CoChat
Sign Up
Cited by 90

The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.

Human iPSC 4R tauopathy model uncovers modifiers of tau propagation

Parra Bravo, Celeste, Giani, Alice Maria, Madero-Perez, Jesus, Zhao, Zeping, Wan, Yuansong, Samelson, Avi J., Wong, Man Ying, Evangelisti, Alessandro, Cordes, Ethan, Fan, Li, Ye, Pearly, Zhu, Daphne, Pozner, Tatyana, Mercedes, Maria, Patel, Tark, Yarahmady, Allan, Carling, Gillian K., Sterky, Fredrik H., Lee, Virginia M.Y., Lee, Edward B., DeTure, Michael, Dickson, Dennis W., Sharma, Manu, Mok, Sue-Ann, Luo, Wenjie, Zhao, Mingrui, Kampmann, Martin, Gong, Shiaoching, Gan, Li·2024·Cell
DOI 10.1016/j.cell.2024.03.015PMC PMC11365117
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.cell.2024.03.015

Cites

13 of 13 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Our findings are consistent with reduced neuronal activity in tau transgenic mice and the negative correlation of tauopathy measured by PET tau tracer with neuronal activity measured with FDG PET.

    “Our findings are also consistent with reduced neuronal activity in tau transgenic mice53 and the negative correlation of tauopathy measured by PET tau tracer with neuronal activity measured with FDG PET87.”

    From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [53]

  • Modeling 4R tauopathy in human neurons and astrocytes has been implemented, providing a unique platform to investigate the molecular and cellular mechanisms underlying the development and progression of tau pathology with both 3R- and 4R-tau isoforms as seen in FTLD and AD patients.

    “Recently, modeling 4 R tauopathy in human neurons53,83,110,111 and astrocytes110 has been implemented, which provides a unique platform to investigate the molecular and cellular mechanisms underlying the development and progression of tau pathology with both 3R- and 4R-tau isoforms as seen in FTLD and AD patients.”

    From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [53]

  • The lack of 4 R isoforms of tau is a common disadvantage of most current culture methods of HNOs, which requires validation of findings in HNOs with both 4 R and 3 R tau, tau mouse models, or human postmortem brain tissue with tau pathology.

    “The lack of 4 R isoforms of tau is a common disadvantage of most current culture methods of HNOs5, which requires the validation of findings in HNOs with both 4 R and 3 R tau, tau mouse models, or human postmortem brain tissue with tau pathology52,53.”

    From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [53]

  • This is consistent with previous reports of decreased neuronal activity in tau mouse models and in vitro models with tau pathology.

    “This is consistent with previous reports of decreased neuronal activity in tau mouse models and in vitro models with tau pathology53,54.”

    From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [53]

  • Our findings coincide with previous literature suggesting tau models can exhibit downregulation of neuronal activity.

    “Our findings coincide with previous literature suggesting tau models can exhibit downregulation of neuronal activity53,54.”

    From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [53]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 78

