Research graph
References from Neuronal lipid composition regulates distinct states of full-length tau assembly, mechanics and membrane interactions. Local targets link to admitted publications; unresolved targets remain external evidence.
Tau pathology and neurodegeneration
10.1016/s1474-4422(13)70090-5 · 2013 · External reference
10.1038/nature23002
10.1038/nature23002 · External reference
10.1523/jneurosci.3542-15.2016
10.1523/jneurosci.3542-15.2016 · External reference
10.1074/jbc.m808759200
10.1074/jbc.m808759200 · External reference
10.1074/jbc.m112.346072
10.1074/jbc.m112.346072 · External reference
10.1073/pnas.1607215114
10.1073/pnas.1607215114 · External reference
10.1016/j.neuron.2014.04.047
10.1016/j.neuron.2014.04.047 · External reference
10.1038/ncb1901
10.1038/ncb1901 · External reference
10.1111/bpa.12044
10.1111/bpa.12044 · External reference
10.1084/jem.20160833
10.1084/jem.20160833 · External reference
10.1523/jneurosci.2642-12.2013
10.1523/jneurosci.2642-12.2013 · External reference
10.1021/bi800783d
10.1021/bi800783d · External reference
Tau aggregation is driven by a transition from random coil to beta sheet structure
2005 · External reference
10.1074/jbc.m301663200
10.1074/jbc.m301663200 · External reference
10.1021/bi201857v
10.1021/bi201857v · External reference
10.1074/jbc.m112.396176
10.1074/jbc.m112.396176 · External reference
Discovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes
10.1038/s41467-017-01575-4 · 2017 · External reference
10.1016/j.bpj.2014.07.046
10.1016/j.bpj.2014.07.046 · External reference
10.1016/j.jmb.2006.07.018
10.1016/j.jmb.2006.07.018 · External reference
10.1016/j.bpj.2009.11.052
10.1016/j.bpj.2009.11.052 · External reference
10.1126/science.1150057
10.1126/science.1150057 · External reference
The circularization of amyloid fibrils formed by apolipoprotein C-II
10.1016/s0006-3495(03)74812-7 · 2003 · External reference
10.2307/2291091
10.2307/2291091 · External reference
Tau N-terminal inserts regulate tau liquid-liquid phase separation and condensates maturation in a neuronal cell model
10.3390/ijms22189728 · 2021 · External reference
A fluorogenic far red-emitting molecular viscometer for ascertaining lysosomal stress in live cells and Caenorhabditis elegans
10.3389/fchem.2022.840297 · 2022 · External reference
10.1038/s41556-020-0546-4
10.1038/s41556-020-0546-4 · External reference
10.1016/bs.mie.2018.02.007
10.1016/bs.mie.2018.02.007 · External reference
10.1021/jacsau.5c01563
10.1021/jacsau.5c01563 · External reference
Interaction of full-length Tau with negatively charged lipid membranes leads to polymorphic aggregates
10.1039/d4nr01343c · 2024 · External reference
10.1016/j.bpj.2010.03.013
10.1016/j.bpj.2010.03.013 · External reference
Reversible cation-selective attachment and self-assembly of human tau on supported brain lipid membranes
10.1021/acs.nanolett.8b01085 · 2018 · External reference
Under heparin-free conditions unsaturated phospholipids inhibit the aggregation of 1N4R and 2N4R Tau
10.1021/acs.jpclett.4c01718 · 2024 · External reference
Identification of lipid heterogeneity and diversity in the developing human brain
10.1021/jacsau.1c00393 · 2021 · External reference
Imaging mass spectrometry (IMS) of cortical lipids from preclinical to severe stages of Alzheimer’s disease
10.1016/j.bbamem.2017.05.009 · 2017 · External reference
10.7554/elife.43584
10.7554/elife.43584 · External reference
Sub-persistence-length complex scaling behavior in lysozyme amyloid fibrils
10.1103/physrevlett.107.238101 · 2011 · External reference
10.1038/s41591-020-0938-9
10.1038/s41591-020-0938-9 · External reference
Local organization of biological membranes modulates Tau–lipid interactions and fibril formation
10.1021/jacsau.6c00374 · 2026 · External reference
Membrane-induced tau amyloid fibrils
10.1038/s42003-023-04847-6 · 2023 · External reference
10.1016/j.bpj.2016.10.016
10.1016/j.bpj.2016.10.016 · External reference
10.1016/j.jbc.2023.104653
10.1016/j.jbc.2023.104653 · External reference
Membrane interfacial potential governs surface condensation and fibrillation of α-Synuclein in neurons
10.1038/s41467-026-70840-2 · 2026 · External reference
