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Active Site Environment of Heme-Bound Amyloid β Peptide Associated with Alzheimer’s Disease
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Characterization and Peroxidase Activity of a Myoglobin Mutant Containing a Distal Arginine
inferredcites →https://doi.org/10.1002/ana.410370609openalex-snapshot
Expression of heme oxygenase‐1 in the senescent and alzheimer‐diseased brain
inferredcites →https://doi.org/10.1002/cbic.200700111openalex-snapshot
Redox Chemistry of Copper–Amyloid‐β: The Generation of Hydroxyl Radical in the Presence of Ascorbate is Linked to Redox‐Potentials and Aggregation State
inferredcites →https://doi.org/10.1002/jnr.10087openalex-snapshot
Brain metabolism and brain disease: Is metabolic deficiency the proximate cause of Alzheimer dementia?
inferredcites →https://doi.org/10.1016/0005-2795(71)90170-xopenalex-snapshot
An electron paramagnetic resonance study of Aplysia myoglobin
inferredcites →https://doi.org/10.1016/0006-3002(59)90407-xopenalex-snapshot
Cleavage of the haem-protein link by acid methylethylketone
inferredcites →https://doi.org/10.1016/0022-2836(81)90254-0openalex-snapshot
Structure of beef liver catalase
inferredcites →https://doi.org/10.1016/j.abb.2009.05.003openalex-snapshot
Human and rodent amyloid-β peptides differentially bind heme: Relevance to the human susceptibility to Alzheimer’s disease
inferredcites →https://doi.org/10.1016/s0006-291x(84)80190-4openalex-snapshot
Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
inferredcites →https://doi.org/10.1016/s0021-9258(18)50024-7openalex-snapshot
Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants
inferredcites →https://doi.org/10.1016/s0021-9258(18)93520-9openalex-snapshot
The Electronic Structure of Protoheme Proteins
inferredcites →https://doi.org/10.1016/s0040-4020(01)97504-0openalex-snapshot
A safer substitute for benzidine in the detection of blood
inferredcites →https://doi.org/10.1016/s0166-2236(03)00067-5openalex-snapshot
The metallobiology of Alzheimer's disease
inferredcites →https://doi.org/10.1016/s0197-4580(00)00112-3openalex-snapshot
A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
inferredcites →https://doi.org/10.1016/s0197-4580(00)00128-7openalex-snapshot
Increased bilirubins and their derivatives in cerebrospinal fluid in Alzheimer’s disease
inferredcites →https://doi.org/10.1016/s0531-5565(00)00112-1openalex-snapshot
Oxidative processes in Alzheimer's disease: the role of Aβ-metal interactions
inferredcites →https://doi.org/10.1021/bi047611eopenalex-snapshot
N-Terminal Deletions Modify the Cu2+Binding Site in Amyloid-β
inferredcites →https://doi.org/10.1021/bi990438fopenalex-snapshot
The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction
inferredcites →https://doi.org/10.1021/ja068952dopenalex-snapshot
Role of Aspartate-1 in Cu(II) Binding to the Amyloid-β Peptide of Alzheimer's Disease
inferredcites →https://doi.org/10.1039/b807980nopenalex-snapshot
The chemistry of Alzheimer’s disease
inferredcites →https://doi.org/10.1073/pnas.0404349101openalex-snapshot
A role for heme in Alzheimer's disease: Heme binds amyloid β and has altered metabolism
inferredcites →https://doi.org/10.1073/pnas.0600134103openalex-snapshot
Amyloid-β peptide binds with heme to form a peroxidase: Relationship to the cytopathologies of Alzheimer’s disease
inferredcites →https://doi.org/10.1073/pnas.63.3.934openalex-snapshot
HEMOGLOBIN A: AN ELECTRON PARAMAGNETIC RESONANCE STUDY OF THE EFFECTS OF INTERCHAIN CONTACTS ON THE HEME SYMMETRY OF HIGH-SPIN AND LOW-SPIN DERIVATIVES OF FERRIC ALPHA CHAINS
inferredcites →https://doi.org/10.1073/pnas.82.12.4245openalex-snapshot
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
