The Many Faces of Tau

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685

A protein factor essential for microtubule assembly

Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089

Mechanisms and Functional Implications of Adult Neurogenesis

Zhao, C., Deng, W., & Gage, F. H. (2008) · