Sarah R Ball
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Explore the profile of Sarah R Ball including associated specialties, affiliations and a list of published articles.
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14
Citations
74
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Recent Articles
1.
Dear A, Teng X, Ball S, Lewin J, Horne R, Clow D, et al.
Chem Sci
. 2024 May;
15(19):7229-7242.
PMID: 38756798
The central hallmark of Parkinson's disease pathology is the aggregation of the α-synuclein protein, which, in its healthy form, is associated with lipid membranes. Purified monomeric α-synuclein is relatively stable...
2.
Chappard A, Leighton C, Saleeb R, Jeacock K, Ball S, Morris K, et al.
Angew Chem Weinheim Bergstr Ger
. 2024 Mar;
135(15):e202216771.
PMID: 38516037
Protein misfolding and aggregation into oligomeric and fibrillar structures is a common feature of many neurogenerative disorders. Single-molecule techniques have enabled characterization of these lowly abundant, highly heterogeneous protein aggregates,...
3.
Sullivan M, Lane S, McKenzie A, Ball S, Sunde M, Neely G, et al.
J Neuroinflammation
. 2024 Jan;
21(1):7.
PMID: 38178159
Background: Widescale evidence points to the involvement of glia and immune pathways in the progression of Alzheimer's disease (AD). AD-associated iPSC-derived glial cells show a diverse range of AD-related phenotypic...
4.
Saleeb R, Leighton C, Lee J, OShaughnessy J, Jeacock K, Chappard A, et al.
Sci Adv
. 2023 Nov;
9(46):eadi7359.
PMID: 37967183
Protein misfolding and aggregation is a characteristic of many neurodegenerative disorders, including Alzheimer's and Parkinson's disease. The oligomers generated during aggregation are likely involved in disease pathogenesis and present promising...
5.
Siddiquee R, Lo V, Johnston C, Buffier A, Ball S, Ciofani J, et al.
Biomacromolecules
. 2023 Sep;
24(11):4783-4797.
PMID: 37747808
Hydrophobins are remarkable proteins due to their ability to self-assemble into amphipathic coatings that reverse surface wettability. Here, the versatility of the Class I hydrophobins EAS and DewY in diverse...
6.
Chappard A, Leighton C, Saleeb R, Jeacock K, Ball S, Morris K, et al.
Angew Chem Int Ed Engl
. 2023 Feb;
62(15):e202216771.
PMID: 36762870
Protein misfolding and aggregation into oligomeric and fibrillar structures is a common feature of many neurogenerative disorders. Single-molecule techniques have enabled characterization of these lowly abundant, highly heterogeneous protein aggregates,...
7.
Ball S, Adamson J, Sullivan M, Zimmermann M, Lo V, Sanz-Hernandez M, et al.
ACS Chem Neurosci
. 2022 Dec;
14(1):87-98.
PMID: 36542544
Alzheimer's disease is imposing a growing social and economic burden worldwide, and effective therapies are urgently required. One possible approach to modulation of the disease outcome is to use small...
8.
Baker M, Shanmugam N, Pham C, Ball S, Sierecki E, Gambin Y, et al.
Molecules
. 2022 Jun;
27(11).
PMID: 35684320
TIR-domain-containing adapter-inducing interferon-β (TRIF) is an innate immune protein that serves as an adaptor for multiple cellular signalling outcomes in the context of infection. TRIF is activated via ligation of...
9.
Kaur A, Adair L, Ball S, New E, Sunde M
Angew Chem Int Ed Engl
. 2021 Dec;
61(10):e202112832.
PMID: 34935241
Many soluble proteins can self-assemble into macromolecular structures called amyloids, a subset of which are implicated in a range of neurodegenerative disorders. The nanoscale size and structural heterogeneity of prefibrillar...
10.
Graziotto M, Adair L, Kaur A, Verite P, Ball S, Sunde M, et al.
RSC Chem Biol
. 2021 Oct;
2(5):1491-1498.
PMID: 34704054
Fluorescent probes for biological imaging have revealed much about the functions of biomolecules in health and disease. Fluorogenic probes, which are fluorescent only upon a bioorthogonal reaction with a specific...