H. Ecroyd

发表

Role of the epididymis in sperm competition.

B. Nixon, Russell C. Jones, J. Dacheux, 2007, Asian journal of andrology.

Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein.

J. Carver, M. Sunde, H. Ecroyd, 2008, Biochemistry.

The two-faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity

J. Carver, H. Ecroyd, D. C. Thorn, 2009 .

Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation*

J. Carver, D. Cox, H. Ecroyd, 2016, The Journal of Biological Chemistry.

Proteomics Approaches for Biomarker and Drug Target Discovery in ALS and FTD

A. Walker, H. Ecroyd, R. San Gil, 2019, Front. Neurosci..

Using Single-Molecule Approaches to Understand the Molecular Mechanisms of Heat-Shock Protein Chaperone Function.

Antoine M. van Oijen, A. V. van Oijen, H. Ecroyd, 2018, Journal of molecular biology.

Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity.

C. Robinson, C. MacPhee, J. Carver, 2007, The Biochemical journal.

AR-12 Inhibits Chaperone Proteins Preventing Virus Replication and the Accumulation of Toxic Misfolded Proteins

P. Dent, E. Damonte, M. Tuñón, 2016, Journal of clinical & cellular immunology.

AR‐12 Inhibits Multiple Chaperones Concomitant With Stimulating Autophagosome Formation Collectively Preventing Virus Replication

P. Dent, C. García, Federico Giovannoni, 2016, Journal of cellular physiology.

Exploiting flow cytometry for the unbiased quantification of protein inclusions in Caenorhabditis elegans

Y. Chew, H. Ecroyd, Kristian Claesson, 2022, Journal of neurochemistry.

Real-time single-molecule observation of chaperone-assisted protein folding

Antoine M. van Oijen, A. V. van Oijen, B. Paudel, 2022, bioRxiv.

Stress in native grasses under ecologically relevant heat waves

S. Robinson, K. French, H. Ecroyd, 2018, PloS one.

Formation and Dissociation of Sperm Bundles in Monotremes1

B. Nixon, V. Labas, Russell C. Jones, 2016, Biology of reproduction.

Monotremes provide a key to understanding the evolutionary significance of epididymal sperm maturation.

B. Nixon, Russell C. Jones, J. Dacheux, 2011, Journal of andrology.

Multi-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone function

B. Shuch, C. Chen, Dasheng Wang, 2016, Oncotarget.

De Novo Design, Synthesis, and Mechanistic Evaluation of Short Peptides That Mimic Heat Shock Protein 27 Activity.

H. Ecroyd, W. Donald, S. McAlpine, 2021, ACS medicinal chemistry letters.

Regional Differences in Heat Shock Protein 25 Expression in Brain and Spinal Cord Astrocytes of Wild-Type and SOD1 G93A Mice

B. Kalmar, L. Greensmith, H. Ecroyd, 2021, Cells.

Post-testicular sperm maturation and identification of an epididymal protein in the Japanese quail (Coturnix coturnix japonica).

B. Nixon, J. Clulow, Russell C. Jones, 2014, Reproduction.

The development of signal transduction pathways during epididymal maturation is calcium dependent.

R. Aitken, Russell C. Jones, H. Ecroyd, 2004, Developmental biology.

Endogenous Redox Activity in Mouse Spermatozoa and Its Role in Regulating the Tyrosine Phosphorylation Events Associated with Sperm Capacitation1

R. Aitken, Russell C. Jones, H. Ecroyd, 2003, Biology of reproduction.

SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation

Elise M. Stewart, C. Dobson, G. Guillemin, 2015, Molecular Neurodegeneration.

Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms

C. Dobson, Mark R. Wilson, H. Ecroyd, 2013, FEBS letters.

Amyloid fibrils from readily available sources: milk casein and lens crystallin proteins.

J. Carver, J. Gerrard, M. Garvey, 2013, Methods in molecular biology.

Phosphomimics Destabilize Hsp 27 Oligomeric Assemblies and Enhance Chaperone Activity Graphical

Blagojce Jovcevski, J. Benesch, J. Aquilina, 2022 .

