H
Heath Ecroyd
Researcher at University of Wollongong
Publications - 109
Citations - 6116
Heath Ecroyd is an academic researcher from University of Wollongong. The author has contributed to research in topics: Protein aggregation & Chaperone (protein). The author has an hindex of 42, co-authored 105 publications receiving 5318 citations. Previous affiliations of Heath Ecroyd include Illawarra Health & Medical Research Institute & Centre national de la recherche scientifique.
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The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds
TL;DR: The Congo red spectral shift assay is demonstrated as a more viable spectrophotometric alternative to ThT, but allied methods, such as transmission electron microscopy, should also be used to assess fibril formation independently of dye‐based assays.
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Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foods
TL;DR: The ability to suppress amyloid fibril formation by forming an alternative amorphous aggregate is also not unique to caseins and underlies the action of molecular chaperones such as the small heat-shock proteins as discussed by the authors.
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Crystallin proteins and amyloid fibrils
Heath Ecroyd,John A. Carver +1 more
TL;DR: The ability of sHsps to prevent fibril formation, their mechanisms of action and the possible in vivo consequences of such associations are discussed, along with the potential use of fibrillar crystallin proteins as bionanomaterials.
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Post-testicular sperm environment and fertility
Jean-Luc Gatti,Sandrine Castella,Françoise Dacheux,Heath Ecroyd,Sonia Métayer,Véronique Thimon,Jean-Louis Dacheux +6 more
TL;DR: It is found that the main secreted proteins are common in different species and that enzymatic activities, capable of controlling the sperm surface changes, are present in the fluid.
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The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity
Georg K. A. Hochberg,Heath Ecroyd,Heath Ecroyd,Cong Liu,Cong Liu,Cong Liu,Dezerae Cox,Dezerae Cox,Duilio Cascio,Duilio Cascio,Duilio Cascio,Michael R. Sawaya,Michael R. Sawaya,Michael R. Sawaya,Miranda P. Collier,James C. Stroud,James C. Stroud,James C. Stroud,John A. Carver,Andrew Baldwin,Carol V. Robinson,David Eisenberg,David Eisenberg,Justin L. P. Benesch,Arthur Laganowsky +24 more
TL;DR: It is found that the core domain of the human molecular chaperone αB-crystallin can function effectively in preventing protein aggregation and amyloid toxicity, and is designed as an equivalently locked cABC to investigate the functional role played by oligomerization, disordered N and C termini, subunit exchange, and variable dimer interfaces in ABC.