Romany N. N. Abskharon

Structural evidence that RNA contributes to polymorphism of tau amyloid fibrils

Romany N. N. Abskharon, Yi Xiao Jiang, Michael R. Sawaya, Peng Ge et autres

. Previously, we determined a cryogenic-electron microscopy (cryo-EM) structure of fibrils of full-length tau bound to unfractionated mammalian RNA, revealing a small tau C-terminal core. Here, we present the cryo-EM structure of fibrils of full-length recombinant tau bound to unfractionated mammalian RNA …

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CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis

Avi J. Samelson, Nabeela Ariqat, Justin McKetney, Gita Rohanitazangi et autres

Aggregation of the protein tau defines tauopathies, the most common age-related neurodegenerative diseases, which include Alzheimer's disease and frontotemporal dementia. Specific neuronal subtypes are selectively vulnerable to tau aggregation, dysfunction, and death. However, molecular mechanisms underlying cell-type-selective vulnerability are unknown. To systematically …

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In Vitro and In Vivo Evaluation of Small-Molecule Disassemblers of Pathological Tau Fibrils

Hope Pan, Xinyi Cheng, Jeffrey Zhang, Ke Hou et autres

Aggregation of the microtubule-binding protein tau is the histopathological hallmark of Alzheimer's disease (AD) and other neurodegenerative diseases, which are collectively known as tauopathies. Tau aggregation in AD patients is correlated with neuron loss, brain atrophy, and cognitive decline, and pro-aggregation tau …

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B-010 Evaluation of Analytical Performance of Amyloid Beta 40, 42, pTau-181, pTau-217, NfL, and APOE4 on the full-automated DZ-Lite i2000 Analyzer for Alzheimer’s Disease Diagnosis

Romany N. N. Abskharon, Ahmad Houneini, Abhijit Datta, Chong Yuan

Abstract Background Alzheimer*s disease (AD), a leading cause of dementia, requires reliable and accessible diagnostic tools for early detection and monitoring. Current methods, such as cerebrospinal fluid (CSF) analysis and positron emission tomography (PET), are accurate but often impractical due to high …

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How short peptides disassemble tau fibrils in Alzheimer’s disease

Ke Hou, P. Ge, Michael R. Sawaya, Liisa Lutter et autres

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Liganded magnetic nanoparticles for magnetic resonance imaging of α-synuclein

Hope Pan, Melinda Balbirnie, Ke Hou, Naomi S. Sta Maria et autres

Aggregation of the protein α-synuclein (α-syn) is the histopathological hallmark of neurodegenerative diseases such as Parkinson's disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA), which are collectively known as synucleinopathies. Currently, patients with synucleinopathies are diagnosed by physical …

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Investigating the In Vivo Effects of Anti-Prion Protein Nanobodies on Prion Disease with AAV Vector

Jingjing Zhang, Mengfei Wang, Dan Wang, Xiangyi Zhang et autres

Prion diseases are fatal neurodegenerative disorders affecting humans and animals, and the central pathogenic event is the conversion of normal prion protein (PrPC) into the pathogenic PrPSc isoform. Previous studies have identified nanobodies that specifically recognize PrPC and inhibit the PrPC to …

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D-peptide-magnetic nanoparticles fragment tau fibrils and rescue behavioral deficits in a mouse model of Alzheimer’s disease

Ke Hou, Hope Pan, Hedieh Shahpasand‐Kroner, Carolyn J. Hu et autres

Amyloid fibrils of tau are increasingly accepted as a cause of neuronal death and brain atrophy in Alzheimer's disease (AD). Diminishing tau aggregation is a promising strategy in the search for efficacious AD therapeutics. Previously, our laboratory designed a six-residue, nonnatural amino …

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CryoEM of Tropomyosin-receptor kinase fused gene protein (TRK-fused gene protein; TFG) Low Complexity Domain (residues 237-327) P285L mutant, amyloid fibers

Gregory M. Rosenberg, Romany N. N. Abskharon, David R. Boyer, P. Ge et autres

EMPIAR, the Electron Microscopy Public Image Archive centered at EMBL-EBI, is a public resource for raw electron microscopy images related to EMDB, contains micrographs, particle sets and tilt-series.

CryoEM of Tropomyosin-receptor kinase fused gene protein (TRK-fused gene protein; TFG) Low Complexity Domain (residues 237-327) G269V mutant, amyloid fibers

Gregory M. Rosenberg, Romany N. N. Abskharon, Boyer DR, P. Ge et autres

EMPIAR, the Electron Microscopy Public Image Archive centered at EMBL-EBI, is a public resource for raw electron microscopy images related to EMDB, contains micrographs, particle sets and tilt-series.

Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation

Jiahui Lu, P. Ge, Michael R. Sawaya, Michael P. Hughes et autres

Heterogeneous nuclear ribonucleoprotein A2 (hnRNPA2) is a human ribonucleoprotein that transports RNA to designated locations for translation via its ability to phase separate. Its mutated form, D290V, is implicated in multisystem proteinopathy known to afflict two families, mainly with myopathy and Paget's …

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Fibril structures of TFG protein mutants validate the identification of TFG as a disease-related amyloid protein by the IMPAcT method

Gregory M. Rosenberg, Romany N. N. Abskharon, David R. Boyer, P. Ge et autres

We previously presented a bioinformatic method for identifying diseases that arise from a mutation in a protein's low-complexity domain that drives the protein into pathogenic amyloid fibrils. One protein so identified was the tropomyosin-receptor kinase-fused gene protein (TRK-fused gene protein or TFG). …

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