N- and C-terminal regions of αB-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation

P. Gooley, D. Cox, H. Ecroyd, 2020, The Journal of Biological Chemistry.

The small heat shock proteins B-crystallin and Hsp 27 suppress SOD 1 aggregation in vitro

H. Ecroyd, J. Yerbury, D. Gower, 2016 .

The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation

J. Carver, K. Bremmell, J. Regini, 2010, Molecular vision.

The epididymal soluble prion protein forms a high-molecular-mass complex in association with hydrophobic proteins.

J. Gatti, M. Belghazi, J. Dacheux, 2005, The Biochemical journal.

Proteostasis and the Regulation of Intra- and Extracellular Protein Aggregation by ATP-Independent Molecular Chaperones: Lens α-Crystallins and Milk Caseins.

J. Carver, R. Truscott, C. Holt, 2018, Accounts of chemical research.

Carboxymethylated-kappa-casein: a convenient tool for the identification of polyphenolic inhibitors of amyloid fibril formation.

J. Carver, H. Ecroyd, Yanqin Liu, 2010, Bioorganic & medicinal chemistry.

Single-molecule fluorescence-based approach reveals novel mechanistic insights into human small heat shock protein chaperone function

Antoine M. van Oijen, A. V. van Oijen, J. Benesch, 2020, The Journal of biological chemistry.

Single-molecule fluorescence-based approach reveals novel mechanistic insights into small heat shock protein chaperone function

Antoine M. van Oijen, A. V. van Oijen, J. Benesch, 2020, bioRxiv.

An Epididymal Form of Cauxin, a Carboxylesterase-Like Enzyme, Is Present and Active in Mammalian Male Reproductive Fluids1

J. Gatti, T. Yamashita, M. Belghazi, 2006, Biology of reproduction.

The monomeric α-crystallin domain of the small heat-shock proteins αB-crystallin and Hsp27 binds amyloid fibril ends.

P. Gooley, H. Ecroyd, M. Griffin, 2022, Journal of molecular biology.

Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins.

C. Dobson, M. Vendruscolo, C. MacPhee, 2007, Journal of molecular biology.

The contribution of proteomics to understanding epididymal maturation of mammalian spermatozoa

V. Labas, J. Gatti, C. Belleannée, 2012, Systems biology in reproductive medicine.

Casein structures in the context of unfolded proteins

J. Carver, C. Holt, H. Ecroyd, 2015 .

Post-testicular sperm environment and fertility.

J. Gatti, J. Dacheux, H. Ecroyd, 2004, Animal reproduction science.

Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foods.

J. Carver, C. Holt, H. Ecroyd, 2013, Journal of dairy science.

The Effect of Milk Constituents and Crowding Agents on Amyloid Fibril Formation by κ-Casein.

J. Carver, Jihua Liu, H. Ecroyd, 2016, Journal of agricultural and food chemistry.

Polymorphism in Casein Protein Aggregation and Amyloid Fibril Formation

J. Carver, H. Ecroyd, D. C. Thorn, 2014 .

AlphaB-crystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide

J. Carver, I. Musgrave, H. Ecroyd, 2014 .

αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide

J. Carver, I. Musgrave, H. Ecroyd, 2010, Cell Stress and Chaperones.

Dissociation from the Oligomeric State Is the Rate-limiting Step in Fibril Formation by κ-Casein*

Danielle M. Williams, P. Hoffmann, J. Carver, 2008, Journal of Biological Chemistry.

Native disulphide-linked dimers facilitate amyloid fibril formation by bovine milk αS2-casein.

Glyn L. Devlin, P. Hoffmann, J. Carver, 2020, Biophysical chemistry.

Extracellular chaperones and proteostasis.

Mark R. Wilson, H. Ecroyd, J. Yerbury, 2013, Annual review of biochemistry.

The dissociated form of kappa-casein is the precursor to its amyloid fibril formation.

J. Carver, H. Ecroyd, D. C. Thorn, 2010, The Biochemical journal.

Post-testicular sperm maturation and identiﬁcation of an epididymal protein in the Japanese quail (

B. Nixon, J. Clulow, Russell C. Jones, 2014 .

Preparation, processing and applications of protein nanofibers

J. Carver, J. Gerrard, M. Garvey, 2013 .

Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils

J. Carver, J. Gerrard, M. Garvey, 2017, Biomolecules.

Site-Directed Mutations in the C-Terminal Extension of Human αB-Crystallin Affect Chaperone Function and Block Amyloid Fibril Formation

Danielle M. Williams, J. Carver, H. Ecroyd, 2007, PloS one.