  1. Götz, 2019, Molecular Pathogenesis of the Tauopathies, Annu. Rev. Pathol., 14, 239, 10.1146/annurev-pathmechdis-012418-012936 · DOI · Paper page
  2. Goedert, 1989, Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease, Neuron, 3, 519, 10.1016/0896-6273(89)90210-9 · DOI · Paper page
  3. Shi, 2021, Structure-based classification of tauopathies, Nature, 598, 359, 10.1038/s41586-021-03911-7 · DOI · Paper page
  4. Spillantini, 1998, Mutation in the tau gene in familial multiple system tauopathy with presenile dementia, Proc. Natl. Acad. Sci. USA., 95, 7737, 10.1073/pnas.95.13.7737 · DOI · Paper page
  5. Mirra, 1999, Tau pathology in a family with dementia and a P301L mutation in tau, J. Neuropathol. Exp. Neurol., 58, 335, 10.1097/00005072-199904000-00004 · DOI · Paper page
  6. Paonessa, 2019, Microtubules Deform the Nuclear Membrane and Disrupt Nucleocytoplasmic Transport in Tau-Mediated Frontotemporal Dementia, Cell Rep., 26, 582, 10.1016/j.celrep.2018.12.085 · DOI
  7. Sposito, 2015, Developmental regulation of tau splicing is disrupted in stem cell-derived neurons from frontotemporal dementia patients with the 10 + 16 splice-site mutation in MAPT, Hum. Mol. Genet., 24, 5260, 10.1093/hmg/ddv246 · DOI · Paper page
  8. Wang, 2017, Scalable Production of iPSC-Derived Human Neurons to Identify Tau-Lowering Compounds by High-Content Screening, Stem Cell Rep., 9, 1221, 10.1016/j.stemcr.2017.08.019 · DOI · Paper page
  9. Liu, 2008, Tau exon 10 alternative splicing and tauopathies, Mol. Neurodegener., 3, 8, 10.1186/1750-1326-3-8 · DOI · Paper page
  10. Yasuda, 2005, Phenotypic heterogeneity within a new family with the MAPT p301s mutation, Ann. Neurol., 58, 920, 10.1002/ana.20668 · DOI
  11. Allen, 2002, Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein, J. Neurosci., 22, 9340, 10.1523/JNEUROSCI.22-21-09340.2002 · DOI
  12. Berriman, 2003, Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure, Proc. Natl. Acad. Sci. USA., 100, 9034, 10.1073/pnas.1530287100 · DOI
  13. Jicha, 1997, Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau, J. Neurosci. Res., 48, 128, 10.1002/(SICI)1097-4547(19970415)48:2<128::AID-JNR5>3.0.CO;2-E · DOI
  14. Gustke, 1994, Domains of tau Protein and Interactions with Microtubules, Biochemistry, 33, 9511, 10.1021/bi00198a017 · DOI · Paper page
  15. Hariri, 2000, Biogenesis of multilamellar bodies via autophagy, Mol. Biol. Cell, 11, 255, 10.1091/mbc.11.1.255 · DOI
  16. Xie, 2022, Lysosomal exocytosis releases pathogenic alpha-synuclein species from neurons in synucleinopathy models, Nat. Commun., 13, 4918, 10.1038/s41467-022-32625-1 · DOI
  17. Arantes, 2006, A role for synaptotagmin VII-regulated exocytosis of lysosomes in neurite outgrowth from primary sympathetic neurons, J. Neurosci., 26, 4630, 10.1523/JNEUROSCI.0009-06.2006 · DOI
  18. Tracy, 2022, Tau interactome maps synaptic and mitochondrial processes associated with neurodegeneration, Cell, 185, 712, 10.1016/j.cell.2021.12.041 · DOI
  19. Bejanin, 2017, Tau pathology and neurodegeneration contribute to cognitive impairment in Alzheimer's disease, Brain, 140, 3286, 10.1093/brain/awx243 · DOI · Paper page
  20. Ossenkoppele, 2022, Amyloid and tau PET-positive cognitively unimpaired individuals are at high risk for future cognitive decline, Nat. Med., 28, 2381, 10.1038/s41591-022-02049-x · DOI · Paper page
