Author

H. Ecroyd

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Cell Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Research Focus:cell type annotation· 2 Assay:fluorescence / live-cell microscopy· 2 Organism:human· 2 Assay:proteomics· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

A. M. van Oijen· 2 shared B. Paudel· 2 shared C. L. Johnston· 2 shared N. R. Marzano· 2 shared A. K. Walker· 1 shared A. van Oijen· 1 shared B. P. Paudel· 1 shared D. Cox· 1 shared

Activity by Year

2020-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

A. M. van Oijen

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Author profile →

5 papers

Recent·Most cited

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

N. Marzano, B. Paudel, A. van Oijen, H. Ecroyd

This study uses single-molecule techniques to observe Hsp70 chaperone interactions during protein folding, revealing binding cycles and distinct mechanisms for DnaJ and DnaK.

bioRxiv · May 9, 2022Biochemistry

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

S. McMahon, S. Bergink, H. H. Kampinga, H. Ecroyd

This study shows DNAJB chaperones inhibit FlucDM aggregation via proteasome-mediated degradation, using a C-terminal region distinct from that preventing amyloid formation.

bioRxiv · Oct 8, 2020Cell Biology

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

N. R. Marzano, K. M. Wray, C. L. Johnston, B. P. Paudel, Y. Hong, A. M. van Oijen, H. Ecroyd

This paper introduces ASCP, a fluorescent probe with enhanced sensitivity and specificity for detecting amyloid fibrils and oligomeric intermediates compared to ThT.

bioRxiv · Jun 25, 2020Biochemistry

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

C. L. Johnston, N. R. Marzano, B. Paudel, G. Wright, J. L. P. Benesch, A. M. van Oijen, H. Ecroyd

This study uses single-molecule fluorescence to reveal a two-step mechanism by which human Bc (HSPB5) interacts with misfolded proteins to prevent aggregation.

bioRxiv · Feb 16, 2020Biochemistry

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

R. San Gil, D. Cox, L. McAlary, T. Berg, A. K. Walker, J. J. Yerbury, L. Ooi, H. Ecroyd

This study shows that neurodegenerative disease-associated protein aggregates fail to induce the heat shock response in neuronal-like cells, unlike non-pathogenic aggregation-prone proteins.

bioRxiv · Jan 6, 2020Cell Biology