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Amanda L Woerman

Explore the profile of Amanda L Woerman including associated specialties, affiliations and a list of published articles. Areas
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Articles 32
Citations 1221
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Recent Articles
1.
Szegvari E, Holec S, Woerman A
J Neurochem . 2025 Mar; 169(3):e70021. PMID: 40026260
Rodent models that accurately recapitulate key aspects of human disease have long been fundamental to the successful development of clinical interventions. This is greatly underscored in the neurodegenerative disease field,...
2.
Reis P, Holec S, Ezeiruaku C, Frost M, Brown C, Liu S, et al.
J Parkinsons Dis . 2025 Feb; 14(8):1543-1558. PMID: 39957201
Background: Multiple system atrophy (MSA) and Parkinson's disease (PD) are caused by misfolded α-synuclein spreading throughout the central nervous system. While familial PD is linked to several α-synuclein mutations, no...
3.
Holec S, Khedmatgozar C, Schure S, Pham T, Woerman A
PLoS Pathog . 2024 Dec; 20(12):e1012746. PMID: 39642110
In patients with synucleinopathies, the protein α-synuclein misfolds into multiple conformations, each of which determines whether a patient develops multiple system atrophy (MSA) or one of three Lewy body diseases...
4.
Woerman A, Luk K
J Parkinsons Dis . 2024 Jul; 14(6):1095-1103. PMID: 39031387
Pre-formed fibrils (PFFs) made from recombinant α-synuclein are broadly used throughout the field in cellular and animal models of Parkinson's disease. However, their ability to successfully recapitulate disease biology is...
5.
Reis P, Holec S, Ezeiruaku C, Frost M, Brown C, Liu S, et al.
bioRxiv . 2024 Jul; PMID: 39026799
Multiple system atrophy (MSA) and Parkinson's disease (PD) are caused by misfolded -synuclein spreading throughout the central nervous system. While familial PD is linked to several point mutations in -synuclein,...
6.
Burre J, Edwards R, Halliday G, Lang A, Lashuel H, Melki R, et al.
Mov Disord . 2024 Jul; 39(10):1663-1678. PMID: 38946200
Various forms of Parkinson's disease, including its common sporadic form, are characterized by prominent α-synuclein (αSyn) aggregation in affected brain regions. However, the role of αSyn in the pathogenesis and...
7.
Woerman A, Bartz J
Trends Neurosci . 2024 May; 47(7):538-550. PMID: 38806297
Prion diseases are a group of neurodegenerative disorders caused by misfolding of proteins into pathogenic conformations that self-template to spread disease. Although this mechanism is largely associated with the prion...
8.
Khedmatgozar C, Holec S, Woerman A
PLoS Pathog . 2024 Jan; 20(1):e1011920. PMID: 38271292
No abstract available.
9.
Zeng Z, Tsay K, Vijayan V, Frost M, Prakash S, Quddus A, et al.
bioRxiv . 2023 Jul; PMID: 37502998
The discovery by cryo-electron microscopy (cryo-EM) that the neu-ropathological hallmarks of different tauopathies, including Alzheimer's disease, corticobasal degeneration (CBD), and progressive supranuclear palsy (PSP), are caused by unique misfolded conformations...
10.
Holec S, Lee J, Oehler A, Batia L, Wiggins-Gamble A, Lau J, et al.
PLoS Pathog . 2022 Dec; 18(12):e1010956. PMID: 36454879
In multiple system atrophy (MSA), the α-synuclein protein misfolds into a self-templating prion conformation that spreads throughout the brain, leading to progressive neurodegeneration. While the E46K mutation in α-synuclein causes...