Article
Biochemistry & Molecular Biology
Lei Gu, Zhefeng Guo
Summary: The formation of A beta oligomers and fibrils is crucial in Alzheimer's disease pathogenesis. A beta 42 and A beta 40 interact with each other influencing their aggregation, and A beta 40 has been shown to reduce plaque pathology in mouse models. The study suggests that A beta 42 and A beta 40 can form mixed oligomers with direct molecular interactions.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2021)
Review
Biochemistry & Molecular Biology
Ajit Kumar Bishoyi, Pratiksha H. Roham, Kavitha Rachineni, Shreyada Save, M. Asrafuddoza Hazari, Shilpy Sharma, Ashutosh Kumar
Summary: The overexpression of hIAPP in T2DM is associated with misfolding of the peptide, formation of amyloid deposits, and death and dysfunction of pancreatic beta-islets. Studies have shown that during aggregation, hIAPP undergoes conformational changes from helix to beta-sheet and finally to left-handed helical aggregates, with intermediates causing cellular toxicity.
BIOLOGICAL CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Allison Yoon, James Zhen, Zhefeng Guo
Summary: β amyloid 42 plays a central role in the pathogenesis of Alzheimer's disease, forming toxic oligomers in addition to insoluble fibrils. Our study on the structural dynamics of β amyloid 42 globulomers revealed residues 31-34 as the most stable segment, suggesting a lack of well-packed structural core in the globulomers.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2021)
Review
Biochemistry & Molecular Biology
Martin Muschol, Wolfgang Hoyer
Summary: Amyloid Diseases involve the growth and deposition of disease specific proteins into amyloid fibrils and plaques. The role of fibrils or oligomers in amyloid diseases is still debated, but in neurodegenerative disease, amyloid oligomers are believed to be important contributors to disease symptoms. Besides on-pathway oligomer formation, evidence suggests the presence of off-pathway oligomer formation that competes with fibril growth. Understanding the mechanisms and pathways of oligomer formation is crucial for studying their relevance to disease etiology.
FRONTIERS IN MOLECULAR BIOSCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Alexander G. Bobylev, Roman S. Fadeev, Liya G. Bobyleva, Margarita I. Kobyakova, Yuri M. Shlyapnikov, Daniil V. Popov, Ivan M. Vikhlyantsev
Summary: The study found that amyloid aggregates of smooth-muscle titin can impair cell adhesion and lead to cell death. The surface roughness may be a key factor contributing to the highly antiadhesive properties. The negative impact of amyloid aggregates on cell adhesion is likely intrinsic to other amyloid proteins with similar structure and properties.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Review
Biochemistry & Molecular Biology
Jaime Santos, Irantzu Pallares, Salvador Ventura
Summary: This review focuses on the structural and mechanistic characterization of alpha-S synuclein oligomers, which are considered key pathogenic factors in synucleinopathies. Recent advances in understanding these elusive species have paved the way for targeting therapeutics and diagnosis.
Article
Chemistry, Physical
Gufran Ahmed Siddiqui, Aabgeena Naeem
Summary: The study found that protein aggregation can lead to redox perturbation and cytotoxicity in cells, which is associated with various proteopathies including neurodegenerative disorders.
JOURNAL OF MOLECULAR LIQUIDS
(2021)
Article
Neurosciences
Kenya Moore, Urmi Sengupta, Nicha Puangmalai, Nemil Bhatt, Rakez Kayed
Summary: The accumulation of proteinaceous aggregates is a pathological hallmark of many neurodegenerative diseases. Parkinson's disease and dementia with Lewy bodies are characterized by the abnormal accumulation of alpha-synuclein (alpha-Syn). Alpha-Syn and tau, amyloidogenic proteins, can exist as polymorphic aggregates. Alpha-Syn oligomeric polymorphs show distinct properties and interact differently with tau. Monoclonal antibodies targeting the conformational heterogeneity of alpha-Syn oligomeric species have potential therapeutic applications.
MOLECULAR NEUROBIOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Chao Pang, Na Zhang, Mojtaba Falahati
Summary: The study demonstrated that SiO2 NPs can accelerate the formation of α-syn amyloid fibrils and increase their cytotoxicity. Experimental results indicate that SiO2 NPs induce the cytotoxic effects of α-syn amyloid fibrils through the mitochondrial-mediated intrinsic apoptosis pathway.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Neurosciences
Antonio J. Figueira, Joana Saavedra, Isabel Cardoso, Claudio M. Gomes
Summary: Extracellular aggregation of the amyloid-beta 1-42 peptide is a major characteristic of Alzheimer's disease (AD), and recent studies have shown that the intermediate oligomers of amyloid-beta are more cytotoxic than mature fibrils. In this study, the researchers investigated how different chaperone multimers of S100B, a signaling protein increased in AD, influence the formation of amyloid-beta oligomers. It was found that dimeric S100B-Ca2+ C drastically decreased the rate of oligomerization and levels of amyloid-beta oligomers, while tetrameric apo-S100B inhibited both oligomerization and fibril elongation. These findings highlight the potential neuroprotective role of different S100B multimers in AD.