inferredcites →https://doi.org/10.1074/jbc.271.8.4023openalex-snapshot
Role of Arginine 38 in Horseradish Peroxidase
inferredcites →https://doi.org/10.1074/jbc.274.49.35005openalex-snapshot
The Structures of the Horseradish Peroxidase C-Ferulic Acid Complex and the Ternary Complex with Cyanide Suggest How Peroxidases Oxidize Small Phenolic Substrates
inferredcites →https://doi.org/10.1074/jbc.m100175200openalex-snapshot
Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits
inferredcites →https://doi.org/10.1074/jbc.m108362200openalex-snapshot
Heme Deficiency Selectively Interrupts Assembly of Mitochondrial Complex IV in Human Fibroblasts
inferredcites →https://doi.org/10.1074/jbc.m206428200openalex-snapshot
Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid
inferredcites →https://doi.org/10.1074/jbc.m313572200openalex-snapshot
Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease
inferredcites →https://doi.org/10.1074/jbc.m600417200openalex-snapshot
Copper-mediated Amyloid-β Toxicity Is Associated with an Intermolecular Histidine Bridge
inferredcites →https://doi.org/10.1097/00002093-200307000-00005openalex-snapshot
Copper, Zinc, and the Metallobiology of Alzheimer Disease
inferredcites →https://doi.org/10.1097/00005072-198107000-00009openalex-snapshot
The Structure of Neuritic Plaques in the Cerebral Cortex of Aged Rats
inferredcites →https://doi.org/10.1111/j.1432-1033.1987.tb11057.xopenalex-snapshot
Cytochrome c oxidase is three‐copper, two‐heme‐A protein
inferredcites →https://doi.org/10.1111/j.1750-3639.1999.tb00215.xopenalex-snapshot
Oxidative Alterations in Alzheimer's Disease
inferredcites →https://doi.org/10.1126/science.1072994openalex-snapshot
The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics
inferredcites →https://doi.org/10.1126/science.120.3105.32openalex-snapshot
Sulfide Inhibition of Catalase
inferredcites →https://doi.org/10.2174/156720505774932232openalex-snapshot
Activity-Dependent Synapse Modulation and the Pathogenesis of Alzheimer Disease
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.1002/anie.201302989openalex-snapshot
Heme Binding Induces Dimerization and Nitration of Truncated β‐Amyloid Peptide Aβ16 Under Oxidative Stress
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Amyloid beta–heme peroxidase promoted protein nitrotyrosination: relevance to widespread protein nitration in Alzheimer’s disease
inferred← citeshttps://doi.org/10.1007/s00775-012-0922-zopenalex-snapshot
Amyloid beta modulated the selectivity of heme-catalyzed protein tyrosine nitration: an alternative mechanism for selective protein nitration
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Kinetics of serotonin oxidation by heme–Aβ relevant to Alzheimer’s disease
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Interaction of apoNeuroglobin with heme–Aβ complexes relevant to Alzheimer’s disease
inferred← citeshttps://doi.org/10.1007/s00775-016-1367-6openalex-snapshot
Cytochrome c peroxidase activity of heme bound amyloid β peptides
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The secondary coordination sphere and axial ligand effects on oxygen reduction reaction by iron porphyrins: a DFT computational study
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Metal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry
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inferred← citeshttps://doi.org/10.1016/bs.adioch.2022.07.003openalex-snapshot
Heme/Cu-oxygen intermediates of amyloid β peptides associated with Alzheimer's disease
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High-affinity binding and catalytic activity of His/Tyr-based sequences: Extending heme-regulatory motifs beyond CP
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inferred← citeshttps://doi.org/10.1016/j.brainres.2015.09.034openalex-snapshot
