Search Results - "Montalbano, Mauro"

Glypican-3 (GPC-3) Structural Analysis and Cargo in Serum Small Extracellular Vesicles of Hepatocellular Carcinoma Patients by Mauro, Montalbano, Ugo, Perricone, Walton, Zachary, Ali, Shirafkan, Rastellini, Cristiana, Cicalese, Luca

“…Glypican-3 (GPC-3) is a heparin sulfate proteoglycan located extracellularly and anchored to the cell membrane of transformed hepatocytes. GPC-3 is not…”
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Mitochondrial DNA damage and subsequent activation of Z-DNA binding protein 1 links oxidative stress to inflammation in epithelial cells by Szczesny, Bartosz, Marcatti, Michela, Ahmad, Akbar, Montalbano, Mauro, Brunyánszki, Attila, Bibli, Sofia-Iris, Papapetropoulos, Andreas, Szabo, Csaba

“…This report identifies mitochondrial DNA (mtDNA) as a target and active mediator that links low-level oxidative stress to inflammatory response in pulmonary…”
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RNA-binding proteins Musashi and tau soluble aggregates initiate nuclear dysfunction by Montalbano, Mauro, McAllen, Salome, Puangmalai, Nicha, Sengupta, Urmi, Bhatt, Nemil, Johnson, Omar D., Kharas, Michael G., Kayed, Rakez

“…Oligomeric assemblies of tau and the RNA-binding proteins (RBPs) Musashi (MSI) are reported in Alzheimer’s disease (AD). However, the role of MSI and tau…”
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TDP-43 and Tau Oligomers in Alzheimer's Disease, Amyotrophic Lateral Sclerosis, and Frontotemporal Dementia by Montalbano, Mauro, McAllen, Salome, Cascio, Filippa Lo, Sengupta, Urmi, Garcia, Stephanie, Bhatt, Nemil, Ellsworth, Anna, Heidelman, Eric A., Johnson, Omar D., Doskocil, Samantha, Kayed, Rakez

“…Proteinaceous aggregates are major hallmarks of several neurodegenerative diseases. Aggregates of post-translationally modified transactive response (TAR)-DNA…”
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P53 aggregation, interactions with tau, and impaired DNA damage response in Alzheimer's disease by Farmer, Kathleen M, Ghag, Gaurav, Puangmalai, Nicha, Montalbano, Mauro, Bhatt, Nemil, Kayed, Rakez

“…The transcription factor, p53, is critical for many important cellular functions involved in genome integrity, including cell cycle control, DNA damage…”
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Tau Modulates mRNA Transcription, Alternative Polyadenylation Profiles of hnRNPs, Chromatin Remodeling and Spliceosome Complexes by Montalbano, Mauro, Jaworski, Elizabeth, Garcia, Stephanie, Ellsworth, Anna, McAllen, Salome, Routh, Andrew, Kayed, Rakez

“…Tau protein is a known contributor in several neurodegenerative diseases, including Alzheimer's disease (AD) and frontotemporal dementia (FTD). It is…”
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Hazardous air pollutants and primary liver cancer in Texas by Cicalese, Luca, Curcuru, Giuseppe, Montalbano, Mauro, Shirafkan, Ali, Georgiadis, Jeremias, Rastellini, Cristiana

“…The incidence of hepatocellular carcinoma (HCC), the most common primary liver cancer, is increasing in the US and tripled during the past two decades. The…”
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Formation of Toxic Oligomeric Assemblies of RNA-binding Protein: Musashi in Alzheimer's disease by Sengupta, Urmi, Montalbano, Mauro, McAllen, Salome, Minuesa, Gerard, Kharas, Michael, Kayed, Rakez

“…Alzheimer's disease (AD) is the most common neurodegenerative disorder associated with structural and functional alterations of brain cells causing progressive…”
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Modeling of Hepatocytes Proliferation Isolated from Proximal and Distal Zones from Human Hepatocellular Carcinoma Lesion by Montalbano, Mauro, Curcurù, Giuseppe, Shirafkan, Ali, Vento, Renza, Rastellini, Cristiana, Cicalese, Luca

“…Isolation of hepatocytes from cirrhotic human livers and subsequent primary culture are important new tools for laboratory research and cell-based therapeutics…”
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Biology and function of glypican-3 as a candidate for early cancerous transformation of hepatocytes in hepatocellular carcinoma (Review) by Montalbano, Mauro, Georgiadis, Jeremias, Masterson, Ashlyn L, McGuire, Joshua T, Prajapati, Janika, Shirafkan, Ali, Rastellini, Cristiana, Cicalese, Luca

“…Glypican-3 (GPC-3), a transmembrane heparan sulfate proteoglycan (HSPG), has recently been investigated as a player in tissue-dependent cellular signaling,…”
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Pathological tau signatures and nuclear alterations in neurons, astrocytes and microglia in Alzheimer's disease, progressive supranuclear palsy, and dementia with Lewy bodies by Montalbano, Mauro, Majmundar, Lajja, Sengupta, Urmi, Fung, Leiana, Kayed, Rakez