Tyrosine Phosphorylation of HSP-90 During Mammalian Sperm Capacitation1

R. Aitken, Russell C. Jones, H. Ecroyd, 2003, Biology of reproduction.

Small heat-shock proteins: important players in regulating cellular proteostasis

J. Carver, H. Ecroyd, T. Treweek, 2015, Cellular and Molecular Life Sciences.

Testicular descent, sperm maturation and capacitation. Lessons from our most distant relatives, the monotremes.

B. Nixon, J. Dacheux, H. Ecroyd, 2009, Reproduction, fertility, and development.

The growing world of small heat shock proteins: from structure to functions

B. Brundel, H. Kampinga, C. Emanuelsson, 2017, Cell Stress and Chaperones.

The heat shock response in neurons and astroglia and its role in neurodegenerative diseases

H. Ecroyd, L. Ooi, J. Yerbury, 2017, Molecular Neurodegeneration.

DNAJB chaperones suppress destabilised protein aggregation via a region unique from that used to inhibit amyloidogenesis.

H. Kampinga, Steven Bergink, H. Ecroyd, 2021, Journal of cell science.

DNAJB chaperones inhibit aggregation of destabilised proteins via a C-terminal region distinct from that used to prevent amyloid formation

H. Kampinga, Steven Bergink, H. Ecroyd, 2020, bioRxiv.

New proteins identified in epididymal fluid from the platypus (Ornithorhynchus anatinus).

B. Nixon, V. Labas, J. Dacheux, 2009, Reproduction, fertility, and development.

Compartmentalization of Prion Isoforms Within the Reproductive Tract of the Ram1

P. Sarradin, J. Gatti, J. Dacheux, 2004, Biology of reproduction.

The small heat shock proteins αB-crystallin and Hsp27 suppress SOD1 aggregation in vitro

Jodi A. Lee, H. Ecroyd, J. Yerbury, 2013, Cell Stress and Chaperones.

Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic a-Synuclein Oligomers Graphical

C. Dobson, D. Klenerman, M. Horrocks, 2018 .

Walking the tightrope: proteostasis and neurodegenerative disease

A. Dillin, D. Saunders, P. Beart, 2016, Journal of neurochemistry.

High tolerance of repeated heatwaves in Australian native plants

S. Robinson, M. Ashcroft, K. French, 2019, Austral Ecology.

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

Tak W. Kee, J. Carver, S. Hudson, 2009, The FEBS journal.

Extracellular Chaperones

Mark R. Wilson, H. Ecroyd, J. Yerbury, 2012 .

Extracellular Chaperones.

Mark R. Wilson, H. Ecroyd, J. Yerbury, 2010, Topics in current chemistry.

The small heat shock proteins αB-crystallin and Hsp27 suppress SOD1 aggregation in vitro

Jodi A. Lee, H. Ecroyd, J. Yerbury, 2012, Cell Stress and Chaperones.

Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches

Antoine M. van Oijen, A. V. van Oijen, H. Ecroyd, 2021, Computational and structural biotechnology journal.

Preventing α-synuclein aggregation: the role of the small heat-shock molecular chaperone proteins.

J. Carver, D. Cox, H. Ecroyd, 2014, Biochimica et biophysica acta.

Monitoring Early-Stage Protein Aggregation by an Aggregation-Induced Emission Fluorogen.

Yuning Hong, J. Carver, H. Ecroyd, 2017, Analytical chemistry.

Binding of the molecular chaperone alphaB-crystallin to Abeta amyloid fibrils inhibits fibril elongation

Alexander K. Buell, C. Dobson, M. Welland, 2020 .

Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation.

Alexander K. Buell, C. Dobson, M. Welland, 2011, Biophysical journal.

Proteostasis in the Male and Female Germline: A New Outlook on the Maintenance of Reproductive Health

E. Bromfield, B. Nixon, Shenae L. Cafe, 2021, Frontiers in Cell and Developmental Biology.

Effect of molecular chaperones on aberrant protein oligomers in vitro: super-versus sub-stoichiometric chaperone concentrations

C. Dobson, F. Chiti, Mark R. Wilson, 2016, Biological chemistry.

The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins

J. Carver, H. Ecroyd, R. Quinlan, 2017, Cell Stress and Chaperones.

Characterisation of Amyloid Fibril Formation by Small Heat-shock Chaperone Proteins Human αA-, αB- and R120G αB-Crystallins

C. Dobson, M. Vendruscolo, C. MacPhee, 2007 .

Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation

Martin J. Scanlon, Amy L. Robertson, Stephen P. Bottomley, 2010, Proceedings of the National Academy of Sciences.