  21. Grimm, 2015, A general method to improve fluorophores for live-cell and single-molecule microscopy, Nat. Methods, 12, 244, 10.1038/nmeth.3256 · DOI
  22. Zhang, 2023, Fast and sensitive GCaMP calcium indicators for imaging neural populations, Nature, 615, 884, 10.1038/s41586-023-05828-9 · DOI
  23. Wu, 2016, Neuronal activity enhances tau propagation and tau pathology in vivo, Nat. Neurosci., 19, 1085, 10.1038/nn.4328 · DOI · Paper page
  24. Yamada, 2014, Neuronal activity regulates extracellular tau in vivo, J. Exp. Med., 211, 387, 10.1084/jem.20131685 · DOI
  25. Pooler, 2013, Physiological release of endogenous tau is stimulated by neuronal activity, EMBO Rep., 14, 389, 10.1038/embor.2013.15 · DOI · Paper page
  26. Zhu, 2014, Silencing synapses with DREADDs, Neuron, 82, 723, 10.1016/j.neuron.2014.05.002 · DOI
  27. Tian, 2021, Genome-wide CRISPRi/a screens in human neurons link lysosomal failure to ferroptosis, Nat. Neurosci., 24, 1020, 10.1038/s41593-021-00862-0 · DOI · Paper page
  28. Samelson, 2023, CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis, bioRxiv
  29. Liang, 2020, A Genome-wide ER-phagy Screen Highlights Key Roles of Mitochondrial Metabolism and ER-Resident UFMylation, Cell, 180, 1160, 10.1016/j.cell.2020.02.017 · DOI
  30. Eldeeb, 2021, Fine-tuning ER-phagy by post-translational modifications, Bioessays, 43, 10.1002/bies.202000212 · DOI
  31. Sumya, 2023, Acute COG complex inactivation unveiled its immediate impact on Golgi and illuminated the nature of intra-Golgi recycling vesicles, Traffic, 24, 52, 10.1111/tra.12876 · DOI
  32. Chen, 2020, Promoting tau secretion and propagation by hyperactive p300/CBP via autophagy-lysosomal pathway in tauopathy, Mol. Neurodegener., 15, 2, 10.1186/s13024-019-0354-0 · DOI · Paper page
  33. Iba, 2013, Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy, J. Neurosci., 33, 1024, 10.1523/JNEUROSCI.2642-12.2013 · DOI · Paper page
  34. Manos, 2022, Uncovering specificity of endogenous TAU aggregation in a human iPSC-neuron TAU seeding model, iScience, 25, 10.1016/j.isci.2021.103658 · DOI · Paper page
  35. Pérez, 1996, Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction, J. Neurochem., 67, 1183, 10.1046/j.1471-4159.1996.67031183.x · DOI
  36. von Bergen, 2000, Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure, Proc. Natl. Acad. Sci. USA., 97, 5129, 10.1073/pnas.97.10.5129 · DOI · Paper page
  37. Vogel, 2020, Spread of pathological tau proteins through communicating neurons in human Alzheimer's disease, Nat. Commun., 11, 2612, 10.1038/s41467-020-15701-2 · DOI
  38. Franzmeier, 2022, Tau deposition patterns are associated with functional connectivity in primary tauopathies, Nat. Commun., 13, 1362, 10.1038/s41467-022-28896-3 · DOI
  39. García-Cabrero, 2013, Hyperexcitability and epileptic seizures in a model of frontotemporal dementia, Neurobiol. Dis., 58, 200, 10.1016/j.nbd.2013.06.005 · DOI
  40. Sperfeld, 1999, FTDP-17: an early-onset phenotype with parkinsonism and epileptic seizures caused by a novel mutation, Ann. Neurol., 46, 708, 10.1002/1531-8249(199911)46:5<708::AID-ANA5>3.0.CO;2-K · DOI
  41. Gendron, 2009, The role of tau in neurodegeneration, Mol. Neurodegener., 4, 13, 10.1186/1750-1326-4-13 · DOI · Paper page
  42. Spires-Jones, 2009, Tau pathophysiology in neurodegeneration: a tangled issue, Trends Neurosci., 32, 150, 10.1016/j.tins.2008.11.007 · DOI
