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Disease-specific tau polymorphs define unique protein interaction networks across proteinopathies

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Molecular cloning of human growth inhibitory factor cDNA and its down‐regulation in Alzheimer's disease.
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Mass Spectrometry Analysis of Lysine Posttranslational Modifications of Tau Protein from Alzheimer’s Disease Brain
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Phosphorylated serine 199 of microtubule-associated protein tau is a neuronal epitope abundantly expressed in youth and an early marker of tau pathology
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Distribution patterns of tau pathology in progressive supranuclear palsy
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Tau strains shape disease
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A Pharmacogenomics-Based In Silico Investigation of Opioid Prescribing in Post-operative Spine Pain Management and Personalized Therapy
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The Crosstalk Between Pathological Tau Phosphorylation and Mitochondrial Dysfunction as a Key to Understanding and Treating Alzheimer’s Disease
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Phosphomimetics at Ser199/Ser202/Thr205 in Tau Impairs Axonal Transport in Rat Hippocampal Neurons
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Axotrophin/MARCH7 acts as an E3 ubiquitin ligase and ubiquitinates tau protein in vitro impairing microtubule binding
inferredcites →https://doi.org/10.1016/j.cell.2021.12.041openalex-snapshot
Tau interactome maps synaptic and mitochondrial processes associated with neurodegeneration
inferredcites →https://doi.org/10.1016/j.cell.2022.09.002openalex-snapshot
X-linked ubiquitin-specific peptidase 11 increases tauopathy vulnerability in women
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α-Synuclein Multimers Cluster Synaptic Vesicles and Attenuate Recycling
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Redox activity of α-synuclein–Cu is silenced by Zn7-metallothionein-3
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Membrane insertion exacerbates the α-Synuclein-Cu(II) dopamine oxidase activity: Metallothionein-3 targets and silences all α-synuclein-Cu(II) complexes
inferredcites →https://doi.org/10.1016/j.jbc.2022.101766openalex-snapshot
Lysine 63-linked ubiquitination of tau oligomers contributes to the pathogenesis of Alzheimer’s disease
inferredcites →https://doi.org/10.1016/j.nbd.2022.105737openalex-snapshot
SOD1 mediates lysosome-to-mitochondria communication and its dysregulation by amyloid-β oligomers
inferredcites →https://doi.org/10.1016/j.neuron.2010.08.044openalex-snapshot
Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy
inferredcites →https://doi.org/10.1016/j.neuron.2016.09.055openalex-snapshot
Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo
inferredcites →https://doi.org/10.1016/j.neuron.2023.04.020openalex-snapshot
Synaptic oligomeric tau in Alzheimer’s disease — A potential culprit in the spread of tau pathology through the brain
inferredcites →https://doi.org/10.1016/j.parkreldis.2020.09.030openalex-snapshot
Prevalence and clinical associations of tau in Lewy body dementias: A systematic review and meta-analysis
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Biochemical pathways that regulate acetyltransferase and deacetylase activity in mammalian cells
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Optimized proximity ligation assay (PLA) for detection of RNA-protein complex interactions in cell lines
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Metallothionein III is reduced in Alzheimer’s disease
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Tau biomarkers in Alzheimer's disease: towards implementation in clinical practice and trials
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Cytoscape stringApp 2.0: Analysis and Visualization of Heterogeneous Biological Networks
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Quantitative Assessment of the Effects of Trypsin Digestion Methods on Affinity Purification–Mass Spectrometry-based Protein–Protein Interaction Analysis
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Cytoscape StringApp: Network Analysis and Visualization of Proteomics Data
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A Network Module for the Perseus Software for Computational Proteomics Facilitates Proteome Interaction Graph Analysis
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Site-Specific Phospho-Tau Aggregation-Based Biomarker Discovery for AD Diagnosis and Differentiation
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Proteome survey reveals modularity of the yeast cell machinery
inferredcites →https://doi.org/10.1038/nature23002openalex-snapshot
Cryo-EM structures of tau filaments from Alzheimer’s disease
inferredcites →https://doi.org/10.1038/nbt.1511openalex-snapshot
MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
inferredcites →https://doi.org/10.1038/ncomms1255openalex-snapshot
The acetylation of tau inhibits its function and promotes pathological tau aggregation