Small heat shock proteins: multifaceted proteins with important implications for life

Tangchun Wu, R. Klevit, J. Carver, 2019, Cell Stress and Chaperones.

Rapid flow cytometric measurement of protein inclusions and nuclear trafficking

M. Wilson, H. Ecroyd, J. Yerbury, 2016, Scientific Reports.

Molecular Dynamics Analysis of Apolipoprotein-D - Lipid Hydroperoxide Interactions: Mechanism for Selective Oxidation of Met-93

B. Garner, A. Oakley, H. Ecroyd, 2012, PloS one.

(-)-epigallocatechin-3-gallate (EGCG) maintains kappa-casein in its pre-fibrillar state without redirecting its aggregation pathway.

J. Carver, S. Hudson, I. Musgrave, 2009, Journal of molecular biology.

Structural and Functional Aspects of Hetero-oligomers Formed by the Small Heat Shock Proteins αB-Crystallin and HSP27*

Amie M. Morris, J. Aquilina, H. Ecroyd, 2013, The Journal of Biological Chemistry.

Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers

C. Dobson, D. Klenerman, M. Horrocks, 2018, Cell reports.

The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity

Antoine M. van Oijen, C. Dobson, D. Klenerman, 2018, The Journal of Biological Chemistry.

Redefining the chaperone mechanism of sHsps: not just holdase chaperones

H. Ecroyd, 2015 .

Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity.

Blagojce Jovcevski, J. Benesch, J. Aquilina, 2015, Chemistry & biology.

Assessment of metal concentrations in the SOD1G93A mouse model of amyotrophic lateral sclerosis and its potential role in muscular denervation, with particular focus on muscle tissue

B. Kalmar, H. Ecroyd, J. Yerbury, 2018, Molecular and Cellular Neuroscience.

Assessment of metal concentrations in the SOD 1 G 93 A mouse model of 1 amyotrophic lateral sclerosis and its potential role in muscular denervation , with 2 particular focus on muscle tissue 3 4

B. Kalmar, H. Ecroyd, J. Yerbury, 2018 .

Longitudinal assessment of metal concentrations and copper isotope ratios in the G93A SOD1 mouse model of amyotrophic lateral sclerosis.

H. Ecroyd, J. Yerbury, A. Dosseto, 2017, Metallomics : integrated biometal science.

Analysis of the mechanism by which calcium negatively regulates the tyrosine phosphorylation cascade associated with sperm capacitation

R. Aitken, M. Baker, S. Roman, 2004, Journal of Cell Science.

The two-faced nature of small heat shock proteins: amyloid assembly and the inhibition of fibril formation. Relevance to disease states

J. Carver, H. Ecroyd, Sarah Meehan, 2010 .

Mimicking phosphorylation of αB-crystallin affects its chaperone activity

Cait E. MacPhee, Carol V. Robinson, Justin L. P. Benesch, 2007 .

Enhanced molecular chaperone activity of the small heat-shock protein alphaB-cystallin following covalent immobilization onto a solid-phase support.

H. Griesser, J. Shapter, J. Carver, 2011, Biopolymers.

High tolerance of repeated heatwaves in 1 Australian native plants 2 3

Robinson, M. Ashcroft, K. French, 2019 .

Unraveling the mysteries of protein folding and misfolding

J. Carver, H. Ecroyd, 2008, IUBMB life.

Crystallin proteins and amyloid fibrils

J. Carver, H. Ecroyd, John A. Carver, 2008, Cellular and Molecular Life Sciences.

Small heat shock proteins: multifaceted proteins with important implications for life

Tangchun Wu, R. Klevit, J. Carver, 2019, Cell Stress and Chaperones.

The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin

Blagojce Jovcevski, J. Benesch, H. Ecroyd, 2018, Cell stress & chaperones (Print).