Neuronal constitutive endolysosomal perforations enable α-synuclein aggregation by internalized PFFs
2024 · External reference
Tau protein liquid–liquid phase separation can initiate tau aggregation
10.15252/embj.201798049 · 2018 · External reference
10.1073/pnas.2315690121
10.1073/pnas.2315690121 · External reference
10.1007/s00401-020-02254-3
10.1007/s00401-020-02254-3 · External reference
Giant plasma membrane vesicles to study plasma membrane structure and dynamics
10.1016/j.bbamem.2021.183857 · 2022 · External reference
10.1093/brain/awaa376
10.1093/brain/awaa376 · External reference
The release and trans-synaptic transmission of Tau via exosomes
10.1186/s13024-016-0143-y · 2017 · External reference
10.1074/jbc.m115.709485
10.1074/jbc.m115.709485 · External reference
10.1038/nn.4132
10.1038/nn.4132 · External reference
Plasma tau biomarkers for biological staging of Alzheimer’s disease
10.1038/s43587-025-00951-w · 2025 · External reference
Amyloid proteins: methods and protocols
2004 · External reference
In vitro assay for studying the aggregation of tau protein and drug screening
2018 · External reference
10.1006/jmbi.1996.0687
10.1006/jmbi.1996.0687 · External reference
10.1007/bf01025868
10.1007/bf01025868 · External reference
10.1016/j.bpj.2013.05.024
10.1016/j.bpj.2013.05.024 · External reference
Phagocytosis of full-length Tau oligomers by Actin-remodeling of activated microglia
10.1186/s12974-019-1694-y · 2020 · External reference
Microglia degrade Tau oligomers deposit via purinergic P2Y12-associated podosome and filopodia formation and induce chemotaxis
10.1186/s13578-023-01028-0 · 2023 · External reference
α-Linolenic acid induces clearance of Tau seeds via Actin-remodeling in Microglia
10.1186/s43556-021-00028-1 · 2021 · External reference
10.1111/tra.12784
10.1111/tra.12784 · External reference
10.1083/jcb.85.3.890
10.1083/jcb.85.3.890 · External reference
l-Lactate mediates neuroprotection against ischaemia by increasing TREK 1 channel expression in rat hippocampal astrocytes in vitro
10.1111/jnc.13638 · 2016 · External reference
10.1006/jmbi.1996.0687
10.1006/jmbi.1996.0687 · ExternalCitation · doi-reference
10.1007/bf01025868
10.1007/bf01025868 · ExternalCitation · doi-reference
10.1007/s00401-020-02254-3
10.1007/s00401-020-02254-3 · ExternalCitation · doi-reference
10.1016/bs.mie.2018.02.007
10.1016/bs.mie.2018.02.007 · ExternalCitation · doi-reference
Imaging mass spectrometry (IMS) of cortical lipids from preclinical to severe stages of Alzheimer’s disease
10.1016/j.bbamem.2017.05.009 · ExternalCitation · doi-reference
Giant plasma membrane vesicles to study plasma membrane structure and dynamics
10.1016/j.bbamem.2021.183857 · ExternalCitation · doi-reference
10.1016/j.bpj.2009.11.052
10.1016/j.bpj.2009.11.052 · ExternalCitation · doi-reference
10.1016/j.bpj.2010.03.013
10.1016/j.bpj.2010.03.013 · ExternalCitation · doi-reference
10.1016/j.bpj.2013.05.024
10.1016/j.bpj.2013.05.024 · ExternalCitation · doi-reference
10.1016/j.bpj.2014.07.046
10.1016/j.bpj.2014.07.046 · ExternalCitation · doi-reference
10.1016/j.bpj.2016.10.016
10.1016/j.bpj.2016.10.016 · ExternalCitation · doi-reference
10.1016/j.jbc.2023.104653
10.1016/j.jbc.2023.104653 · ExternalCitation · doi-reference
10.1016/j.jmb.2006.07.018
10.1016/j.jmb.2006.07.018 · ExternalCitation · doi-reference
10.1016/j.neuron.2014.04.047
10.1016/j.neuron.2014.04.047 · ExternalCitation · doi-reference
The circularization of amyloid fibrils formed by apolipoprotein C-II
10.1016/s0006-3495(03)74812-7 · ExternalCitation · doi-reference
Tau pathology and neurodegeneration
10.1016/s1474-4422(13)70090-5 · ExternalCitation · doi-reference
Under heparin-free conditions unsaturated phospholipids inhibit the aggregation of 1N4R and 2N4R Tau
10.1021/acs.jpclett.4c01718 · ExternalCitation · doi-reference
Reversible cation-selective attachment and self-assembly of human tau on supported brain lipid membranes
10.1021/acs.nanolett.8b01085 · ExternalCitation · doi-reference
10.1021/bi201857v
10.1021/bi201857v · ExternalCitation · doi-reference
10.1021/bi800783d
10.1021/bi800783d · ExternalCitation · doi-reference
Identification of lipid heterogeneity and diversity in the developing human brain
