Julia Gerson

Julia Gerson
University of Michigan | U-M · Department of Neurology

PhD

About

55
Publications
10,597
Reads
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1,673
Citations
Citations since 2017
25 Research Items
1372 Citations
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2017201820192020202120222023050100150200250
2017201820192020202120222023050100150200250
2017201820192020202120222023050100150200250
Introduction
Additional affiliations
August 2012 - present
University of Texas Medical Branch at Galveston
Position
  • PhD Student

Publications

Publications (55)
Article
Full-text available
The key protein implicated in Parkinson’s disease and other synucleinopathies is α-synuclein, and a post-translationally modified form of the protein, phosphorylated at serine 129 (pS129), is a principal component in Lewy bodies, a pathological hallmark of PD. While altered proteostasis has been implicated in the etiology of Parkinson’s disease, we...
Article
Tau protein accumulation drives toxicity in several neurodegenerative disorders. To better understand the pathways regulating tau homeostasis in disease, we investigated the role of ubiquilins (UBQLNs)-a class of proteins linked to ubiquitin-mediated protein quality control (PQC) and various neurodegenerative diseases-in regulating tau. Cell-based...
Article
Background: The protein quality control protein ubiquilin-2 (UBQLN2) is implicated in synucleinopathies due to its accumulation in Lewy body diseases. However, little is known about how it may interact with and clear α-synuclein (α-syn). This study aimed to define the role of UBQLN2 in handling α-syn. Method: To evaluate whether UBQLN2 regulates...
Article
Full-text available
The aggregation of amyloidogenic polypeptides is strongly linked to several neurodegenerative disorders, including Alzheimer’s and Parkinson’s diseases. Conformational antibodies that selectively recognize protein aggregates are leading therapeutic agents for selectively neutralizing toxic aggregates, diagnostic and imaging agents for detecting dis...
Article
Full-text available
The brain-expressed ubiquilins, UBQLNs 1, 2 and 4, are highly homologous proteins that participate in multiple aspects of protein homeostasis and are implicated in neurodegenerative diseases. Studies have established that UBQLN2 forms liquid-like condensates and accumulates in pathogenic aggregates, much like other proteins linked to neurodegenerat...
Article
Ubiquilin‐2 (UBQLN2) is a protein quality control protein involved primarily in shuttling ubiquitinated substrates to the proteasome for degradation and by modulating autophagy. UBQLN2 has been implicated in neurodegenerative disease due to its accumulation in neuropathological deposits and its potential role in regulating protein dyshomeostasis co...
Preprint
Full-text available
The brain-expressed ubiquilins, UBQLNs 1, 2 and 4, are highly homologous proteins that participate in multiple aspects of protein homeostasis and are implicated in neurodegenerative diseases. Studies have established that UBQLN2 forms liquid-like condensates and accumulates in pathogenic aggregates, much like other proteins linked to neurodegenerat...
Article
Divergent protein context helps explain why polyglutamine expansion diseases differ clinically and pathologically. This heterogeneity may also extend to how polyglutamine disease proteins are handled by cellular pathways of proteostasis. Studies suggest, for example, that the ubiquitin-proteasome shuttle protein Ubiquilin-2 (UBQLN2) selectively int...
Article
Full-text available
The ubiquitin-binding proteasomal shuttle protein UBQLN2 is implicated in common neurodegenerative disorders due to its accumulation in disease-specific aggregates and, when mutated, directly causes familial frontotemporal dementia/amyotrophic lateral sclerosis (FTD/ALS). Like other proteins linked to FTD/ALS, UBQLN2 undergoes phase separation to f...
Article
https://deepblue.lib.umich.edu/bitstream/2027.42/152960/1/alzjjalz2019063816.pdf
Article
Full-text available
Antibodies that recognize amyloidogenic aggregates with high conformational and sequence specificity are important for detecting and potentially treating a wide range of neurodegenerative disorders, including Alzheimer's and Parkinson’s diseases. However, these types of antibodies are challenging to generate because of the large size, hydrophobicit...
Article
Full-text available
Background: We have evaluated the efficacy of targeting the toxic, oligomeric form of tau protein by passive immunotherapy in a mouse model of synucleinopathy. Parkinson's disease and Lewy body dementia are two of the most common neurodegenerative disorders and are primarily characterized by the accumulation of α-synuclein in Lewy bodies. However,...
Article
Full-text available
