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Zsofia Lengyel-Zhand

Researcher at University of Pennsylvania

Publications -  9
Citations -  118

Zsofia Lengyel-Zhand is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Internalization & Receptor. The author has an hindex of 4, co-authored 8 publications receiving 37 citations.

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Journal ArticleDOI

The Sigma-2 Receptor/TMEM97, PGRMC1, and LDL Receptor Complex Are Responsible for the Cellular Uptake of Aβ42 and Its Protein Aggregates.

TL;DR: The intact Sigma-2 receptor complex may potentially be a novel pharmacological target to decrease neuronal Aβ42 internalization and accumulation, which may represent a new strategy for inhibiting the rate of neurotoxicity, neurodegeneration, and progression of AD.
Journal ArticleDOI

Identification of a nanomolar affinity α-synuclein fibril imaging probe by ultra-high throughput in silico screening

TL;DR: Ultra-high throughput in silico screening identified molecules that bind to α-synuclein fibrils, which were analyzed by photo-crosslinking, structure-activity studies, and radioligand binding to validate this approach for finding imaging probes.
Posted ContentDOI

The Sigma-2 Receptor/TMEM97, PGRMC1, and LDL Receptor complex are responsible for the cellular uptake of Aβ42 and its protein aggregates

TL;DR: The intact Sigma-2 receptor complex may potentially be a novel pharmacological target to decrease neuronal Aβ42 internalization and accumulation, which may represent a new strategy for inhibiting the rate of neurotoxicity, neurodegeneration, and progression of AD.
Journal ArticleDOI

Synthesis and characterization of high affinity fluorogenic α-synuclein probes

TL;DR: This work explores benzofuranone as a potential scaffold for the design of fluorescent α-synuclein probes that have high affinity for α- synuclein, show fluorescent turn-on upon binding to fibrils, and display different binding to Lewy bodies, Lewy neurites and glial cytoplasmic inclusion pathologies in post-mortem brain tissue.
Journal ArticleDOI

Poly (ADP-ribose) Interacts With Phosphorylated α-Synuclein in Post Mortem PD Samples

TL;DR: In this article, the PAR-pαSyn interactions were investigated using immunofluorescence-based assays to explore if PAR-1 enzymatic product (PAR) promotes the aberrant cytoplasmic accumulation of pαSyn.