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Impact of Tyrosine Amination on the Aggregation and Neurotoxicity of Amyloid-Β: Unveiling a Potential Defensive Mechanism in Alzheimer's Disease

https://doi.org/10.2139/ssrn.4954663
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Outgoing claims: the papers this work cites, builds on, or argues with.

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Site‐Directed Chemical Modification of Amyloid by Polyoxometalates for Inhibition of Protein Misfolding and Aggregation
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A Hexameric Peptide Barrel as Building Block of Amyloid‐β Protofibrils
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Protofibril–Fibril Interactions Inhibit Amyloid Fibril Assembly by Obstructing Secondary Nucleation
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Site‐Directed Chemical Modification of Amyloid by Polyoxometalates for Inhibition of Protein Misfolding and Aggregation
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H2O2/Nitrite‐Induced Post‐translational Modifications of Human Hemoglobin Determined by Mass Spectrometry: Redox Regulation of Tyrosine Nitration and 3‐Nitrotyrosine Reduction by Antioxidants
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An Azo Coupling Strategy for Protein 3‐Nitrotyrosine Derivatization
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Role of protein tyrosine nitration in neurodegenerative diseases and atherosclerosis
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Understanding peroxynitrite biochemistry and its potential for treating human diseases
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Oxidation and nitration of α-synuclein and their implications in neurodegenerative diseases
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Biochemistry of protein tyrosine nitration in cardiovascular pathology
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NIA‐AA Research Framework: Toward a biological definition of Alzheimer's disease
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Unveiling the human nitroproteome: Protein tyrosine nitration in cell signaling and cancer
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Nitration of amyloid-β peptide (1–42) as a protective mechanism for the amyloid-β peptide (1–42) against copper ion toxicity
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Nitration of Tyrosine 10 Critically Enhances Amyloid β Aggregation and Plaque Formation
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Nitration of hIAPP promotes its toxic oligomer formation and exacerbates its toxicity towards INS-1 cells
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Y12 nitration of human calcitonin (hCT): A promising strategy to produce non-aggregation bioactive hCT
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Fundamentals on the biochemistry of peroxynitrite and protein tyrosine nitration
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Reductive modification of genetically encoded 3-nitrotyrosine sites in alpha synuclein expressed in E.coli
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Alterations of 3-nitrotyrosine concentration in the cerebrospinal fluid during aging and in patients with Alzheimer's disease
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Infrared spectroscopy of proteins and peptides in lipid bilayers
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Alzheimer’s Disease: A Heme–Aβ Perspective
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Chemical and Enzymatic Transformations of Nimesulide to GSH Conjugates through Reductive and Oxidative Mechanisms
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Nitration of Tyrosine Residue Y10 of Aβ1–42 Significantly Inhibits Its Aggregation and Cytotoxicity
inferredcites →https://doi.org/10.1021/acs.chemrev.7b00568openalex-snapshot
Biochemistry of Peroxynitrite and Protein Tyrosine Nitration
inferredcites →https://doi.org/10.1021/acs.jafc.8b05404openalex-snapshot
Anthocyanins Extracted from Aronia melanocarpa Protect SH-SY5Y Cells against Amyloid-beta (1–42)-Induced Apoptosis by Regulating Ca2+ Homeostasis and Inhibiting Mitochondrial Dysfunction
inferredcites →https://doi.org/10.1021/cn900015vopenalex-snapshot
Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process
inferredcites →https://doi.org/10.1021/ja105684wopenalex-snapshot
Peroxynitrite Mediates Active Site Tyrosine Nitration in Manganese Superoxide Dismutase. Evidence of a Role for the Carbonate Radical Anion
inferredcites →https://doi.org/10.1021/ja204628bopenalex-snapshot
Heme–Cu Bound Aβ Peptides: Spectroscopic Characterization, Reactivity, and Relevance to Alzheimer’s Disease
inferredcites →https://doi.org/10.1021/ja206980qopenalex-snapshot
Copper-Catalyzed Tyrosine Nitration
inferredcites →https://doi.org/10.1021/jacs.4c01028openalex-snapshot
Protein Tyrosine Amination: Detection, Imaging, and Chemoproteomic Profiling with Synthetic Probes
inferredcites →https://doi.org/10.1021/jacs.5b11913openalex-snapshot
Amyloid β-Protein Assembly and Alzheimer’s Disease: Dodecamers of Aβ42, but Not of Aβ40, Seed Fibril Formation
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Mitochondrial Nitroreductase Activity Enables Selective Imaging and Therapeutic Targeting
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Identification of Aldehyde Oxidase as the Neonicotinoid Nitroreductase
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Key Roles for Tyrosine 10 in Aβ–Heme Complexes and Its Relevance to Oxidative Stress
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Nitration of Y10 in Aβ1–40: Is It a Compensatory Reaction against Oxidative/Nitrative Stress and Aβ Aggregation?
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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Pathways towards and away from Alzheimer's disease
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Molecular mechanisms of protein aggregation from global fitting of kinetic models
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Increased mitochondrial calcium levels associated with neuronal death in a mouse model of Alzheimer’s disease
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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
inferredcites →https://doi.org/10.1073/pnas.1401564111openalex-snapshot
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
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Synthetic Dimeric Aβ(28–40) Mimics the Complex Epitope of Human Anti-Aβ Autoantibodies against Toxic Aβ Oligomers
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Nitration of Tyrosine 247 Inhibits Protein Kinase G-1α Activity by Attenuating Cyclic Guanosine Monophosphate Binding
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Protein Tyrosine Nitration in the Mitochondria from Diabetic Mouse Heart
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