Amyloid β25–35 induced ROS-burst through NADPH oxidase is sensitive to iron chelation in microglial Bv2 cells
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Metal-associated amyloid-β species in Alzheimer's disease
inferred← citeshttps://doi.org/10.1016/j.cbpa.2022.102142openalex-snapshot
Assembly of redox active metallo-enzymes and metallo-peptides on electrodes: Abiological constructs to probe natural processes
inferred← citeshttps://doi.org/10.1016/j.ccr.2012.02.025openalex-snapshot
Interaction of amyloid β peptides with redox active heme cofactor: Relevance to Alzheimer's disease
inferred← citeshttps://doi.org/10.1016/j.ccr.2012.03.037openalex-snapshot
Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-β peptides involved in Alzheimer disease. Part 1: An overview
inferred← citeshttps://doi.org/10.1016/j.ccr.2017.05.007openalex-snapshot
Alzheimer’s disease: How metal ions define β-amyloid function
inferred← citeshttps://doi.org/10.1016/j.ccr.2020.213255openalex-snapshot
Metal complexes that bind to the amyloid-β peptide of relevance to Alzheimer’s disease
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Is there correlation between Aβ-heme peroxidase activity and the peptide aggregation state? A literature review combined with hypothesis
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Modulation effect of acidulated human serum albumin on Cu 2+ -mediated amyloid β-protein aggregation and cytotoxicity under a mildly acidic condition
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Heme prevents highly amyloidogenic human calcitonin (hCT) aggregation: A potential new strategy for the clinical reuse of hCT
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Interaction of ApoMyoglobin with Heme-hIAPP complex
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In vitro coordination of Fe-protoheme with amyloid β is non-specific and exhibits multiple equilibria
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Heme-Aβ in SDS micellar environment: Active site environment and reactivity
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Hemin, copper and amyloid-β: A medley involved in Alzheimer's disease. An interaction that fine regulates the reactivity
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Heme and lithospermic acid synergistically inhibit aggregation of human islet amyloid polypeptide: A novel hIAPP inhibitor for the potential therapy of type 2 diabetes
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Effect of mutation on Aβ1-42-Heme complex in aggregation mechanism: Alzheimer’s disease
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inferred← citeshttps://doi.org/10.1021/acs.jmedchem.6b01432openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/acsami.0c15147openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/acsami.5b11567openalex-snapshot
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Multiple Function Fluorescein Probe Performs Metal Chelation, Disaggregation, and Modulation of Aggregated Aβ and Aβ-Cu Complex
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inferred← citeshttps://doi.org/10.1021/acsomega.1c06056openalex-snapshot
Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces
inferred← citeshttps://doi.org/10.1021/acsomega.8b01736openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/acssuschemeng.9b04216openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/cn300231qopenalex-snapshot
Interaction between Amyloid-β Peptide and Heme Probed by Electrochemistry and Atomic Force Microscopy
inferred← citeshttps://doi.org/10.1021/cr300009xopenalex-snapshot
Bioinorganic Chemistry of Alzheimer’s Disease
inferred← citeshttps://doi.org/10.1021/ct400364bopenalex-snapshot