Significance UBQLN2, a ubiquitin-linked quality-control protein, accumulates in common neurodegenerative diseases and, when mutated, directly causes neurodegeneration. Employing a range of model systems, we show that UBQLN2 is intrinsically prone to self-assemble, leading to the formation of liquid-like droplets and amyloid aggregates. A disease-ca...
Article
Full-text available
Purpose Retinal ganglion cell (RGC) death following axonal injury occurring in traumatic optic neuropathy (TON) causes irreversible vision loss. GRP78 is a molecular chaperone that enhances protein folding and controls activation of endoplasmic reticulum (ER) stress pathways. This study determined whether adeno-associated virus (AAV)-mediated gene...
Article
https://deepblue.lib.umich.edu/bitstream/2027.42/153267/1/alzjjalz2018061510.pdf
Article
https://deepblue.lib.umich.edu/bitstream/2027.42/152872/1/alzjjalz2018062650.pdf
Article
Full-text available
Background The coexistence of α-synuclein and tau aggregates in several neurodegenerative disorders, including Parkinson’s disease (PD) and Alzheimer’s disease (AD), raises the possibility that a seeding mechanism is involved in disease progression. Methods To further investigate the role of α-synuclein in the tau aggregation pathway, we performed...
Chapter
The accumulation of pathological protein deposits, amyloids, in neurodegenerative disease represents a formidable challenge for drug development. With no effective treatment in sight, and recent findings suggesting that protein aggregates are diverse, dynamic, and capable of spreading, it is crucial that researchers find safe and successful therape...
Chapter
Tau oligomers have been shown to be the main toxic tau species in a number of neurodegenerative disorders. In order to study tau oligomers both in vitro and in vivo, we have established methods for the reliable preparation, isolation, and detection of tau oligomers. Methods for the seeding of tau oligomers, isolation of tau oligomers from tissue, a...
Article
Full-text available
The importance of vascular contributions to cognitive impairment and dementia (VCID) associated with Alzheimer’s disease (AD) and related neurodegenerative diseases is increasingly recognized, however, the underlying mechanisms remain obscure. There is growing evidence that in addition to Aβ deposition, accumulation of hyperphosphorylated oligomeri...
Article
Full-text available
It is well-established that inflammation plays an important role in Alzheimer's disease (AD) and frontotemporal lobar dementia (FTLD). Inflammation and synapse loss occur in disease prior to the formation of larger aggregates, but the contribution of tau to inflammation has not yet been thoroughly investigated. Tau pathologically aggregates to form...
Article
The accumulation of protein aggregates in the brain is a defining feature of a number of neurodegenerative diseases. Though diseases vary in the composition of aggregated proteins (amyloid-β and tau are primarily implicated in Alzheimer's disease, α-synuclein is the primary protein aggregate in Parkinson's disease, etc.), similarities in the format...
Article
Full-text available
The culmination of many years of increasing research into the toxicity of tau aggregation in neurodegenerative disease has led to the consensus that soluble, oligomeric forms of tau are likely the most toxic entities in disease. While tauopathies overlap in the presence of tau pathology, each disease has a unique combination of symptoms and patholo...
Article
Full-text available
Neurodegenerative diseases characterized by the accumulation of tau aggregates are increasing in prevalence to epidemic-like levels and there is currently no effective treatment. For many years, the focus of tau-based research was on the fibrillar, neurofibrillary tangles. However, the compilation of evidence obtained from numerous laboratories in...
Article
Full-text available
Tau aggregation is a pathological feature of numerous neurodegenerative disorders and has also been shown to occur under certain conditions of traumatic brain injury (TBI). Currently, no effective treatments exist for the long-term effects of TBI. In some cases, TBI not only induces cognitive changes immediately following injury, but also leads to...
Chapter
Recently tau protein has emerged as a viable therapeutic target for Alzheimer’s disease (AD) and multiple other neurodegenerative disorders known as tauopathies. Neurofibrillary tangles have long been known to be hallmarks of these disorders and to spread stereotypically through the brain. Further study into the toxicity of the protein has led many...
Article
Full-text available
Alzheimer’s disease (AD) is a progressive disorder in which the most noticeable symptoms are cognitive impairment and memory loss. However, the precise mechanism by which those symptoms develop remains unknown. Of note, neuronal loss occurs at sites where synaptic dysfunction is observed earlier, suggesting that altered synaptic connections precede...
Article
