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Chiral Interface of Amyloid Beta (Aβ): Relevance to Protein Aging, Aggregation and Neurodegeneration

https://doi.org/10.3390/sym12040585

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/jnr.10350openalex-snapshot

Isoaspartate formation at position 23 of amyloid beta peptide enhanced fibril formation and deposited onto senile plaques and vascular amyloids in Alzheimer's disease

inferredcites →https://doi.org/10.1007/s00401-016-1546-0openalex-snapshot

Phosphorylation of the amyloid β-peptide at Ser26 stabilizes oligomeric assembly and increases neurotoxicity

inferredcites →https://doi.org/10.1016/j.bpj.2008.10.022openalex-snapshot

Structural Differences between Aβ(1-40) Intermediate Oligomers and Fibrils Elucidated by Proteolytic Fragmentation and Hydrogen/Deuterium Exchange

inferredcites →https://doi.org/10.1016/j.bpj.2019.05.013openalex-snapshot

Protein Glycation by Glyoxal Promotes Amyloid Formation by Islet Amyloid Polypeptide

inferredcites →https://doi.org/10.1016/j.clinbiochem.2006.07.009openalex-snapshot

Biochemistry of amino acid racemization and clinical application to musculoskeletal disease

inferredcites →https://doi.org/10.1016/j.jalz.2017.07.595openalex-snapshot

[P4–435]: NON‐EQUILIBRIUM PHASE TRANSITION IN BIOCHEMICAL SYSTEMS: CHAIN OF CHIRALITY TRANSFER AS DETERMINANT OF BRAIN FUNCTIONAL LATERALITY — RELEVANCE TO ALZHEIMER DISEASE AND COGNITIVE PSYCHOLOGY

inferredcites →https://doi.org/10.1016/j.jtherbio.2017.06.004openalex-snapshot

The small heat shock protein Hsp27: Present understanding and future prospects

inferredcites →https://doi.org/10.1016/j.neuint.2017.08.007openalex-snapshot

APP/Aβ structural diversity and Alzheimer's disease pathogenesis

inferredcites →https://doi.org/10.1016/s0006-291x(86)80329-1openalex-snapshot

The presence of free D-aspartic acid in rodents and man

inferredcites →https://doi.org/10.1016/s0021-9258(17)34045-0openalex-snapshot

Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues.

inferredcites →https://doi.org/10.1016/s0021-9258(18)48354-8openalex-snapshot

Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II.

inferredcites →https://doi.org/10.1016/s0021-9258(18)53661-9openalex-snapshot

Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease.

inferredcites →https://doi.org/10.1016/s0047-6374(01)00363-3openalex-snapshot

Racemization of aspartic acid in human proteins

inferredcites →https://doi.org/10.1016/s0076-6879(99)09009-6openalex-snapshot

[7] Chemical modifications of deposited amyloid-β peptides

inferredcites →https://doi.org/10.1016/s0306-4522(01)00155-5openalex-snapshot

Drastic neuronal loss in vivo by β-amyloid racemized at Ser26 residue: conversion of non-toxic [D-Ser26]β-amyloid 1–40 to toxic and proteinase-resistant fragments

inferredcites →https://doi.org/10.1016/s0925-4439(98)00014-3openalex-snapshot

Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of Aβ peptides of Alzheimer's disease

inferredcites →https://doi.org/10.1021/ja953505bopenalex-snapshot

Accelerated Racemization of Aspartic Acid and Asparagine Residues via Succinimide Intermediates: An ab Initio Theoretical Exploration of Mechanism

inferredcites →https://doi.org/10.1021/tx500353sopenalex-snapshot

Nitration of Y10 in Aβ1–40: Is It a Compensatory Reaction against Oxidative/Nitrative Stress and Aβ Aggregation?

inferredcites →https://doi.org/10.1038/ncomms11359openalex-snapshot

Phosphorylation modifies the molecular stability of β-amyloid deposits

inferredcites →https://doi.org/10.1038/nsmb.2991openalex-snapshot

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

inferredcites →https://doi.org/10.1038/s41467-019-11183-zopenalex-snapshot

Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface

inferredcites →https://doi.org/10.1038/s41598-017-10422-xopenalex-snapshot

Diversity of Amyloid-beta Proteoforms in the Alzheimer’s Disease Brain

inferredcites →https://doi.org/10.1038/s41598-019-54918-0openalex-snapshot

Structural and biochemical basis of the formation of isoaspartate in the complementarity-determining region of antibody 64M-5 Fab

inferredcites →https://doi.org/10.1038/tp.2015.52openalex-snapshot

d-serine levels in Alzheimer’s disease: implications for novel biomarker development

inferredcites →https://doi.org/10.1039/c4ra04694copenalex-snapshot

Unusual post-translational protein modifications: the benefits of sophistication

inferredcites →https://doi.org/10.1039/c7mb00249aopenalex-snapshot

Phosphorylation of a full length amyloid-β peptide modulates its amyloid aggregation, cell binding and neurotoxic properties

inferredcites →https://doi.org/10.1039/c8cc03235aopenalex-snapshot

Chiral modulation of amyloid beta fibrillation and cytotoxicity by enantiomeric carbon dots

inferredcites →https://doi.org/10.1042/bst0380539openalex-snapshot

Alzheimer's disease and amyloid β-peptide deposition in the brain: a matter of ‘aging’?

