Author

L. C. Serpell

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

Biology Disciplines

Click to filter author papers

Biophysics· 5 Biochemistry· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 5 Research Focus:protein folding & dynamics· 4 Organism:human· 3 Assay:proteomics· 3 Research Focus:cell type annotation· 2 Approach:microscopy & imaging analysis· 2 Assay:cryo-EM· 1 Assay:electronic health records· 1

Frequent Co-Authors

G. Burra· 3 shared C. M. Wischik· 2 shared L. Lutter· 2 shared M. B. Maina· 2 shared W.-F. Xue· 2 shared Y. Al-Hilaly· 2 shared A. B. Siemer· 1 shared A. K. Thakur· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiophysics

G. Burra

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Structural reconstruction of individual filaments in Abeta42 fibril populations assembled in vitro reveal rare species that resemble ex vivo amyloid polymorphs from human brains

L. D. Aubrey, L. Lutter, K. Fennell, T. J. Purton, N. Ward, L. C. Serpell, W.-F. Xue

The paper uses atomic force microscopy and cryo-electron microscopy to analyze Aβ42 fibril structures in vitro, identifying rare polymorphs similar to those found in human brain amyloid.

bioRxiv · Jul 14, 2023 · PreprintBiophysics

Solid-state NMR of paired helical filaments formed by the core tau fragment tau(297-391)

Y. K. Al-Hilaly, C. Hurt, J. E. Rickard, C. R. Harrington, J. M. D. Storey, C. M. Wischik, L. C. Serpell, A. B. Siemer

This study uses solid-state NMR to analyze tau(297-391) filaments, showing that non-reducing conditions lead to more dynamic and less ordered structures compared to those with DTT.

bioRxiv · Jun 9, 2022 · PreprintBiophysics

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

Structural identification of individual helical amyloid filaments by integration of cryo-electron microscopy-derived maps in comparative morphometric atomic force microscopy image analysis

L. Lutter, Y. Al-Hilaly, C. J. Serpell, M. F. Tuite, C. M. Wischik, L. C. Serpell, W.-F. Xue

This paper develops a method to identify individual amyloid fibril structures using AFM with cryo-EM maps, showing dGAE fibrils are structurally distinct from heparin-induced tau fibrils and related to Alzheimer's PHFs.

bioRxiv · Oct 19, 2021Biophysics

Cell-derived hexameric β-amyloid: a novel insight into composition, self-assembly and nucleating properties

D. M. Vadukul, C. Vrancx, P. Burguet, S. Contino, N. Suelves, L. C. Serpell, L. Quinton, P. Kienlen-Campard

This study identifies and characterizes cell-derived hexameric Aβ42, showing its nucleating properties and dependence on monomer availability in amyloid self-assembly.

bioRxiv · Dec 15, 2020 · PreprintBiochemistry

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