Amyloid-beta (Aβ) oligomers have emerged as the most toxic species in Alzheimer's disease (AD) and other amyloid pathologies. Also, Aβ-42 peptide is more aggregation-prone compared to other Aβ isoforms. Thus, we synthesized a small peptide of repeated sequence containing the last three amino acids, Val-40, Ile-41, and Ala-42 of Aβ-42 that was subse...
Article
Full-text available
Background: The majority of neurodegenerative tauopathies are associated with the pathological accumulation of additional amyloid proteins, notably amyloid-β in Alzheimer's disease (AD). Studies have shown that intermediate aggregates known as oligomers are the most toxic species in disease. The common toxic factor in these diseases, the tau oligom...
Article
Full-text available
Various neurodegenerative diseases are characterized by the accumulation of amyloidogenic proteins such as tau, α-synuclein, and amyloid-β. Prior to the formation of these stable aggregates, intermediate species of the respective proteins-oligomers-appear. Recently acquired data have shown that oligomers may be the most toxic and pathologically sig...
Article
Ethinyl Estradiol (EE), a synthetic, orally bio-available estrogen, is the most commonly prescribed form of estrogen in oral contraceptives, and is found in at least 30 different contraceptive formulations currently prescribed to women as well as hormone therapies prescribed to menopausal women. Thus, EE is prescribed clinically to women at ages ra...
Article
Full-text available
Background: Aberrant accumulation of α-synuclein constitutes inclusion bodies that are considered a characteristic feature of a group of neurological disorders described as synucleinopathies. Often, multiple disease-causing proteins overlap within a given disease pathology. An emerging body of research focuses on the oligomeric populations of vari...
Article
Full-text available
We constructed an 11-arm, walk-through, human radial-arm maze (HRAM) as a translational instrument to compare existing methodology in the areas of rodent and human learning and memory research. The HRAM, utilized here, serves as an intermediary test between the classic rat radial-arm maze (RAM) and standard human neuropsychological and cognitive te...
Article
Neurodegenerative disease is one of the greatest health concerns today and with no effective treatment in sight, it is crucial that researchers find a safe and successful therapeutic. While neurofibrillary tangles are considered the primary tauopathy hallmark, more evidence continues to come to light to suggest that soluble, intermediate tau aggreg...
Article
Full-text available
Background Progressive supranuclear palsy (PSP) is a neurodegenerative tauopathy which is primarily defined by the deposition of tau into globose-type neurofibrillary tangles (NFT). Tau in its native form has important functions for microtubule dynamics. Tau undergoes alternative splicing in exons 2, 3, and 10 which results in six different isoform...
Article
Full-text available
Pathological aggregation of the microtubule-associated protein tau and subsequent accumulation of neurofibrillary tangles (NFTs) or other tau-containing inclusions are defining histopathological features of many neurodegenerative diseases, which are collectively known as tauopathies. Due to conflicting results regarding a correlation between the pr...
Article
Full-text available
Recent findings suggest that tau oligomers, which form before neurofibrillary tangles (NFTs), are the true neurotoxic tau entities in neurodegenerative tauopathies, including Alzheimer's disease (AD). Studies in animal models of tauopathy suggest that tau oligomers play a key role in eliciting behavioral and cognitive impairments. Here, we used a n...
Article
Full-text available
Neurodegenerative disease is one of the greatest health crises in the world and as life expectancy rises, the number of people affected will continue to increase. The most common neurodegenerative disease, Alzheimer's disease, is a tauopathy, characterized by the presence of aggregated tau, namely in the form of neurofibrillary tangles. Historicall...
Article
Full-text available
Tau misfolding and aggregation leads to the formation of neurofibrillary tangles (NFTs), which have long been considered one of the main pathological hallmarks for numerous neurodegenerative diseases known as tauopathies, including Alzheimer's Disease (AD) and Parkinson's Disease (PD). However, recent studies completed both in vitro and in vivo sug...
Article
After natural menopause in women, androstenedione becomes the primary hormone secreted by the residual follicle-depleted ovaries. In two independent studies, in rodents that had undergone ovarian follicular depletion, we found that higher endogenous serum androstenedione levels correlated with increased working memory errors. This led to the hypoth...

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Project (1)
Project
What is the regulatory role of UBQLN2 on aggregate-prone proteins? Does UBQLN2 intrinsic aggregation lead to toxicity in neurodegenerative disease?