  43. Zhang, 2021, PET imaging of neural activity, beta-amyloid, and tau in normal brain aging, Eur. J. Nucl. Med. Mol. Imaging, 48, 3859, 10.1007/s00259-021-05230-5 · DOI · Paper page
  44. Busche, 2019, Tau impairs neural circuits, dominating amyloid-beta effects, in Alzheimer models in vivo, Nat. Neurosci., 22, 57, 10.1038/s41593-018-0289-8 · DOI · Paper page
  45. Decker, 2016, The Tau/A152T mutation, a risk factor for frontotemporal-spectrum disorders, leads to NR2B receptor-mediated excitotoxicity, EMBO Rep., 17, 552, 10.15252/embr.201541439 · DOI
  46. Maeda, 2016, Expression of A152T human tau causes age-dependent neuronal dysfunction and loss in transgenic mice, EMBO Rep., 17, 530, 10.15252/embr.201541438 · DOI
  47. Carosi, 2021, Retromer dysfunction at the nexus of tauopathies, Cell Death Differ., 28, 884, 10.1038/s41418-020-00727-2 · DOI · Paper page
  48. Ye, 2020, Retromer subunit, VPS29, regulates synaptic transmission and is required for endolysosomal function in the aging brain, Elife, 9, 10.7554/eLife.51977 · DOI · Paper page
  49. Baños-Mateos, 2019, VPS29, a tweak tool of endosomal recycling, Curr. Opin. Cell Biol., 59, 81, 10.1016/j.ceb.2019.03.010 · DOI
  50. Williams, 2017, VPS35, the Retromer Complex and Parkinson's Disease, J. Parkinsons Dis., 7, 219, 10.3233/JPD-161020 · DOI
  51. Small, 2005, Model-guided microarray implicates the retromer complex in Alzheimer's disease, Ann. Neurol., 58, 909, 10.1002/ana.20667 · DOI · Paper page
  52. Llamas-Rodríguez, 2022, Entorhinal Subfield Vulnerability to Neurofibrillary Tangles in Aging and the Preclinical Stage of Alzheimer's Disease, J. Alzheimers Dis., 87, 1379, 10.3233/JAD-215567 · DOI
  53. Asadzadeh, 2022, Retromer deficiency in Tauopathy models enhances the truncation and toxicity of Tau, Nat. Commun., 13, 5049, 10.1038/s41467-022-32683-5 · DOI · Paper page
  54. Chen, 2019, Parkinson's disease-linked D620N VPS35 knockin mice manifest tau neuropathology and dopaminergic neurodegeneration, Proc. Natl. Acad. Sci. USA., 116, 5765, 10.1073/pnas.1814909116 · DOI
  55. Simoes, 2020, Tau and other proteins found in Alzheimer's disease spinal fluid are linked to retromer-mediated endosomal traffic in mice and humans, Sci. Transl. Med., 12, 10.1126/scitranslmed.aba6334 · DOI · Paper page
  56. Gerakis, 2019, The UFMylation System in Proteostasis and Beyond, Trends Cell Biol., 29, 974, 10.1016/j.tcb.2019.09.005 · DOI
  57. Nahorski, 2018, Biallelic UFM1 and UFC1 mutations expand the essential role of ufmylation in brain development, Brain, 141, 1934, 10.1093/brain/awy135 · DOI
  58. Walczak, 2019, Ribosomal protein RPL26 is the principal target of UFMylation, Proc. Natl. Acad. Sci. USA., 116, 1299, 10.1073/pnas.1816202116 · DOI
  59. Wang, 2023, SAYSD1 senses UFMylated ribosome to safeguard co-translational protein translocation at the endoplasmic reticulum, Cell Rep., 42
  60. Bindea, 2009, ClueGO: a Cytoscape plug-in to decipher functionally grouped gene ontology and pathway annotation networks, Bioinformatics, 25, 1091, 10.1093/bioinformatics/btp101 · DOI · Paper page
  61. Shannon, 2003, Cytoscape: a software environment for integrated models of biomolecular interaction networks, Genome Res., 13, 2498, 10.1101/gr.1239303 · DOI · Paper page
  62. Langmead, 2009, Ultrafast and memory-efficient alignment of short DNA sequences to the human genome, Genome Biol., 10, R25, 10.1186/gb-2009-10-3-r25 · DOI · Paper page