10.1021/jacsau.1c00393 · ExternalCitation · doi-reference
10.1021/jacsau.5c01563
10.1021/jacsau.5c01563 · ExternalCitation · doi-reference
Local organization of biological membranes modulates Tau–lipid interactions and fibril formation
10.1021/jacsau.6c00374 · ExternalCitation · doi-reference
10.1038/nature23002
10.1038/nature23002 · ExternalCitation · doi-reference
10.1038/ncb1901
10.1038/ncb1901 · ExternalCitation · doi-reference
10.1038/nn.4132
10.1038/nn.4132 · ExternalCitation · doi-reference
Discovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes
10.1038/s41467-017-01575-4 · ExternalCitation · doi-reference
Membrane interfacial potential governs surface condensation and fibrillation of α-Synuclein in neurons
10.1038/s41467-026-70840-2 · ExternalCitation · doi-reference
10.1038/s41556-020-0546-4
10.1038/s41556-020-0546-4 · ExternalCitation · doi-reference
10.1038/s41591-020-0938-9
10.1038/s41591-020-0938-9 · ExternalCitation · doi-reference
Membrane-induced tau amyloid fibrils
10.1038/s42003-023-04847-6 · ExternalCitation · doi-reference
Plasma tau biomarkers for biological staging of Alzheimer’s disease
10.1038/s43587-025-00951-w · ExternalCitation · doi-reference
Interaction of full-length Tau with negatively charged lipid membranes leads to polymorphic aggregates
10.1039/d4nr01343c · ExternalCitation · doi-reference
10.1073/pnas.1607215114
10.1073/pnas.1607215114 · ExternalCitation · doi-reference
10.1073/pnas.2315690121
10.1073/pnas.2315690121 · ExternalCitation · doi-reference
10.1074/jbc.m112.346072
10.1074/jbc.m112.346072 · ExternalCitation · doi-reference
10.1074/jbc.m112.396176
10.1074/jbc.m112.396176 · ExternalCitation · doi-reference
10.1074/jbc.m115.709485
10.1074/jbc.m115.709485 · ExternalCitation · doi-reference
10.1074/jbc.m301663200
10.1074/jbc.m301663200 · ExternalCitation · doi-reference
10.1074/jbc.m808759200
10.1074/jbc.m808759200 · ExternalCitation · doi-reference
10.1083/jcb.85.3.890
10.1083/jcb.85.3.890 · ExternalCitation · doi-reference
10.1084/jem.20160833
10.1084/jem.20160833 · ExternalCitation · doi-reference
10.1093/brain/awaa376
10.1093/brain/awaa376 · ExternalCitation · doi-reference
Sub-persistence-length complex scaling behavior in lysozyme amyloid fibrils
10.1103/physrevlett.107.238101 · ExternalCitation · doi-reference
10.1111/bpa.12044
10.1111/bpa.12044 · ExternalCitation · doi-reference
l-Lactate mediates neuroprotection against ischaemia by increasing TREK 1 channel expression in rat hippocampal astrocytes in vitro
10.1111/jnc.13638 · ExternalCitation · doi-reference
10.1111/tra.12784
10.1111/tra.12784 · ExternalCitation · doi-reference
10.1126/science.1150057
10.1126/science.1150057 · ExternalCitation · doi-reference
Phagocytosis of full-length Tau oligomers by Actin-remodeling of activated microglia
10.1186/s12974-019-1694-y · ExternalCitation · doi-reference
The release and trans-synaptic transmission of Tau via exosomes
10.1186/s13024-016-0143-y · ExternalCitation · doi-reference
Microglia degrade Tau oligomers deposit via purinergic P2Y12-associated podosome and filopodia formation and induce chemotaxis
10.1186/s13578-023-01028-0 · ExternalCitation · doi-reference
α-Linolenic acid induces clearance of Tau seeds via Actin-remodeling in Microglia
10.1186/s43556-021-00028-1 · ExternalCitation · doi-reference
10.1523/jneurosci.2642-12.2013
10.1523/jneurosci.2642-12.2013 · ExternalCitation · doi-reference
10.1523/jneurosci.3542-15.2016
10.1523/jneurosci.3542-15.2016 · ExternalCitation · doi-reference
Tau protein liquid–liquid phase separation can initiate tau aggregation
10.15252/embj.201798049 · ExternalCitation · doi-reference
10.2307/2291091
10.2307/2291091 · ExternalCitation · doi-reference
A fluorogenic far red-emitting molecular viscometer for ascertaining lysosomal stress in live cells and Caenorhabditis elegans
10.3389/fchem.2022.840297 · ExternalCitation · doi-reference
Tau N-terminal inserts regulate tau liquid-liquid phase separation and condensates maturation in a neuronal cell model
10.3390/ijms22189728 · ExternalCitation · doi-reference
10.7554/elife.43584
10.7554/elife.43584 · ExternalCitation · doi-reference
