Michael Vigers
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View article: Structure‐specific Mini‐prion Model for Alzheimer's Disease Tau Fibrils
Structure‐specific Mini‐prion Model for Alzheimer's Disease Tau Fibrils Open
Background One of the most significant discoveries of the past decade is that tau protein assembles into amyloid fibrils with distinct, disease‐specific hallmark structures in each tauopathy. Tau pathology is thought to progress via a "pri…
View article: Structure-specific Mini-Prion Model for Alzheimer’s Disease Tau Fibrils
Structure-specific Mini-Prion Model for Alzheimer’s Disease Tau Fibrils Open
A critical discovery of the past decade is that tau protein fibrils adopt disease-specific hallmark structures in each tauopathy. The faithful generation of synthetic fibrils adopting hallmark structures that can serve as targets for devel…
View article: Water-directed pinning is key to tau prion formation
Water-directed pinning is key to tau prion formation Open
Tau forms fibrillar aggregates that are pathological hallmarks of a family of neurodegenerative diseases known as tauopathies. The synthetic replication of disease-specific fibril structures is a critical gap for developing diagnostic and …
View article: Phosphoryl group wires stabilize pathological tau fibrils as revealed by multiple quantum spin counting NMR
Phosphoryl group wires stabilize pathological tau fibrils as revealed by multiple quantum spin counting NMR Open
Hyperphosphorylation of the protein tau is one of the biomarkers of neurodegenerative diseases in the category of tauopathies. However, the molecular level, mechanistic, role of this common post- translational modification (PTM) in enhanci…
View article: Precision proteoform design for 4R tau isoform selective templated aggregation
Precision proteoform design for 4R tau isoform selective templated aggregation Open
Prion-like spread of disease-specific tau conformers is a hallmark of all tauopathies. A 19-residue probe peptide containing a P301L mutation and spanning the R2/R3 splice junction of tau folds and stacks into seeding-competent fibrils and…
View article: Tau P301L mutation promotes core 4R tauopathy fibril fold through near-surface water structuring and conformational rearrangement
Tau P301L mutation promotes core 4R tauopathy fibril fold through near-surface water structuring and conformational rearrangement Open
Tau forms toxic fibrillar aggregates in a family of neurodegenerative diseases known as tauopathies. The faithful replication of tauopathy-specific fibril structures is a critical gap for developing diagnostic and therapeutic tools. This s…
View article: Precision Proteoform Design for 4R Tau Isoform Selective Templated Aggregation
Precision Proteoform Design for 4R Tau Isoform Selective Templated Aggregation Open
Prion-like spread of disease-specific tau conformers is a hallmark of all tauopathies. A 19-residue probe peptide containing a P301L mutation and spanning the R2/R3 splice junction of tau, folds and stacks into seeding-competent fibrils an…
View article: Passaging Human Tauopathy Patient Samples in Cells Generates Heterogeneous Fibrils with a Subpopulation Adopting Disease Folds
Passaging Human Tauopathy Patient Samples in Cells Generates Heterogeneous Fibrils with a Subpopulation Adopting Disease Folds Open
The recent discovery by cryo-electron microscopy (cryo-EM) that the neuropathological hallmarks of different tauopathies, including Alzheimer’s disease, corticobasal degeneration (CBD), and progressive supranuclear palsy (PSP), are caused …
View article: Homo-oligomerization of the human adenosine A2A receptor is driven by the intrinsically disordered C-terminus
Homo-oligomerization of the human adenosine A2A receptor is driven by the intrinsically disordered C-terminus Open
G protein-coupled receptors (GPCRs) have long been shown to exist as oligomers with functional properties distinct from those of the monomeric counterparts, but the driving factors of oligomerization remain relatively unexplored. Herein, w…
View article: Author response: Homo-oligomerization of the human adenosine A2A receptor is driven by the intrinsically disordered C-terminus
Author response: Homo-oligomerization of the human adenosine A2A receptor is driven by the intrinsically disordered C-terminus Open
Article Figures and data Abstract Introduction Results Discussion Materials and methods Data availability References Decision letter Author response Article and author information Metrics Abstract G protein-coupled receptors (GPCRs) have l…
View article: Oligomerization of the Human Adenosine A <sub>2A</sub> Receptor is Driven by the Intrinsically Disordered C-terminus
Oligomerization of the Human Adenosine A <sub>2A</sub> Receptor is Driven by the Intrinsically Disordered C-terminus Open
G protein-coupled receptors (GPCRs) have long been shown to exist as oligomers with functional properties distinct from those of the monomeric counterparts, but the driving factors of GPCR oligomerization remain relatively unexplored. In t…
View article: The proline-rich domain promotes Tau liquid–liquid phase separation in cells
The proline-rich domain promotes Tau liquid–liquid phase separation in cells Open
Tau protein in vitro can undergo liquid–liquid phase separation (LLPS); however, observations of this phase transition in living cells are limited. To investigate protein state transitions in living cells, we attached Cry2 to Tau and studi…
View article: The Proline-rich Domain Promotes Tau Liquid Liquid Phase Separation in Cells
The Proline-rich Domain Promotes Tau Liquid Liquid Phase Separation in Cells Open
Tau protein in vitro can undergo liquid liquid phase separation (LLPS); however, observations of this phase transition in living cells are limited. To investigate protein state transitions in living cells we found that Cry2 can optogentica…
View article: Cofactors are essential constituents of stable and seeding-active tau fibrils
Cofactors are essential constituents of stable and seeding-active tau fibrils Open
Significance The tau protein is involved in Alzheimer’s and other neurodegenerative diseases, where the location, morphology, and quantity of amyloid fibrils composed of tau correlate with the disease type and stage. While tau fibrillary a…
View article: Correction: Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments
Correction: Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments Open
Correction for ‘Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments’ by Yann Fichou et al., Chem. Commun., 2018, 54, 4573–4576.