inferredcites →https://doi.org/10.1038/ncomms9490openalex-snapshot
Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer’s disease brain
inferredcites →https://doi.org/10.1038/nmeth.3901openalex-snapshot
The Perseus computational platform for comprehensive analysis of (prote)omics data
inferredcites →https://doi.org/10.1038/s41392-024-01800-9openalex-snapshot
Protein neddylation and its role in health and diseases
inferredcites →https://doi.org/10.1038/s41398-020-00954-8openalex-snapshot
Neuroinflammation in dementia with Lewy bodies: a human post-mortem study
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Alpha-synuclein in Parkinson’s disease and other synucleinopathies: from overt neurodegeneration back to early synaptic dysfunction
inferredcites →https://doi.org/10.1038/s41419-023-05909-7openalex-snapshot
High glucose induces tau hyperphosphorylation in hippocampal neurons via inhibition of ALKBH5-mediated Dgkh m6A demethylation: a potential mechanism for diabetic cognitive dysfunction
inferredcites →https://doi.org/10.1038/s41467-019-13787-xopenalex-snapshot
Transmission of tauopathy strains is independent of their isoform composition
inferredcites →https://doi.org/10.1038/s41467-020-18022-6openalex-snapshot
RNA-binding proteins Musashi and tau soluble aggregates initiate nuclear dysfunction
inferredcites →https://doi.org/10.1038/s41467-021-23597-9openalex-snapshot
UBE4B, a microRNA-9 target gene, promotes autophagy-mediated Tau degradation
inferredcites →https://doi.org/10.1038/s41467-023-37840-yopenalex-snapshot
Soluble pathogenic tau enters brain vascular endothelial cells and drives cellular senescence and brain microvascular dysfunction in a mouse model of tauopathy
inferredcites →https://doi.org/10.1038/s41586-021-03911-7openalex-snapshot
Structure-based classification of tauopathies
inferredcites →https://doi.org/10.1038/s41593-020-0687-6openalex-snapshot
Synergy between amyloid-β and tau in Alzheimer’s disease
inferredcites →https://doi.org/10.1038/s41596-018-0103-9openalex-snapshot
Pathway enrichment analysis and visualization of omics data using g:Profiler, GSEA, Cytoscape and EnrichmentMap
inferredcites →https://doi.org/10.1038/s41598-023-38000-4openalex-snapshot
Detection, visualization and quantification of protein complexes in human Alzheimer’s disease brains using proximity ligation assay
inferredcites →https://doi.org/10.1038/s42003-024-05855-wopenalex-snapshot
Quantity and quality of minichromosome maintenance protein complexes couple replication licensing to genome integrity
inferredcites →https://doi.org/10.1038/s42003-025-07499-wopenalex-snapshot
Brain-derived tau oligomer polymorphs: distinct aggregations, stability profiles, and biological activities
inferredcites →https://doi.org/10.1038/srep00700openalex-snapshot
Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau
inferredcites →https://doi.org/10.1038/srep09386openalex-snapshot
Module organization and variance in protein-protein interaction networks
inferredcites →https://doi.org/10.1073/pnas.1607215114openalex-snapshot
Cytosolic Fc receptor TRIM21 inhibits seeded tau aggregation
inferredcites →https://doi.org/10.1074/jbc.ra120.014630openalex-snapshot
Modulating disease-relevant tau oligomeric strains by small molecules
inferredcites →https://doi.org/10.1074/mcp.m113.031591openalex-snapshot
Accurate Proteome-wide Label-free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ
inferredcites →https://doi.org/10.1074/mcp.m115.049221openalex-snapshot
Systematic Determination of Human Cyclin Dependent Kinase (CDK)-9 Interactome Identifies Novel Functions in RNA Splicing Mediated by the DEAD Box (DDX)-5/17 RNA Helicases*
inferredcites →https://doi.org/10.1074/mcp.m116.060277openalex-snapshot
Defining the Protein-Protein Interaction Network of the Human Protein Tyrosine Phosphatase Family
inferredcites →https://doi.org/10.1093/brain/awab218openalex-snapshot
Dementia with Lewy bodies: association of Alzheimer pathology with functional connectivity networks
inferredcites →https://doi.org/10.1093/brain/awp099openalex-snapshot
Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease
inferredcites →https://doi.org/10.1093/braincomms/fcaa090openalex-snapshot
Differential cross-seeding properties of tau and α-synuclein in mouse models of tauopathy and synucleinopathy
inferredcites →https://doi.org/10.1093/braincomms/fcad356openalex-snapshot
Role of oxidative stress in neurodegenerative disorders: a review of reactive oxygen species and prevention by antioxidants
inferredcites →https://doi.org/10.1093/hmg/ddab363openalex-snapshot
Mitochondrial oxidative stress contributes to the pathological aggregation and accumulation of tau oligomers in Alzheimer’s disease
inferredcites →https://doi.org/10.1093/toxsci/kfp132openalex-snapshot
Potential Role of α-Synuclein and Metallothionein in Lead-Induced Inclusion Body Formation
inferredcites →https://doi.org/10.1097/00001756-200110290-00007openalex-snapshot
Paradoxical phosphorylation of the serine 199 on tau proteins from young individuals
inferredcites →https://doi.org/10.1097/nen.0000000000000018openalex-snapshot
Confluence of α-Synuclein, Tau, and β-Amyloid Pathologies in Dementia With Lewy Bodies
