Cargando…

Capping of Aβ42 Oligomers by Small Molecule Inhibitors

[Image: see text] Aβ42 peptides associate into soluble oligomers and protofibrils in the process of forming the amyloid fibrils associated with Alzheimer’s disease. The oligomers have been reported to be more toxic to neurons than fibrils, and have been targeted by a wide range of small molecule and...

Descripción completa

Detalles Bibliográficos
Autores principales:	Fu, Ziao, Aucoin, Darryl, Ahmed, Mahiuddin, Ziliox, Martine, Van Nostrand, William E., Smith, Steven O.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	American Chemical Society 2014
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4278677/ https://www.ncbi.nlm.nih.gov/pubmed/25422864 http://dx.doi.org/10.1021/bi500910b

Ejemplares similares

Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils
por: Ahmed, Mahiuddin, et al.
Publicado: (2010)

Anti-Parallel β-Hairpin Structure in Soluble Aβ Oligomers of Aβ40-Dutch and Aβ40-Iowa
por: Fu, Ziao, et al.
Publicado: (2021)

Single-Molecule Imaging Reveals that Small Amyloid-β(1–42) Oligomers Interact with the Cellular Prion Protein (PrP(C))
por: Ganzinger, Kristina A, et al.
Publicado: (2014)

Effect of Lauric Acid on the Stability of Aβ(42) Oligomers
por: Khatua, Prabir, et al.
Publicado: (2021)

Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
por: Ruggeri, Francesco Simone, et al.
Publicado: (2021)

Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution
por: Wolff, Martin, et al.
Publicado: (2017)

Interaction of Aβ42 with Membranes Triggers the Self-Assembly into Oligomers
por: Banerjee, Siddhartha, et al.
Publicado: (2020)

Impact of Aβ40 and Aβ42 Fibrils on the Transcriptome of Primary Astrocytes and Microglia
por: Zhu, Xiaoyue, et al.
Publicado: (2022)

Nonphosphorylated tau slows down Aβ(1–42) aggregation, binds to Aβ(1–42) oligomers, and reduces Aβ(1–42) toxicity
por: Beeg, Marten, et al.
Publicado: (2021)

Structure of ring-shaped Aβ(42) oligomers determined by conformational selection
por: Tran, Linh, et al.
Publicado: (2016)

Critical aggregation concentration for the formation of early Amyloid-β (1–42) oligomers
por: Novo, Mercedes, et al.
Publicado: (2018)

Amyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets
por: Baldassarre, Maurizio, et al.
Publicado: (2017)

Aβ42-oligomer Interacting Peptide (AIP) neutralizes toxic amyloid-β42 species and protects synaptic structure and function
por: Barucker, Christian, et al.
Publicado: (2015)

The Role of Intracellular Ca(2+) and Mitochondrial ROS in Small Aβ(1-42) Oligomer-Induced Microglial Death
por: Jekabsone, Aiste, et al.
Publicado: (2023)

Oligomer Formation by Amyloid-β42 in a Membrane-Mimicking Environment in Alzheimer’s Disease
por: Rosenberry, Terrone L., et al.
Publicado: (2022)

Nanoelectrochemistry reveals how soluble Aβ(42) oligomers alter vesicular storage and release of glutamate
por: Yang, Xiao-Ke, et al.
Publicado: (2023)

Site specific NMR characterization of abeta-40 oligomers cross seeded by abeta-42 oligomers
por: Chang, Han-Wen, et al.
Publicado: (2022)

Lysosomal Enzyme Glucocerebrosidase Protects against Aβ(1-42) Oligomer-Induced Neurotoxicity
por: Choi, Seulah, et al.
Publicado: (2015)

S100B chaperone multimers suppress the formation of oligomers during Aβ42 aggregation
por: Figueira, António J., et al.
Publicado: (2023)

Cerebral vascular amyloid seeds drive amyloid β-protein fibril assembly with a distinct anti-parallel structure
por: Xu, Feng, et al.
Publicado: (2016)

Aβ42 oligomers modulate β-secretase through an XBP-1s-dependent pathway involving HRD1
por: Gerakis, Yannis, et al.
Publicado: (2016)