inferredcites →https://doi.org/10.1073/pnas.0501823102openalex-snapshot

Implications of the serine protease HtrA1 in amyloid precursor protein processing

inferredcites →https://doi.org/10.1073/pnas.1620001114openalex-snapshot

How nonequilibrium thermodynamics speaks to the mystery of life

inferredcites →https://doi.org/10.1074/jbc.m111.279133openalex-snapshot

Phosphorylation of Amyloid-β Peptide at Serine 8 Attenuates Its Clearance via Insulin-degrading and Angiotensin-converting Enzymes

inferredcites →https://doi.org/10.1093/jnen/62.3.248openalex-snapshot

β-Amyloid Racemized at the Ser26Residue in the Brains of Patients with Alzheimer Disease: Implications in the Pathogenesis of Alzheimer Disease

inferredcites →https://doi.org/10.1097/00001756-200112040-00047openalex-snapshot

Phosphorylation of amyloid-β at the serine 26 residue by human cdc2 kinase

inferredcites →https://doi.org/10.1111/j.1432-1033.1994.t01-1-00917.xopenalex-snapshot

Aspartate‐Bond Isomerization Affects the Major Conformations of Synthetic Peptides

inferredcites →https://doi.org/10.1111/j.1471-4159.1988.tb13231.xopenalex-snapshot

Neuritic Plaque Amyloid in Alzheimer's Disease Is Highly Racemized

inferredcites →https://doi.org/10.1159/000212218openalex-snapshot

Considerations on the Role of Aspartic Acid Racemization in the Aging Process

inferredcites →https://doi.org/10.1186/1471-2105-12-190openalex-snapshot

Stereochemical errors and their implications for molecular dynamics simulations

inferredcites →https://doi.org/10.1371/journal.pone.0128553openalex-snapshot

Preclinical Pharmacokinetic Studies of the Tritium Labelled D-Enantiomeric Peptide D3 Developed for the Treatment of Alzheimer´s Disease

inferredcites →https://doi.org/10.1371/journal.pone.0161526openalex-snapshot

Distinct 3D Architecture and Dynamics of the Human HtrA2(Omi) Protease and Its Mutated Variants

inferredcites →https://doi.org/10.15698/cst2018.07.143openalex-snapshot

Alzheimer’s disease: amyloid-based pathogenesis and potential therapies

inferredcites →https://doi.org/10.1620/tjem.174.251openalex-snapshot

Racemization: Its Biological Significance on Neuropathogenesis of Alzheimer's Disease.

inferredcites →https://doi.org/10.18632/aging.100362openalex-snapshot

Phosphorylation of amyloid beta (Aβ) peptides – A trigger for formation of toxic aggregates in Alzheimer's disease

inferredcites →https://doi.org/10.2174/1389203717666160311115750openalex-snapshot

Pathogenic Role of Serine Protease HtrA2/Omi in Neurodegenerative Diseases

inferredcites →https://doi.org/10.3389/fchem.2019.00472openalex-snapshot

Three Decades of Amyloid Beta Synthesis: Challenges and Advances

inferredcites →https://doi.org/10.3389/fgene.2014.00346openalex-snapshot

Heat shock protein 27 phosphorylation state is associated with cancer progression

inferredcites →https://doi.org/10.3389/fnmol.2018.00302openalex-snapshot

Phosphorylation of the Amyloid-Beta Peptide Inhibits Zinc-Dependent Aggregation, Prevents Na,K-ATPase Inhibition, and Reduces Cerebral Plaque Deposition

inferredcites →https://doi.org/10.3390/catal7120363openalex-snapshot

Racemization of Serine Residues Catalyzed by Dihydrogen Phosphate Ion: A Computational Study

inferredcites →https://doi.org/10.3390/ijms17101698openalex-snapshot

Racemization of the Succinimide Intermediate Formed in Proteins and Peptides: A Computational Study of the Mechanism Catalyzed by Dihydrogen Phosphate Ion

inferredcites →https://doi.org/10.3390/sym11060814openalex-snapshot

Chemical Basis of Biological Homochirality during the Abiotic Evolution Stages on Earth

inferredcites →https://doi.org/10.3748/wjg.v22.i27.6192openalex-snapshot

Aberrant post-translational protein modifications in the pathogenesis of alcohol-induced liver injury

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