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Article: Highly tunable bimane-based fluorescent probes: design, synthesis, and application as a selective amyloid binding dye.

Venkatesh, Yarra / Marotta, Nicholas P / Lee, Virginia M-Y / Petersson, E James

2024 Volume 15, Issue 16, Page(s) 6053–6063

Abstract: Small molecule fluorescent probes are indispensable tools for a broad range of biological applications. Despite many probes being available, there is still a need for probes where photophysical properties and biological selectivity can be tuned as ... ...

Abstract	Small molecule fluorescent probes are indispensable tools for a broad range of biological applications. Despite many probes being available, there is still a need for probes where photophysical properties and biological selectivity can be tuned as desired. Here, we report the rational design and synthesis of a palette of fluorescent probes based on the underexplored bimane scaffold. The newly developed probes with varied electronic properties show tunable absorption and emission in the visible region with large Stokes shifts. Probes featuring electron-donating groups exhibit rotor effects that are sensitive to polarity and viscosity by "intramolecular charge transfer" (ICT) and twisted intramolecular charge transfer (TICT) mechanisms, respectively. These properties enable their application as "turn-on" fluorescent probes to detect fibrillar aggregates of the α-synuclein (αS) protein that are a hallmark of Parkinson's disease (PD). One probe shows selective binding to αS fibrils relative to soluble proteins in cell lysates and amyloid fibrils of tau and amyloid-β. Finally, we demonstrate the diagnostic potential of the probe in selectively detecting αS fibrils amplified from PD with dementia (PDD) patient samples.
Language	English
Publishing date	2024-03-26
Publishing country	England
Document type	Journal Article
ZDB-ID	2559110-1
ISSN	2041-6539 ; 2041-6520
ISSN (online)	2041-6539
ISSN	2041-6520
DOI	10.1039/d4sc00024b
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: In Vitro Amplification of Pathogenic Tau Seeds from Neurodegenerative Disease Patient Brains.

Xu, Hong / Lee, Virginia M-Y

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2561, Page(s) 279–292

Abstract: Aggregated microtubule-associated protein tau (tau) is the hallmark lesion of a group of neurodegenerative diseases, termed tauopathies. Normal endogenous tau is highly soluble and intrinsically disordered when it is not bound to microtubules. ... ...

Abstract	Aggregated microtubule-associated protein tau (tau) is the hallmark lesion of a group of neurodegenerative diseases, termed tauopathies. Normal endogenous tau is highly soluble and intrinsically disordered when it is not bound to microtubules. Pathological tau proteins are aggregates of bioactive filaments capable of inducing their normal counterparts into pathological conformations that are human tauopathy dependent. Taking advantage of this feature, we established an in vitro seeding reaction to amplify faithfully human-derived tau strains. This approach allows us to expand the quantity and improve the quality of pathogenic tau strains derived from human patient postmortem brains and to further understand tau pathogenesis in models of tauopathy. Here, we describe the approach to generate human pathogenic tau using human-derived tau seeds and recombinant human tau in vitro.
MeSH term(s)	Humans ; tau Proteins/genetics ; tau Proteins/metabolism ; Neurodegenerative Diseases/metabolism ; Tauopathies/metabolism ; Brain/metabolism ; Autopsy
Chemical Substances	tau Proteins
Language	English
Publishing date	2022-11-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2655-9_15
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Book: Fatal attractions

Lee, Virginia M.-Y.

protein aggregates in neurodegenerative disorders ; with 7 tables ; [meeting in Paris on April 12, 1999]

(Research and perspectives in Alzheimer's disease)