“…Accumulation of pathological tau aggregates is a prominent feature in tauopathies that leads during the course of the diseases to neuronal dysfunction before…”
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Tau oligomer induced HMGB1 release contributes to cellular senescence and neuropathology linked to Alzheimer’s disease and frontotemporal dementia by Gaikwad, Sagar, Puangmalai, Nicha, Bittar, Alice, Montalbano, Mauro, Garcia, Stephanie, McAllen, Salome, Bhatt, Nemil, Sonawane, Minal, Sengupta, Urmi, Kayed, Rakez

“…Aging, pathological tau oligomers (TauO), and chronic inflammation in the brain play a central role in tauopathies, including Alzheimer’s disease (AD) and…”
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RNA‐Binding Proteins Musashi and Tau Aggresome in Alzheimer’s disease by Montalbano, Mauro, Aday, Abbigael, Jerez, Cynthia, Fung, Leiana, Kayed, Rakez

“…Background Tauopathies, such as Alzheimer’s disease (AD), are characterized by the accumulation of toxic tau oligomers in the brain and accumulation of…”
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Lysine 63-linked ubiquitination of tau oligomers contributes to the pathogenesis of Alzheimer’s disease by Puangmalai, Nicha, Sengupta, Urmi, Bhatt, Nemil, Gaikwad, Sagar, Montalbano, Mauro, Bhuyan, Arijit, Garcia, Stephanie, McAllen, Salome, Sonawane, Minal, Jerez, Cynthia, Zhao, Yingxin, Kayed, Rakez

“…Ubiquitin-modified tau aggregates are abundantly found in human brains diagnosed with Alzheimer’s disease (AD) and other tauopathies. Soluble tau oligomers…”
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Tau oligomers mediate aggregation of RNA‐binding proteins Musashi1 and Musashi2 inducing Lamin alteration by Montalbano, Mauro, McAllen, Salome, Sengupta, Urmi, Puangmalai, Nicha, Bhatt, Nemil, Ellsworth, Anna, Kayed, Rakez

“…The exact mechanisms leading to neurodegeneration in Alzheimer's disease (AD) and other tauopathies are not yet entirely understood. However, it is known that…”
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Modulating disease-relevant tau oligomeric strains by small molecules by Lo Cascio, Filippa, Garcia, Stephanie, Montalbano, Mauro, Puangmalai, Nicha, McAllen, Salome, Pace, Andrea, Palumbo Piccionello, Antonio, Kayed, Rakez

“…The pathological aggregation of tau plays an important role in Alzheimer's disease and many other related neurodegenerative diseases, collectively referred to…”
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Tau modulates mRNA transcription, alternative polyadenylation (APA) profiles of hnRNPs, chromatin remodeling and spliceosome complexes by Montalbano, Mauro, Jaworski, Elizabeth, Garcia, Stephanie, Ellsworth, Anna, McAllen, Salome, Routh, Andrew, Kayed, Rakez

“…Tau protein is a known contributor in several neurodegenerative diseases, including Alzheimer ’s disease (AD) and frontotemporal dementia (FTD). It is…”
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Aβ/tau oligomer interplay at human synapses supports shifting therapeutic targets for Alzheimer’s disease by Marcatti, Michela, Fracassi, Anna, Montalbano, Mauro, Natarajan, Chandramouli, Krishnan, Balaji, Kayed, Rakez, Taglialatela, Giulio

“…Background Alzheimer’s disease (AD) is characterized by progressive cognitive decline due to accumulating synaptic insults by toxic oligomers of amyloid beta…”
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Nasal tau immunotherapy clears intracellular tau pathology and improves cognitive functions in aged tauopathy mice by Gaikwad, Sagar, Puangmalai, Nicha, Sonawane, Minal, Montalbano, Mauro, Price, Rachel, Iyer, Malini S, Ray, Anamika, Moreno, Sandra, Kayed, Rakez

“…Pathological tau aggregates cause cognitive decline in neurodegenerative tauopathies, including Alzheimer's disease (AD). These aggregates are prevalent within…”
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Internalization mechanisms of brain-derived tau oligomers from patients with Alzheimer’s disease, progressive supranuclear palsy and dementia with Lewy bodies by Puangmalai, Nicha, Bhatt, Nemil, Montalbano, Mauro, Sengupta, Urmi, Gaikwad, Sagar, Ventura, Frank, McAllen, Salome, Ellsworth, Anna, Garcia, Stephanie, Kayed, Rakez

“…Tau aggregates propagate in brain cells and transmit to neighboring cells as well as anatomically connected brain regions by prion-like mechanisms. Soluble tau…”
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