inferredcites →https://doi.org/10.1097/wco.0b013e32833be924openalex-snapshot
Neuropathology of variants of progressive supranuclear palsy
inferredcites →https://doi.org/10.1101/cshperspect.a005918openalex-snapshot
Protein Regulation in Signal Transduction
inferredcites →https://doi.org/10.1111/acel.14120openalex-snapshot
S100A8 ‐enriched microglia populate the brain of tau‐seeded and accelerated aging mice
inferredcites →https://doi.org/10.1111/j.1582-4934.2012.01604.xopenalex-snapshot
Neddylation dysfunction in Alzheimer's disease
inferredcites →https://doi.org/10.1111/jnc.15796openalex-snapshot
Identification of phosphorylated tau protein interactors in progressive supranuclear palsy ( PSP ) reveals networks involved in protein degradation, stress response, cytoskeletal dynamics, metabolic processes, and neurotransmission
inferredcites →https://doi.org/10.1111/jnc.15975openalex-snapshot
Site‐specific phosphorylation of tau impacts mitochondrial function and response to stressors
inferredcites →https://doi.org/10.1126/sciadv.aaw6404openalex-snapshot
Experimental evidence for the age dependence of tau protein spread in the brain
inferredcites →https://doi.org/10.1126/science.1195227openalex-snapshot
α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro
inferredcites →https://doi.org/10.1126/science.abn1366openalex-snapshot
Cytosolic antibody receptor TRIM21 is required for effective tau immunotherapy in mouse models
inferredcites →https://doi.org/10.1136/jnnp-2020-325549openalex-snapshot
Neuroinflammation predicts disease progression in progressive supranuclear palsy
inferredcites →https://doi.org/10.1146/annurev-pathmechdis-051222-120750openalex-snapshot
Neurodegenerative Disease Tauopathies
inferredcites →https://doi.org/10.1152/ajplung.00224.2016openalex-snapshot
BRD4 mediates NF-κB-dependent epithelial-mesenchymal transition and pulmonary fibrosis via transcriptional elongation
inferredcites →https://doi.org/10.1186/1750-1326-6-39openalex-snapshot
Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
inferredcites →https://doi.org/10.1186/s13024-021-00476-xopenalex-snapshot
Cellular and pathological heterogeneity of primary tauopathies
inferredcites →https://doi.org/10.1186/s13024-022-00572-6openalex-snapshot
Tau interactome and RNA binding proteins in neurodegenerative diseases
inferredcites →https://doi.org/10.1186/s40478-018-0557-6openalex-snapshot
Phosphorylation of different tau sites during progression of Alzheimer’s disease
inferredcites →https://doi.org/10.1186/s40478-018-0637-7openalex-snapshot
Different tau species lead to heterogeneous tau pathology propagation and misfolding
inferredcites →https://doi.org/10.1186/s40478-024-01786-zopenalex-snapshot
Neuroinflammation is associated with Alzheimer’s disease co-pathology in dementia with Lewy bodies
inferredcites →https://doi.org/10.1186/s40478-025-01930-3openalex-snapshot
Tau oligomers impair memory and synaptic plasticity through the cellular prion protein
inferredcites →https://doi.org/10.1523/eneuro.0503-22.2023openalex-snapshot
Characterization of the Tau Interactome in Human Brain Reveals Isoform-Dependent Interaction with 14-3-3 Family Proteins
inferredcites →https://doi.org/10.1523/jneurosci.08-08-02804.1988openalex-snapshot
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
inferredcites →https://doi.org/10.1523/jneurosci.1230-17.2017openalex-snapshot
Pathological Tau Strains from Human Brains Recapitulate the Diversity of Tauopathies in Nontransgenic Mouse Brain
inferredcites →https://doi.org/10.2478/s13380-012-0032-yopenalex-snapshot
Soluble forms of tau are toxic in Alzheimer’s disease
inferredcites →https://doi.org/10.3389/fcell.2021.774650openalex-snapshot
Synuclein Regulates Synaptic Vesicle Clustering and Docking at a Vertebrate Synapse
inferredcites →https://doi.org/10.3389/fncel.2020.00175openalex-snapshot
Truncated Tau Induces Mitochondrial Transport Failure Through the Impairment of TRAK2 Protein and Bioenergetics Decline in Neuronal Cells
inferredcites →https://doi.org/10.3389/fneur.2021.786353openalex-snapshot
Tau Ubiquitination in Alzheimer's Disease
inferredcites →https://doi.org/10.3389/fnins.2018.00163openalex-snapshot
The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease
inferredcites →https://doi.org/10.3389/fnins.2019.01258openalex-snapshot
Seeding Activity-Based Detection Uncovers the Different Release Mechanisms of Seed-Competent Tau Versus Inert Tau via Lysosomal Exocytosis
inferredcites →https://doi.org/10.3389/fphar.2021.685011openalex-snapshot
Post-Translational Modifications of Deubiquitinating Enzymes: Expanding the Ubiquitin Code
inferredcites →https://doi.org/10.3390/ijms19051360openalex-snapshot
Acetylation Disfavors Tau Phase Separation
inferredcites →https://doi.org/10.3390/ijms21176344openalex-snapshot
Insights into Disease-Associated Tau Impact on Mitochondria
inferredcites →https://doi.org/10.3390/ijms25094969openalex-snapshot
The Enigma of Tau Protein Aggregation: Mechanistic Insights and Future Challenges
inferredcites →https://doi.org/10.4172/2161-0460.1000444openalex-snapshot
The Contribution of Tau, Amyloid-Beta and Alpha-Synuclein Pathology to Dementia in Lewy Body Disorders
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