Fe(III)–Heme Complexes with the Amyloid Beta Peptide of Alzheimer’s Disease: QM/MM Investigations of Binding and Redox Properties of Heme Bound to the His Residues of Aβ(1–42)
inferred← citeshttps://doi.org/10.1021/ic301865nopenalex-snapshot
Ligand-Field and Ligand-Binding Analysis of the Active Site of Copper-Bound Aβ Associated with Alzheimer’s Disease
inferred← citeshttps://doi.org/10.1021/ic302131nopenalex-snapshot
Interaction of NO with Cu and Heme-Bound Aβ Peptides Associated with Alzheimer’s Disease
inferred← citeshttps://doi.org/10.1021/ic302369vopenalex-snapshot
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inferred← citeshttps://doi.org/10.1021/ic4001413openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/ic401771jopenalex-snapshot
Apomyoglobin Sequesters Heme from Heme Bound Aβ Peptides
inferred← citeshttps://doi.org/10.1021/ic402297fopenalex-snapshot
Selective 4e–/4H+ O2 Reduction by an Iron(tetraferrocenyl)Porphyrin Complex: From Proton Transfer Followed by Electron Transfer in Organic Solvent to Proton Coupled Electron Transfer in Aqueous Medium
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Molecular Structures and Solvation of Free Monomeric and Dimeric Ferriheme in Aqueous Solution: Insights from Molecular Dynamics Simulations and Extended X-ray Absorption Fine Structure Spectroscopy
inferred← citeshttps://doi.org/10.1021/ja204628bopenalex-snapshot
Heme–Cu Bound Aβ Peptides: Spectroscopic Characterization, Reactivity, and Relevance to Alzheimer’s Disease
inferred← citeshttps://doi.org/10.1021/ja303930fopenalex-snapshot
Self-Assembled Monolayers of Aβ peptides on Au Electrodes: An Artificial Platform for Probing the Reactivity of Redox Active Metals and Cofactors Relevant to Alzheimer’s Disease
inferred← citeshttps://doi.org/10.1021/jacsau.2c00572openalex-snapshot
The Role of Heme and Copper in Alzheimer’s Disease and Type 2 Diabetes Mellitus
inferred← citeshttps://doi.org/10.1021/jacsau.6c00856openalex-snapshot
Heme-Catalyzed Dityrosine Formation and Serotonin Oxidation in the Presence of Insulin
inferred← citeshttps://doi.org/10.1021/tx300441eopenalex-snapshot
Aβ Interacts with Both the Iron Center and the Porphyrin Ring of Heme: Mechanism of Heme’s Action on Aβ Aggregation and Disaggregation
inferred← citeshttps://doi.org/10.1021/tx5003035openalex-snapshot
Key Roles for Tyrosine 10 in Aβ–Heme Complexes and Its Relevance to Oxidative Stress
inferred← citeshttps://doi.org/10.1038/aps.2014.166openalex-snapshot
Curcumin inhibits appoptosin-induced apoptosis via upregulating heme oxygenase-1 expression in SH-SY5Y cells
inferred← citeshttps://doi.org/10.1038/s42003-021-02026-zopenalex-snapshot
Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects
inferred← citeshttps://doi.org/10.1039/c2cc37626aopenalex-snapshot
Analogues of oxy-heme Aβ: reactive intermediates relevant to Alzheimer's disease
inferred← citeshttps://doi.org/10.1039/c3cp52354copenalex-snapshot
Heme prevents amyloid beta peptide aggregation through hydrophobic interaction based on molecular dynamics simulation
inferred← citeshttps://doi.org/10.1039/c3md00019bopenalex-snapshot
Synthesis and biological evaluation of primaquine–chloroquine twin drug: a novel heme-interacting molecule prevents free heme and hydroxyl radical-mediated protein degradation
inferred← citeshttps://doi.org/10.1039/c4cs00138aopenalex-snapshot
Biological metals and metal-targeting compounds in major neurodegenerative diseases
inferred← citeshttps://doi.org/10.1039/c4dt01991aopenalex-snapshot
Self-assembly of stable oligomeric and fibrillar aggregates of Aβ peptides relevant to Alzheimer's disease: morphology dependent Cu/heme toxicity and inhibition of PROS generation
inferred← citeshttps://doi.org/10.1039/c6dt02183bopenalex-snapshot