2000

Institution	Fondation IPSEN pour la recherche thérapeutique
Author's details	[Fondation IPSEN pour la Recherche Therapeutique]. V. M.-Y. Lee ... (ed.)
Series title	Research and perspectives in Alzheimer's disease
Keywords	Neurodegenerative Diseases / etiology ; Mutation / genetics ; Neurodegenarative Diseases / genetics ; Nervendegeneration ; Tau-Protein ; Mutation ; Alzheimerkrankheit ; Parkinson-Krankheit
Subject	Protein Tau ; Schüttellähmung ; Paralysis agitans ; Idiopathischer Parkinsonismus ; Morbus Parkinson ; Alzheimer-Krankheit ; Alzheimersche Krankheit ; Alzheimer-Demenz ; Morbus Alzheimer ; Greisenblödsinn ; Alzheimer's Disease ; Neurodegenerative Krankheit ; Neurodegenerative Erkrankung
Language	English
Size	XII, 140 S. : Ill., graph. Darst.
Publisher	Springer
Publishing place	Berlin u.a.
Publishing country	Germany
Document type	Book
HBZ-ID	HT012787704
ISBN	3-540-67172-2 ; 978-3-540-67172-5
Database	Catalogue ZB MED Medicine, Health

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2000 A 3719	order for loan	Magazin

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Article ; Online: Modeling the cellular fate of alpha-synuclein aggregates: A pathway to pathology.

Marotta, Nicholas P / Lee, Virginia M-Y

Current opinion in neurobiology

2022 Volume 72, Page(s) 171–177

Abstract: Parkinson's disease is a progressive neurodegenerative disorder that is characterized by pathological protein inclusions that form in the brains of patients, leading to neuron loss and the observed clinical symptoms. These inclusions, containing ... ...

Abstract	Parkinson's disease is a progressive neurodegenerative disorder that is characterized by pathological protein inclusions that form in the brains of patients, leading to neuron loss and the observed clinical symptoms. These inclusions, containing aggregates of the protein α-Synuclein, spread throughout the brain as the disease progresses. This spreading follows patterns that inform our understanding of the disease. One way to further our understanding of disease progression is to model the discrete steps from when a cell first encounters an aggregate to when those aggregates propagate to new cells. This review will serve to highlight the recent progress made in the effort to better understand the mechanistic steps that determine how this propagation happens at the cellular level.
MeSH term(s)	Brain/metabolism ; Cell Differentiation ; Disease Progression ; Humans ; Parkinson Disease/pathology ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2022-02-04
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1078046-4
ISSN	1873-6882 ; 0959-4388
ISSN (online)	1873-6882
ISSN	0959-4388
DOI	10.1016/j.conb.2022.01.003
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Article: Manipulation of the diet-microbiota-brain axis in Alzheimer's disease.

Lee, Daniel / Lee, Virginia M-Y / Hur, Seong Kwon

Frontiers in neuroscience

2022 Volume 16, Page(s) 1042865

Abstract: Several studies investigating the pathogenesis of Alzheimer's disease have identified various interdependent constituents contributing to the exacerbation of the disease, including Aβ plaque formation, tau protein hyperphosphorylation, neurofibrillary ... ...

Abstract	Several studies investigating the pathogenesis of Alzheimer's disease have identified various interdependent constituents contributing to the exacerbation of the disease, including Aβ plaque formation, tau protein hyperphosphorylation, neurofibrillary tangle accumulation, glial inflammation, and the eventual loss of proper neural plasticity. Recently, using various models and human patients, another key factor has been established as an influential determinant in brain homeostasis: the gut-brain axis. The implications of a rapidly aging population and the absence of a definitive cure for Alzheimer's disease have prompted a search for non-pharmaceutical tools, of which gut-modulatory therapies targeting the gut-brain axis have shown promise. Yet multiple recent studies examining changes in human gut flora in response to various probiotics and environmental factors are limited and difficult to generalize; whether the state of the gut microbiota in Alzheimer's disease is a cause of the disease, a result of the disease, or both through numerous feedback loops in the gut-brain axis, remains unclear. However, preliminary findings of longitudinal studies conducted over the past decades have highlighted dietary interventions, especially Mediterranean diets, as preventative measures for Alzheimer's disease by reversing neuroinflammation, modifying the intestinal and blood-brain barrier (BBB), and addressing gut dysbiosis. Conversely, the consumption of Western diets intensifies the progression of Alzheimer's disease through genetic alterations, impaired barrier function, and chronic inflammation. This review aims to support the growing body of experimental and clinical data highlighting specific probiotic strains and particular dietary components in preventing Alzheimer's disease
Language	English
Publishing date	2022-11-04
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2411902-7
ISSN	1662-453X ; 1662-4548
ISSN (online)	1662-453X
ISSN	1662-4548
DOI	10.3389/fnins.2022.1042865
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Article ; Online: Identification of small molecules and related targets that modulate tau pathology in a seeded primary neuron model.

