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The ER-Mitochondria Tethering Complex VAPB-PTPIP51 Regulates Autophagy

Current biology, 2017-02, Vol.27 (3), p.371-385

2017

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Tau phosphorylation: the therapeutic challenge for neurodegenerative disease

Trends in molecular medicine, 2009-03, Vol.15 (3), p.112-119

2009

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Physiological release of endogenous tau is stimulated by neuronal activity

EMBO reports, 2013-04, Vol.14 (4), p.389-394

2013

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A role for tau at the synapse in Alzheimer's disease pathogenesis

Neuropharmacology, 2014-01, Vol.76, p.1-8

2014

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The importance of tau phosphorylation for neurodegenerative diseases

Frontiers in neurology, 2013-01, Vol.4, p.83-83

2013

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Roles of tau protein in health and disease

Acta Neuropathologica, 2017-05, Vol.133 (5), p.665-704

2017

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Tau phosphorylation affects its axonal transport and degradation

Neurobiology of aging, 2013-09, Vol.34 (9), p.2146-2157

2013

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Tau cleavage and tau aggregation in neurodegenerative disease

Biochemical Society transactions, 2010-08, Vol.38 (4), p.1016-1020

2010

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Astrocytes and neuroinflammation in Alzheimer's disease

Biochemical Society transactions, 2014-10, Vol.42 (5), p.1321-1325

2014

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Novel Phosphorylation Sites in Tau from Alzheimer Brain Support a Role for Casein Kinase 1 in Disease Pathogenesis

The Journal of biological chemistry, 2007-08, Vol.282 (32), p.23645-23654

2007

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Inhibition of glycogen synthase kinase-3 by BTA-EG4 reduces tau abnormalities in an organotypic brain slice culture model of Alzheimer’s disease

Scientific reports, 2017-08, Vol.7 (1), p.1-11, Article 7434

2017

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Functional Implications of Glycogen Synthase Kinase-3-Mediated Tau Phosphorylation

International journal of alzheimer's disease, 2011, Vol.2011 (2011), p.1-11

2011

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Reduced number of axonal mitochondria and tau hypophosphorylation in mouse P301L tau knockin neurons

Neurobiology of disease, 2016-01, Vol.85, p.1-10

2016

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Editorial: Tau Propagation Mechanisms: Cell Models, Animal Models, and Beyond

Frontiers in neuroscience, 2020-05, Vol.14, p.456-456

2020

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Age-dependent axonal transport and locomotor changes and tau hypophosphorylation in a “P301L” tau knockin mouse

Neurobiology of aging, 2012-03, Vol.33 (3), p.621.e1-621.e15

2012

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Functional implications of the association of tau with the plasma membrane

Biochemical Society transactions, 2010-08, Vol.38 (4), p.1012-1015

2010

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Trimming away tau in neurodegeneration

Science (American Association for the Advancement of Science), 2023-07, Vol.381 (6656), p.377-378

2023

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Mediators of tau phosphorylation in the pathogenesis of Alzheimer's disease

Expert review of neurotherapeutics, 2009-11, Vol.9 (11), p.1647-1666

2009

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Direct analysis of tau from PSP brain identifies new phosphorylation sites and a major fragment of N-terminally cleaved tau containing four microtubule-binding repeats

Journal of neurochemistry, 2008-06, Vol.105 (6), p.2343-2352

2008

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A new TAO kinase inhibitor reduces tau phosphorylation at sites associated with neurodegeneration in human tauopathies

Acta neuropathologica communications, 2018-05, Vol.6 (1), p.37-37, Article 37

2018

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A pathogenic tau fragment compromises microtubules, disrupts insulin signaling and induces the unfolded protein response

Acta neuropathologica communications, 2019-01, Vol.7 (1), p.2-2, Article 2

2019

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α-Synuclein binds to the ER–mitochondria tethering protein VAPB to disrupt Ca2+ homeostasis and mitochondrial ATP production

Acta neuropathologica, 2017-07, Vol.134 (1), p.129-149

2017

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Intracellular and Extracellular Roles for Tau in Neurodegenerative Disease

Journal of Alzheimer's disease, 2014-05, Vol.40 (s1), p.S37-S45

2014

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Mislocalization of neuronal tau in the absence of tangle pathology in phosphomutant tau knockin mice

Neurobiology of aging, 2016-03, Vol.39, p.1-18

2016

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Corrigendum: The disease associated Tau35 fragment has an increased propensity to aggregate compared to full-length tau

Frontiers in molecular biosciences, 2023-09, Vol.10, p.1276677-1276677

2023

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The ER-Mitochondria Tethering Complex VAPB-PTPIP51 Regulates Autophagy

Tau phosphorylation: the therapeutic challenge for neurodegenerative disease

Physiological release of endogenous tau is stimulated by neuronal activity

A role for tau at the synapse in Alzheimer's disease pathogenesis

The importance of tau phosphorylation for neurodegenerative diseases

Roles of tau protein in health and disease

Tau phosphorylation affects its axonal transport and degradation

Tau cleavage and tau aggregation in neurodegenerative disease

Astrocytes and neuroinflammation in Alzheimer's disease

Novel Phosphorylation Sites in Tau from Alzheimer Brain Support a Role for Casein Kinase 1 in Disease Pathogenesis

Inhibition of glycogen synthase kinase-3 by BTA-EG4 reduces tau abnormalities in an organotypic brain slice culture model of Alzheimer’s disease

Functional Implications of Glycogen Synthase Kinase-3-Mediated Tau Phosphorylation

Reduced number of axonal mitochondria and tau hypophosphorylation in mouse P301L tau knockin neurons

Editorial: Tau Propagation Mechanisms: Cell Models, Animal Models, and Beyond

Age-dependent axonal transport and locomotor changes and tau hypophosphorylation in a “P301L” tau knockin mouse

Functional implications of the association of tau with the plasma membrane

Trimming away tau in neurodegeneration

Mediators of tau phosphorylation in the pathogenesis of Alzheimer's disease

Direct analysis of tau from PSP brain identifies new phosphorylation sites and a major fragment of N-terminally cleaved tau containing four microtubule-binding repeats

A new TAO kinase inhibitor reduces tau phosphorylation at sites associated with neurodegeneration in human tauopathies

A pathogenic tau fragment compromises microtubules, disrupts insulin signaling and induces the unfolded protein response

α-Synuclein binds to the ER–mitochondria tethering protein VAPB to disrupt Ca2+ homeostasis and mitochondrial ATP production

Intracellular and Extracellular Roles for Tau in Neurodegenerative Disease

Mislocalization of neuronal tau in the absence of tangle pathology in phosphomutant tau knockin mice

Corrigendum: The disease associated Tau35 fragment has an increased propensity to aggregate compared to full-length tau

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