Results 81 to 90 of about 659,948 (302)

QBP1 Peptide as a Potential Anti‐Amyloidogenic Therapy for Type 2 Diabetes: An In Vitro Study

Advanced Science, EarlyView.
The anti‐amyloidogenic peptide QBP1 effectively halts human islet amyloid polypeptide (hIAPP) aggregation, preventing the formation of toxic β‐structured intermediates. Through a combination of biophysical assays, molecular dynamics, and cell‐based studies, QBP1 is shown to preserve β‐cell viability and metabolic homeostasis, positioning it as a ...
María M. Tejero‐Ojeda, Ada Bernaus Vives, Michał Wojciechowski, Dinh Quoc Huy Pham, Mateusz Chwastyk, Mario Vallejo, Anna Novials, Douglas V. Laurents, Mariano Carrión‐Vázquez   +8 more
wiley   +1 more source

Alpha-, beta-, and gamma-synuclein: developmental localisation and response to cellular insult in neurons and oligodendrocytes

, 2009
Alpha-synuclein is a highly conserved, ubiquitously expressed protein in the vertebrate brain. It was discovered in 1988 and was purported to play a role in song learning, implicating a role in synaptic plasticity.
Quilty, M (15507635)
core   +2 more sources

Carboranyl‐Curcuminoids for the Neutron Capture‐Based Treatment of Amyloid Aggregates in Alzheimer's Disease

Advanced Science, EarlyView.
The 10B‐enriched monocarbonyl analog of curcumin (BMAC) 10B‐9 enables site‐specific Boron Neutron Capture Therapy (BNCT) on amyloid‐β (Aβ) fibrils. Neutron irradiation induces histidine oxidation and fibril destabilization, as revealed by 1H‐NMR and FESEM analyses.
Sebastiano Micocci, Stefano Parisotto, Diego Alberti, Alberto Lanfranco, Valeria Bitonto, Polyssena Renzi, Martina Salmi, Andrea Magnani, Federica Dal Bello, Katiuscia Pagano, Laura Ragona, Nicoletta Protti, Annamaria Deagostino, Simonetta Geninatti Crich   +13 more
wiley   +1 more source

The Interaction of Alpha-synuclein with Membranes and its Implication in Parkinson's Disease: A Literature Review

Natural Product Communications, 2015
Alpha-synuclein belongs to the class of intrinsically disordered proteins lacking a well-folded structure under physiological conditions. The conversion of alpha-synuclein from a soluble monomer to an insoluble fibril may underlie the neurodegeneration ...
Azucena Gonzalez-Horta
doaj   +1 more source

Striatal dopamine transmission is subtly modified in human A53Tα-synuclein overexpressing mice

, 2012
Mutations in, or elevated dosage of, SNCA, the gene for α-synuclein (α-syn), cause familial Parkinson's disease (PD). Mouse lines overexpressing the mutant human A53Tα-syn may represent a model of early PD.
Auburger, G, Gispert, Suzana, Stephanie J Cragg, Suzana Gispert, Auburger Georg, Cragg, Stephanie J., Cragg Stephanie J., Georg Auburger, Gispert, S, Platt Nicola J., Auburger, Georg, Platt, NJ, Cragg, Stephanie, Nicola J Platt, Gispert Suzana, Platt, Nicola J.   +15 more
core   +1 more source

A Circuit of Mechanically Regulated Transcription Factors Balances Regenerative and Fibrotic Memory of Mesenchymal Stromal Cells

Advanced Science, EarlyView.
Producing MSCs on rigid culture substrates induces a scar‐making phenotype, jeapordizing therapeutic success. ‘Tissue‐soft’ surfaces prevent MSC fibrogenesis and preserve regenerative traits. An epigenetic network, driven by HOXA11 and SALL1, maintains ‘soft memory’ by keeping chromatin open in relaxed MSCs, promoting anti‐fibrotic programs.
Fereshteh Sadat Younesi, Andrew E. Miller, Li Diao, Xinying Guo, Natalie Andonian, Elham Karimizadeh, Thomas H. Barker, Boris Hinz   +7 more
wiley   +1 more source

Orthogonal Ionic Liquid‐Based Extraction Strategy Enables Amyloid‐Specific Profiling of Aggregate Proteome

Advanced Science, EarlyView.
An orthogonal ionic‐liquid extraction (Orth‐iEA) enables selective isolation of amyloid fibrils. TMGBF4 disrupts hydrogen‐bonded β‐sheet networks to solubilize amyloid aggregates, whereas C12ImCl interacts with hydrophobic regions of non‐amyloid proteins.
Shiying Zheng, Ye Liu, Bowen Zhong, Huiying Chu, Zhou Gong, Baofeng Zhao, Mengchun Cheng, Zhen Liang, Yukui Zhang, Qun Zhao, Lihua Zhang   +10 more
wiley   +1 more source

Cutaneous Alpha-Synuclein From Paraffin Embedded Autopsy Specimens in Parkinson’s Disease

Journal of Parkinson’s Disease, 2017
Background: Parkinson disease (PD) is neurodegenerative disorder characterized by tremor, rigidity and bradykinesia and pathologically by the deposition of alpha-synuclein within different tissues. We, and others, have reported the detection of cutaneous
Christopher H. Gibbons, Ningshan Wang, Roy Freeman   +2 more
doaj   +1 more source

Fine‐Tuned Regulation of mRNA Translation and Transport by STAU2 Condensate Facilitates Neuronal Development and Plasticity

Advanced Science, EarlyView.
STAU2 undergoes phase separation to form dynamic condensates that package target mRNAs and deliver them to the distal ends of growing neuronal dendrites. STAU2 condensates stabilize embedded mRNAs and repress their translation. Synaptic activity bidirectionally remodels STAU2 condensates, coordinating local translation of STAU2‐associated mRNAs ...
Shijing Huang, Yuanyuan Chu, Ruiqian Zhao, Siyu Li, Yu Feng, Hongdan Zheng, Yunli Xie, Tong Wang, Wenyu Wen   +8 more
wiley   +1 more source

Phospho-S129 Alpha-Synuclein Is Present in Human Plasma but Not in Cerebrospinal Fluid as Determined by an Ultrasensitive Immunoassay

Frontiers in Neuroscience, 2019
Accumulation and aggregation of misfolded alpha-synuclein is believed to be a cause of Parkinson’s disease (PD). Phosphorylation of alpha-synuclein at S129 is known to be associated with the pathological misfolding process, but efforts to investigate the
Cristina Cariulo, Paola Martufi, Margherita Verani, Lucia Azzollini, Giordana Bruni, Andreas Weiss, Sean M. Deguire, Hilal A. Lashuel, Eugenia Scaricamazza, Giulia Maria Sancesario, Tommaso Schirinzi, Nicola Biagio Mercuri, Nicola Biagio Mercuri, Giuseppe Sancesario, Andrea Caricasole, Lara Petricca   +15 more
doaj   +1 more source