Author

G. Burra

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· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:proteomics· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Assay:protein sequence· 1 Organism:yeast· 1

Frequent Co-Authors

L. C. Serpell· 3 shared M. B. Maina· 3 shared K. Mengham· 2 shared A. K. Thakur· 1 shared A. Thakur· 1 shared C. Harrington· 1 shared C. Wischik· 1 shared K. E. Marshall· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiophysics

L. C. Serpell

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Dityrosine cross-links are present in Alzheimer's disease-derived tau oligomers and paired helical filaments (PHF) which promotes the stability of PHF-core tau (297-391) in vitro.

M. Maina, Y. Al-Hilaly, S. Oakley, G. Burra, T. Khanom, L. Biasetti, K. Mengham, K. E. Marshall, C. Harrington, C. Wischik, L. C. Serpell

This study shows dityrosine crosslinks are present in Alzheimer's disease tau oligomers and paired helical filaments, increasing their stability in vitro.

bioRxiv · May 28, 2022Biochemistry

GNNQQNY: Methodology for biophysical and structural understanding of aggregation

G. Burra, M. B. Maina, L. C. Serpell, A. Thakur

This study describes a solubilisation protocol for GNNQQNY peptides that enables the study of amyloid fibril formation kinetics and thermodynamics.

bioRxiv · Jan 1, 2022 · PreprintBiophysics

Nucleation-dependent aggregation kinetics of Yeast Sup35 fragment GNNQQNY

G. Burra, M. B. Maina, L. C. Serpell, A. K. Thakur

This study experimentally validates the nucleation-dependent aggregation kinetics of the yeast prion protein fragment GNNQQNY, showing temperature-dependent nucleation efficiency and amyloid fiber formation.

bioRxiv · Jul 27, 2020Biophysics

Dityrosine cross-link trapping of amyloid-β intermediates reveals that self-assembly is required for Aβ-induced cytotoxicity

M. B. Maina, K. Mengham, G. Burra, Y. A. Al-Hilaly, L. Serpell

This study shows DiY cross-linking stabilizes Aβ assemblies but does not induce toxicity, while oligomeric non-cross-linked Aβ is toxic to neuroblastoma cells.

bioRxiv · Mar 25, 2020 · PreprintBiochemistry