Gibbons, Garrett S / Gould, Hailey / Lee, Virginia M-Y / Crowe, Alex / Brunden, Kurt R

The Journal of biological chemistry

2023 Volume 299, Issue 7, Page(s) 104876

Abstract: Alzheimer's disease (AD) is characterized by the presence of tau protein inclusions and amyloid beta (Aβ) plaques in the brain, with Aβ peptides generated by cleavage of the amyloid precursor protein (APP) by BACE1 and γ-secretase. We previously ... ...

Abstract	Alzheimer's disease (AD) is characterized by the presence of tau protein inclusions and amyloid beta (Aβ) plaques in the brain, with Aβ peptides generated by cleavage of the amyloid precursor protein (APP) by BACE1 and γ-secretase. We previously described a primary rat neuron assay in which tau inclusions form from endogenous rat tau after seeding cells with insoluble tau isolated from the human AD brain. Here, we used this assay to screen an annotated library of ∼8700 biologically active small molecules for their ability to reduce immuno-stained neuronal tau inclusions. Compounds causing ≥30% inhibition of tau aggregates with <25% loss of DAPI-positive cell nuclei underwent further confirmation testing and assessment of neurotoxicity, and non-neurotoxic hits were subsequently analyzed for inhibitory activity in an orthogonal ELISA that quantified multimeric rat tau species. Of the 173 compounds meeting all criteria, a subset of 55 inhibitors underwent concentration-response testing and 46 elicited a concentration-dependent reduction of neuronal tau inclusions that were distinct from measures of toxicity. Among the confirmed inhibitors of tau pathology were BACE1 inhibitors, several of which, along with γ-secretase inhibitors/modulators, caused a concentration-dependent lowering of neuronal tau inclusions and a reduction of insoluble tau by immunoblotting, although they did not decrease soluble phosphorylated tau species. In conclusion, we have identified a diverse set of small molecules and related targets that reduce neuronal tau inclusions. Notably, these include BACE1 and γ-secretase inhibitors, suggesting that a cleavage product from a shared substrate, such as APP, might affect tau pathology.
MeSH term(s)	Animals ; Humans ; Rats ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Amyloid Precursor Protein Secretases/metabolism ; Aspartic Acid Endopeptidases/metabolism ; Neurons/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; Aspartic Acid Endopeptidases (EC 3.4.23.-) ; tau Proteins
Language	English
Publishing date	2023-06-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.104876
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Article ; Online: Author Correction: O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology.

Balana, Aaron T / Mahul-Mellier, Anne-Laure / Nguyen, Binh A / Horvath, Mian / Javed, Afraah / Hard, Eldon R / Jasiqi, Yllza / Singh, Preeti / Afrin, Shumaila / Pedretti, Rose / Singh, Virender / Lee, Virginia M-Y / Luk, Kelvin C / Saelices, Lorena / Lashuel, Hilal A / Pratt, Matthew R

Nature chemical biology

2024

Language	English
Publishing date	2024-02-27
Publishing country	United States
Document type	Published Erratum
ZDB-ID	2202962-X
ISSN	1552-4469 ; 1552-4450
ISSN (online)	1552-4469
ISSN	1552-4450
DOI	10.1038/s41589-024-01587-4
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Zs.A 6251: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Amyloid-Beta (Aβ) Plaques Promote Seeding and Spreading of Alpha-Synuclein and Tau in a Mouse Model of Lewy Body Disorders with Aβ Pathology.