Interactions between heme and tau-derived R1 peptides: binding and oxidative reactivity
inferred← citeshttps://doi.org/10.1039/c6mt00214eopenalex-snapshot
Fe–oxy adducts of heme–Aβ and heme–hIAPP complexes: intermediates in ROS generation
inferred← citeshttps://doi.org/10.1039/c7an01683bopenalex-snapshot
Combined determination of copper ions and β-amyloid peptide by a single ratiometric electrochemical biosensor
inferred← citeshttps://doi.org/10.1039/c7dt01700fopenalex-snapshot
Copper induced spin state change of heme–Aβ associated with Alzheimer's disease
inferred← citeshttps://doi.org/10.1039/c7dt01822copenalex-snapshot
NPY binds with heme to form a NPY–heme complex: enhancing peroxidase activity in free heme and promoting NPY nitration and inactivation
inferred← citeshttps://doi.org/10.1039/c7ta09179fopenalex-snapshot
Functional adlayers on Au electrodes: some recent applications in hydrogen evolution and oxygen reduction
inferred← citeshttps://doi.org/10.1039/c8ay02743aopenalex-snapshot
Electrochemical sensing of H 2 O 2 released from living cells based on AuPd alloy-modified PDA nanotubes
inferred← citeshttps://doi.org/10.1039/c8nr02573hopenalex-snapshot
Facile synthesis of 3D N-doped porous carbon nanosheets as highly active electrocatalysts toward the reduction of hydrogen peroxide
inferred← citeshttps://doi.org/10.1039/c8sc01992dopenalex-snapshot
Photoactive chlorin e6 is a multifunctional modulator of amyloid-β aggregation and toxicity via specific interactions with its histidine residues
inferred← citeshttps://doi.org/10.1039/c9cc09758aopenalex-snapshot
Peroxidase activity of heme bound amyloid β peptides associated with Alzheimer's disease
inferred← citeshttps://doi.org/10.1039/c9dt00914kopenalex-snapshot
Nitrite reductase activity of heme and copper bound Aβ peptides
inferred← citeshttps://doi.org/10.1039/c9nr00473dopenalex-snapshot
Multifunctional carbon dots as a therapeutic nanoagent for modulating Cu( ii )-mediated β-amyloid aggregation
inferred← citeshttps://doi.org/10.1039/c9nr09148copenalex-snapshot
A robust Mn@FeNi-S/graphene oxide nanocomposite as a high-efficiency catalyst for the non-enzymatic electrochemical detection of hydrogen peroxide
inferred← citeshttps://doi.org/10.1039/c9sc01679aopenalex-snapshot
Formation of compound I in heme bound Aβ-peptides relevant to Alzheimer's disease
inferred← citeshttps://doi.org/10.1039/d0sc01020kopenalex-snapshot
Molecular crowding effects on the biochemical properties of amyloid β–heme, Aβ–Cu and Aβ–heme–Cu complexes
inferred← citeshttps://doi.org/10.1039/d0sc06258hopenalex-snapshot
Intermediates involved in serotonin oxidation catalyzed by Cu bound Aβ peptides
inferred← citeshttps://doi.org/10.1039/d2dt00162dopenalex-snapshot
Simultaneous binding of heme and Cu with amyloid β peptides: active site and reactivities
inferred← citeshttps://doi.org/10.1039/d2sc05008kopenalex-snapshot
Spin state dependent peroxidase activity of heme bound amyloid β peptides relevant to Alzheimer's disease
inferred← citeshttps://doi.org/10.1039/d3cc04657eopenalex-snapshot
In situ monitoring of ROS secretion from single cells with a dual-nanopore biosensor
inferred← citeshttps://doi.org/10.1039/d3cc05025dopenalex-snapshot
Rapid autoxidation of ferrous heme-Aβ complexes relevant to Alzheimer's disease
inferred← citeshttps://doi.org/10.1039/d5cs00544bopenalex-snapshot
Mechanism of oxidative stress and neurotoxicity associated with heme and copper–Aβ relevant to Alzheimer's disease
inferred← citeshttps://doi.org/10.1039/d5dt00234fopenalex-snapshot
Heme–Aβ compound 0: a common intermediate in ROS generation and peroxidase activity
inferred← citeshttps://doi.org/10.1039/d6cc03615eopenalex-snapshot
Heme–copper–Aβ mediated dopamine oxidation through self-sustaining redox cycling