FRONTIERS IN NEUROSCIENCE
(2023)
Article
Mathematics, Applied
P. Ghosh, J. Pateras, V Rangachari, A. Vaidya
Summary: The self-assembly of proteins into amyloid aggregates is important in neurodegenerative diseases, with a focus on understanding the formation and behavior of toxic oligomers. A theoretical framework is expanded to explore the network topological structures in amyloid formation kinetics. The use of thermodynamic free energy computations and mechanistic approaches help identify dominant pathways and intervention strategies to draw dynamics away from off-pathways.
APPLIED MATHEMATICS AND COMPUTATION
(2021)
Article
Biochemistry & Molecular Biology
Zeyaul Islam, Mohamed H. Ali, Anton Popelka, Raghvendra Mall, Ehsan Ullah, Janarthanan Ponraj, Prasanna R. Kolatkar
Summary: Amyloid fibrillation, related to various neurological disorders, was studied by examining lysozyme fibrillation using nano-infrared spectroscopy (nanoIR). The study showed that lysozyme transformed into mainly parallel beta-sheets in its fibrillar structure, and nanoIR can complement other biophysical studies in analyzing the aggregation process for potential therapeutic design against amyloid disorders.
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
(2021)
Review
Biochemistry & Molecular Biology
Jie Yang, Sarah Perrett, Si Wu
Summary: The misfolding and aggregation of polypeptide chains into amyloid fibrils are associated with neurodegenerative diseases. The oligomeric intermediates in early amyloid formation, rather than mature fibrils, are cytotoxic and potentially therapeutic targets. Single molecule fluorescence techniques have been developed to investigate amyloid oligomers and aggregation mechanisms.
Article
Biochemistry & Molecular Biology
Lei Gu, Zhefeng Guo
Summary: Formation of amyloid oligomers and fibrils, underlying neurodegenerative diseases like Alzheimer's, involves interactions with cellular membranes. The conversion of Aβ42 globulomers to fibrils in the presence of DOPC liposomes suggests a dynamic nature of interactions between Aβ oligomers and membranes. Lipid membranes can reduce membrane-disrupting activities caused by Aβ oligomers by converting them to fibrils.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2021)
Article
Cell Biology
Abigail K. Elias, Mark R. Wilson, John A. Carver, Ian F. Musgrave
Summary: Clusterin plays an important role in preventing the formation of SEVI amyloid fibrils, dissociating them, and mitigating their enhancement of HIV infection in semen.
Article
Geriatrics & Gerontology
Ilaria Luccarini, Cristina Grossi, Stefania Rigacci, Elisabetta Coppi, Anna Maria Pugliese, Daniela Pantano, Giancarlo la Marca, Teresa Ed Dami, Andrea Berti, Massimo Stefani, Fiorella Casamenti
NEUROBIOLOGY OF AGING
(2015)
Article
Biochemistry & Molecular Biology
Francesca Pellistri, Monica Bucciantini, Gaetano Invernizzi, Elena Gatta, Amanda Penco, Anna Maria Frana, Daniele Nosi, Annalisa Relini, Maria Elena Regonesi, Alessandra Gliozzi, Paolo Tortora, Mauro Robello, Massimo Stefani
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
(2013)
Review
Biochemistry & Molecular Biology
Massimo Stefani, Stefania Rigacci
Article
Biochemistry & Molecular Biology
Cristina Cecchi, Massimo Stefani
BIOPHYSICAL CHEMISTRY
(2013)
Review
Clinical Neurology
Stefania Rigacci, Massimo Stefani
EXPERT REVIEW OF NEUROTHERAPEUTICS
(2015)
Article
Cell Biology
Elisa Evangelisti, Cristina Cecchi, Roberta Cascella, Caterina Sgromo, Matteo Becatti, Christopher M. Dobson, Fabrizio Chiti, Massimo Stefani
JOURNAL OF CELL SCIENCE
(2012)
Article
Chemistry, Physical
Monica Bucciantini, Stefania Rigacci, Massimo Stefani
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2014)
Article
Clinical Neurology
Cristina Grossi, Teresa Ed Dami, Stefania Rigacci, Massimo Stefani, Ilaria Luccarini, Fiorella Casamenti
NEURODEGENERATIVE DISEASES
(2014)
Article
Neurosciences
Ilaria Luccarini, Teresa Ed Dami, Cristina Grossi, Stefania Rigacci, Massimo Stefani, Fiorella Casamenti
NEUROSCIENCE LETTERS
(2014)
Article
Multidisciplinary Sciences
Luisa Diomede, Stefania Rigacci, Margherita Romeo, Massimo Stefani, Mario Salmona
Article
Multidisciplinary Sciences
Cristina Grossi, Stefania Rigacci, Stefano Ambrosini, Teresa Ed Dami, Ilaria Luccarini, Chiara Traini, Paola Failli, Andrea Berti, Fiorella Casamenti, Massimo Stefani
Article
Chemistry, Physical
Tamer Al Kayal, Edda Russo, Laura Pieri, Gabriella Caminati, Debora Berti, Monica Bucciantini, Massimo Stefani, Piero Baglioni
Article
Biochemistry & Molecular Biology
Elisabetta Borchi, Valentina Bargelli, Valentina Guidotti, Andrea Berti, Massimo Stefani, Chiara Nediani, Stefania Rigacci
Review
Neurosciences
Fiorella Casamenti, Cristina Grossi, Stefania Rigacci, Daniela Pantano, Ilaria Luccarini, Massimo Stefani
JOURNAL OF ALZHEIMERS DISEASE
(2015)