Bassil, Fares / Brown, Hannah J / Pattabhiraman, Shankar / Iwasyk, Joe E / Maghames, Chantal M / Meymand, Emily S / Cox, Timothy O / Riddle, Dawn M / Zhang, Bin / Trojanowski, John Q / Lee, Virginia M-Y

Neuron

2023 Volume 111, Issue 22, Page(s) 3699

Language	English
Publishing date	2023-12-07
Publishing country	United States
Document type	Published Erratum
ZDB-ID	808167-0
ISSN	1097-4199 ; 0896-6273
ISSN (online)	1097-4199
ISSN	0896-6273
DOI	10.1016/j.neuron.2023.10.030
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Zs.A 2496: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 92: Show issues

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Article ; Online: Protein transmission in neurodegenerative disease.

Peng, Chao / Trojanowski, John Q / Lee, Virginia M-Y

Nature reviews. Neurology

2020 Volume 16, Issue 4, Page(s) 199–212

Abstract: Most neurodegenerative diseases are characterized by the intracellular or extracellular aggregation of misfolded proteins such as amyloid-β and tau in Alzheimer disease, α-synuclein in Parkinson disease, and TAR DNA-binding protein 43 in amyotrophic ... ...

Abstract	Most neurodegenerative diseases are characterized by the intracellular or extracellular aggregation of misfolded proteins such as amyloid-β and tau in Alzheimer disease, α-synuclein in Parkinson disease, and TAR DNA-binding protein 43 in amyotrophic lateral sclerosis. Accumulating evidence from both human studies and disease models indicates that intercellular transmission and the subsequent templated amplification of these misfolded proteins are involved in the onset and progression of various neurodegenerative diseases. The misfolded proteins that are transferred between cells are referred to as 'pathological seeds'. Recent studies have made exciting progress in identifying the characteristics of different pathological seeds, particularly those isolated from diseased brains. Advances have also been made in our understanding of the molecular mechanisms that regulate the transmission process, and the influence of the host cell on the conformation and properties of pathological seeds. The aim of this Review is to summarize our current knowledge of the cell-to-cell transmission of pathological proteins and to identify key questions for future investigation.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/metabolism ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Axonal Transport ; Brain/metabolism ; Brain/pathology ; Cell Communication ; DNA-Binding Proteins/metabolism ; Endocytosis ; Exosomes/metabolism ; Genetic Predisposition to Disease ; Humans ; Huntingtin Protein/metabolism ; Huntington Disease/metabolism ; Huntington Disease/pathology ; Membrane Fusion ; Nanotubes ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neuroglia/metabolism ; Neurons/metabolism ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/pathology ; Protein Transport ; alpha-Synuclein/metabolism ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; DNA-Binding Proteins ; Huntingtin Protein ; TARDBP protein, human ; alpha-Synuclein ; tau Proteins
Language	English
Publishing date	2020-03-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2491514-2
ISSN	1759-4766 ; 1759-4758
ISSN (online)	1759-4766
ISSN	1759-4758
DOI	10.1038/s41582-020-0333-7
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Zs.MG 88: Show issues

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Article ; Online: Fluent molecular mixing of Tau isoforms in Alzheimer’s disease neurofibrillary tangles

Aurelio J. Dregni / Pu Duan / Hong Xu / Lakshmi Changolkar / Nadia El Mammeri / Virginia M.-Y. Lee / Mei Hong

Nature Communications, Vol 13, Iss 1, Pp 1-

2022 Volume 11

Abstract: The tau protein in Alzheimer’s disease contains two isoforms. Using solid-state NMR and seeded growth of isotopically labeled tau, here the authors determined that the two isoforms mix fluently on the molecular level to propagate the AD tau structure. ...

Abstract	The tau protein in Alzheimer’s disease contains two isoforms. Using solid-state NMR and seeded growth of isotopically labeled tau, here the authors determined that the two isoforms mix fluently on the molecular level to propagate the AD tau structure.
Keywords	Science ; Q
Language	English
Publishing date	2022-05-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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