inferred← citeshttps://doi.org/10.1101/629238openalex-snapshot
Heme minimizes Parkinson’s disease-associated toxicity by inducing a conformational distortion in the oligomers of alpha-Synuclein
inferred← citeshttps://doi.org/10.1142/s1088424621500346openalex-snapshot
Electronic structure and reactivity of heme bound insulin
inferred← citeshttps://doi.org/10.1149/1945-7111/abe44bopenalex-snapshot
A Highly Efficient Nonenzymatic Hydrogen Peroxide Electrochemical Sensor Using Mesoporous Carbon Doped ZnO Nanocomposite
inferred← citeshttps://doi.org/10.1149/1945-7111/ad2644openalex-snapshot
Efficient Amperometric Detection of H2O2 using Gold Nanoparticle decorated Polythiophene/Hematite Ore Nanocomposite
inferred← citeshttps://doi.org/10.1186/s13195-020-00634-1openalex-snapshot
Plasma transferrin and hemopexin are associated with altered Aβ uptake and cognitive decline in Alzheimer’s disease pathology
inferred← citeshttps://doi.org/10.1515/bmc.2011.019openalex-snapshot
Beta-amyloid oligomers: recent developments
inferred← citeshttps://doi.org/10.1517/17460441.2011.550914openalex-snapshot
The concept of privileged structures in rational drug design: focus on acridine and quinoline scaffolds in neurodegenerative and protozoan diseases
inferred← citeshttps://doi.org/10.20964/2022.04.38openalex-snapshot
Hedgehog Shaped Microspheres Assembled by Mn2CuO4 Nanobelts Decorated on Graphene Oxide for Highly Efficient Sensing of Hydrogen Peroxide
inferred← citeshttps://doi.org/10.2139/ssrn.4869989openalex-snapshot
Hybrid Graphene Nanoflakes for Electrochemical Sensing with Multianalyte Detection Capability
inferred← citeshttps://doi.org/10.3389/fmolb.2020.590979openalex-snapshot
Low Cerebrospinal Fluid Levels of Hemopexin Are Associated With Increased Alzheimer's Pathology, Hippocampal Hypometabolism, and Cognitive Decline
inferred← citeshttps://doi.org/10.3390/antiox12071319openalex-snapshot
Biological Oxidations and Nitrations Promoted by the Hemin–Aβ16 Complex
inferred← citeshttps://doi.org/10.3390/antiox13121441openalex-snapshot
The Neural Palette of Heme: Altered Heme Homeostasis Underlies Defective Neurotransmission, Increased Oxidative Stress, and Disease Pathogenesis
inferred← citeshttps://doi.org/10.3390/biom13071031openalex-snapshot
Shapes and Patterns of Heme-Binding Motifs in Mammalian Heme-Binding Proteins
inferred← citeshttps://doi.org/10.3390/bios10110151openalex-snapshot
Progress of Advanced Nanomaterials in the Non-Enzymatic Electrochemical Sensing of Glucose and H2O2
inferred← citeshttps://doi.org/10.3390/bios13070704openalex-snapshot
A Flexible and Transparent PtNP/SWCNT/PET Electrochemical Sensor for Nonenzymatic Detection of Hydrogen Peroxide Released from Living Cells with Real-Time Monitoring Capability
inferred← citeshttps://doi.org/10.3390/chemosensors8030063openalex-snapshot
Electrochemical Detection of H2O2 Released from Prostate Cancer Cells Using Pt Nanoparticle-Decorated rGO–CNT Nanocomposite-Modified Screen-Printed Carbon Electrodes
inferred← citeshttps://doi.org/10.3390/molecules25215044openalex-snapshot
Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes
inferred← citeshttps://doi.org/10.4062/biomolther.2024.224openalex-snapshot
Pro-Oxidative and Inflammatory Actions of Extracellular Hemoglobin and Heme: Molecular Events and Implications for Alzheimer's and Parkinson Disease
inferred← citeshttps://doi.org/10.4103/1673-5374.235021openalex-snapshot
Amyloid β and free heme: bloody new insights into the pathogenesis of Alzheimer’s disease
inferred← citeshttps://doi.org/10.7150/thno.30649openalex-snapshot
Using near-infrared enhanced thermozyme and scFv dual-conjugated Au nanorods for detection and targeted photothermal treatment of Alzheimer's disease
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