Author

H. Y. Gastall

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· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Organism:human· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Approach:experimental assay· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

I. Pritisanac· 2 shared J. L. P. Benesch· 2 shared T. R. Alderson· 2 shared A. Baldwin· 1 shared A. Bax· 1 shared A. J. Baldwin· 1 shared B. Asselbergh· 1 shared E. Adriaenssens· 1 shared

Activity by Year

2018-2019 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersBiochemistry

I. Pritisanac

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2 papers

Recent·Most cited

BiochemistrybioRxivPreprintSep 10, 2019

Dysregulated interactions triggered by a neuropathy-causing mutation in the IPV motif of HSP27

T. R. Alderson, E. Adriaenssens, B. Asselbergh…·J. L. P. Benesch

This study investigates how the P182L mutation in HSP27's IxI/V motif disrupts protein interactions, leading to aggregation and disease.

DOI 10.1101/708180

humanproteomics

𝕏 PostBluesky

BiophysicsbioRxivJun 14, 2018

Local unfolding of the HSP27 monomer regulates chaperone activity

T. R. Alderson, J. Roche, H. Y. Gastall…·A. J. Baldwin

This study shows that redox-induced monomerization of HSP27 enhances its chaperone activity but also increases aggregation risk, with mutations in an unstructured region linked to neuropathies.

DOI 10.1038/s41467-019-08557-8

humanprotein structure

𝕏 PostBluesky