Cellular Prion Protein as a Receptor of Toxic Amyloid-β42 Oligomers Is Important for Alzheimer’s Disease
por: Zhang, Yuan, et al.
Publicado: (2019)

Cajaninstilbene Acid Ameliorates Cognitive Impairment Induced by Intrahippocampal Injection of Amyloid-β(1–42) Oligomers
por: Wang, Li-Sha, et al.
Publicado: (2019)

Carnosine Protects Macrophages against the Toxicity of Aβ1-42 Oligomers by Decreasing Oxidative Stress
por: Caruso, Giuseppe, et al.
Publicado: (2021)

Exploring the Pathological Effect of Aβ42 Oligomers on Neural Networks in Primary Cortical Neuron Culture
por: Ganbat, Dulguun, et al.
Publicado: (2023)

The intracerebral injection of Aβ(1-42) oligomers does not invariably alter seizure susceptibility in mice
por: Vande Vyver, Maxime, et al.
Publicado: (2023)

Alzheimer's Therapeutics Targeting Amyloid Beta 1–42 Oligomers II: Sigma-2/PGRMC1 Receptors Mediate Abeta 42 Oligomer Binding and Synaptotoxicity
por: Izzo, Nicholas J., et al.
Publicado: (2014)

Characterization of Homogeneous and Heterogeneous Amyloid-β42 Oligomer Preparations with Biochemical Methods and Infrared Spectroscopy Reveals a Correlation between Infrared Spectrum and Oligomer Size
por: Vosough, Faraz, et al.
Publicado: (2021)

Differentiating Aβ40 and Aβ42 in amyloid plaques with a small molecule fluorescence probe
por: Yang, Jing, et al.
Publicado: (2020)

Pharmacologic targeting of Cdc42 GTPase by a small molecule Cdc42 activity-specific inhibitor prevents platelet activation and thrombosis
por: Duan, Xin, et al.
Publicado: (2021)

Trodusquemine enhances Aβ(42) aggregation but suppresses its toxicity by displacing oligomers from cell membranes
por: Limbocker, Ryan, et al.
Publicado: (2019)

Intra‐gastrointestinal amyloid‐β1–42 oligomers perturb enteric function and induce Alzheimer's disease pathology
por: Sun, Yayi, et al.
Publicado: (2020)

Activated Bone Marrow-Derived Macrophages Eradicate Alzheimer's-Related Aβ(42) Oligomers and Protect Synapses
por: Li, Songlin, et al.
Publicado: (2020)

Aβ42 oligomer-specific antibody ALZ-201 reduces the neurotoxicity of Alzheimer’s disease brain extracts
por: Sandberg, Anders, et al.
Publicado: (2022)

Amphiphilic stilbene derivatives attenuate the neurotoxicity of soluble Aβ(42) oligomers by controlling their interactions with cell membranes
por: Yu, Zhengxin, et al.
Publicado: (2022)

Synthesis and electronic properties of pyridine end-capped cyclopentadithiophene-vinylene oligomers
por: Guijarro, Fernando G., et al.
Publicado: (2020)

Discovery of small molecule inhibitors that effectively disrupt IQGAP1-Cdc42 interaction in breast cancer cells
por: Sayedyahossein, Samar, et al.
Publicado: (2022)

Alzheimer's Therapeutics Targeting Amyloid Beta 1–42 Oligomers I: Abeta 42 Oligomer Binding to Specific Neuronal Receptors Is Displaced by Drug Candidates That Improve Cognitive Deficits
por: Izzo, Nicholas J., et al.
Publicado: (2014)

Small molecule-mediated co-assembly of amyloid-β oligomers reduces neurotoxicity through promoting non-fibrillar aggregation
por: Liu, Hao, et al.
Publicado: (2020)

Protection against Amyloid-β Oligomer Neurotoxicity by Small Molecules with Antioxidative Properties: Potential for the Prevention of Alzheimer’s Disease Dementia
por: Araki, Wataru, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_cli7lhmkmrhs0a0s19cmohpfog