An automated chromatography procedure optimized for analysis of stable Cu isotopes from biological materials

H. Ecroyd, A. Dosseto, M. P. Field, 2016 .

The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity

Georg K. A. Hochberg, D. Eisenberg, J. Stroud, 2014, Proceedings of the National Academy of Sciences.

The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin.

H. Ecroyd, Heath Ecroyd, Melissa Kulig, 2012, The Biochemical journal.

Using bicistronic constructs to evaluate the chaperone activities of heat shock proteins in cells

H. Ecroyd, R. San Gil, T. Berg, 2017, Scientific Reports.

Evaluating the Effect of Phosphorylation on the Structure and Dynamics of Hsp27 Dimers by Means of Ion Mobility Mass Spectrometry.

Blagojce Jovcevski, J. Benesch, J. Aquilina, 2017, Analytical chemistry.

Model for amorphous aggregation processes.

J. Carver, E. Waters, S. Stranks, 2009, Physical review. E, Statistical, nonlinear, and soft matter physics.

Analysis of the mechanism by which calcium negatively regulates the tyrosine phosphorylation cascade associated with sperm capacitation.

R. Aitken, M. Baker, S. Roman, 2003, Journal of cell science.

An α-cyanostilbene derivative for the enhanced detection and imaging of amyloid fibril aggregates

Antoine M. van Oijen, Yuning Hong, A. V. van Oijen, 2020, bioRxiv.

The Interaction of αB-Crystallin with Mature α-Synuclein Amyloid Fibrils Inhibits Their Elongation

C. Dobson, J. Skepper, M. Welland, 2010, Biophysical journal.

Neurodegenerative disease-associated protein aggregates are poor inducers of the heat shock response in neuronal cells

D. Cox, A. Walker, H. Ecroyd, 2020, Journal of Cell Science.

Exploiting flow cytometry for the unbiased quantification of protein inclusions in Caenorhabditis elegans

Yee Lian Chew, H. Ecroyd, Kristian Claesson, 2021, bioRxiv.

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

J. Carver, H. Ecroyd, M. Griffin, 2013, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

The small heat shock proteins αB-crystallin (HSPB5) and Hsp27 (HSPB1) inhibit the intracellular aggregation of α-synuclein

D. Cox, H. Ecroyd, Dezerae Cox, 2017, Cell Stress and Chaperones.

The beauty and complexity of the small heat shock proteins: a report on the proceedings of the fourth workshop on small heat shock proteins.

H. Taguchi, W. Lau, R. Klevit, 2023, Cell stress & chaperones.

NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ.

Danielle M. Williams, H. Fu, J. Carver, 2011, The Biochemical journal.

The effect of small molecules in modulating the chaperone activity of αB‐crystallin against ordered and disordered protein aggregation

J. Carver, H. Ecroyd, Heath Ecroyd, 2008, The FEBS journal.

CRISPR-mediated adaptive immune systems in bacteria and archaea.

Rotem Sorek, Mark R. Wilson, J. Berger, 2013, Annual review of biochemistry.

Photosystem II: the reaction center of oxygenic photosynthesis.

David W. Russell, J. Berger, David J. Vinyard, 2013, Annual review of biochemistry.

Explorer Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic -Synuclein Oligomers

D. Klenerman, M. Horrocks, H. Ecroyd, 2018 .

Explorer Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic -Synuclein Oligomers

D. Klenerman, M. Horrocks, H. Ecroyd, 2018 .

Structural and Functional Aspects of Hetero-oligomers Formed by the Small Heat Shock Proteins αB-Crystallin and HSP27*

Amie M. Morris, J. Aquilina, H. Ecroyd, 2013, The Journal of Biological Chemistry.

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

Tak W. Kee, J. Carver, S. Hudson, 2009, The FEBS journal.

Dissociation from the Oligomeric State Is the Rate-limiting Step in Fibril Formation by κ-Casein*

Danielle M. Williams, Glyn L. Devlin, P. Hoffmann, 2008, Journal of Biological Chemistry.

Extracellular chaperones.

Mark R. Wilson, H. Ecroyd, J. Yerbury, 2013, Topics in current chemistry.

Crystallin proteins and amyloid fibrils

J. Carver, H. Ecroyd, 2008, Cellular and Molecular Life Sciences.

Mimicking phosphorylation of αB-crystallin affects its chaperone activity

C. Robinson, C. MacPhee, J. Carver, 2007 .