using fluorescence detection

YF Mok, TM Ryan, S Yang, DM Hatters, GJ Howlett, MDW Griffin

2011-05-01

The assembly of proteins into large fibrillar aggregates, known as amyloid fibrils, is associated with a number of common and debi..

High-affinity amphipathic modulators of amyloid fibril nucleation and elongation

TM Ryan, MDW Griffin, CL Teoh, J Ooi, GJ Howlett

2011-02-25

The misfolding and aggregation of proteins to form amyloid fibrils are associated with a number of debilitating, age-related disea..

A structural model for apolipoprotein C-II amyloid fibrils: Experimental characterization and molecular dynamics simulations

CL Teoh, CLL Pham, N Todorova, A Hung, CN Lincoln, E Lees, YH Lam, KJ Binger, NH Thomson, SE Radford, TA Smith, SA Müller, A Engel, MDW Griffin, I Yarovsky, PR Gooley, GJ Howlett

2011-02-04

The self-assembly of specific proteins to form insoluble amyloid fibrils is a characteristic feature of a number of age-related an..

Visualization of polymorphism in apolipoprotein C-II amyloid fibrils

CL Teoh, H Yagi, MDW Griffin, Y Goto, GJ Howlett

2011-01-01

The misfolding and self-assembly of proteins into amyloid fibrils, which occur in several debilitating and age-related diseases, a..

Phospholipids enhance nucleation but not elongation of apolipoprotein C-II amyloid fibrils

TM Ryan, CL Teoh, MDW Griffin, MF Bailey, P Schuck, GJ Howlett

2010-01-01

Amyloid fibrils and their oligomeric intermediates accumulate in several age-related diseases where their presence is considered t..