  63. Miyaoka, 2014, Isolation of single-base genome-edited human iPS cells without antibiotic selection, Nat. Methods, 11, 291, 10.1038/nmeth.2840 · DOI
  64. Mok, 2018, Mapping interactions with the chaperone network reveals factors that protect against tau aggregation, Nat. Struct. Mol. Biol., 25, 384, 10.1038/s41594-018-0057-1 · DOI
  65. Martin, 2011, Cutadapt Removes Adapter Sequences From High-Throughput Sequencing Reads, EMBnet. j., 17, 10, 10.14806/ej.17.1.200 · DOI · Paper page
  66. Dobin, 2013, STAR: ultrafast universal RNA-seq aligner, Bioinformatics, 29, 15, 10.1093/bioinformatics/bts635 · DOI · Paper page
  67. Trapnell, 2010, Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation, Nat. Biotechnol., 28, 511, 10.1038/nbt.1621 · DOI · Paper page
  68. Anders, 2015, HTSeq--a Python framework to work with high-throughput sequencing data, Bioinformatics, 31, 166, 10.1093/bioinformatics/btu638 · DOI · Paper page
  69. Love, 2014, Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2, Genome Biol., 15, 550, 10.1186/s13059-014-0550-8 · DOI · Paper page
  70. Jerber, 2021, Population-scale single-cell RNA-seq profiling across dopaminergic neuron differentiation, Nat. Genet., 53, 304, 10.1038/s41588-021-00801-6 · DOI
  71. Ito, 1968, Formaldehyde-Glutaraldehyde Fixatives Containing Trinitro Compounds, JCB (J. Cell Biol.), 39, 168A
  72. Venable, 1965, A Simplified Lead Citrate Stain for Use in Electron Microscopy, J. Cell Biol., 25, 407, 10.1083/jcb.25.2.407 · DOI
  73. Horlbeck, 2016, Compact and highly active next-generation libraries for CRISPR-mediated gene repression and activation, Elife, 5, 10.7554/eLife.19760 · DOI · Paper page
  74. Kampmann, 2014, Functional genomics platform for pooled screening and generation of mammalian genetic interaction maps, Nat. Protoc., 9, 1825, 10.1038/nprot.2014.103 · DOI
  75. Shen, 2022, GeneOverlap: Test and visualize gene overlaps, R package version, 1.34.0
  76. Tippani, 2022, CaPTure: Calcium PeakToolbox for analysis of in vitro calcium imaging data, BMC Neurosci., 23, 71, 10.1186/s12868-022-00751-7 · DOI
  77. Jia, 2011, In vivo two-photon imaging of sensory-evoked dendritic calcium signals in cortical neurons, Nat. Protoc., 6, 28, 10.1038/nprot.2010.169 · DOI
  78. Sun, 2021, A simple Ca2+-imaging approach to neural network analyses in cultured neurons, J. Neurosci. Methods, 349, 10.1016/j.jneumeth.2020.109041 · DOI

Cited by

Sorted by citations

Metadata

Authors
Parra Bravo, C., Giani, A. M., Madero-Perez, J., Zhao, Z., Wan, Y., Samelson, A. J., Wong, M. Y., Evangelisti, A., Cordes, E., Fan, L., Ye, P., Zhu, D., Pozner, T., Mercedes, M., Patel, T., Yarahmady, A., Carling, G. K., Sterky, F. H., Lee, V. M. Y., Lee, E. B., DeTure, M., Dickson, D. W., Sharma, M., Mok, S.-A., Luo, W., Zhao, M., Kampmann, M., Gong, S., & Gan, L.
ORCID
Gan, Li
Venue
Cell
Publisher
Elsevier BV
Published
2024-05
Volume
187
Issue
10
Pages
2446-2464.e22
ISSN
0092-8674
DOI
10.1016/j.cell.2024.03.015
PMC
PMC11365117
Cited by
90
References
13
Language
en
Licence
Funders
  • National Institutes of Health (R01AG072758, U54NS100717, R25GM130494, R01AG054214, R01AG074541, R01AG064239, P30AG072979)
  • Tau Consortium
  • JPB Foundation
  • Fondation Brain Canada

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review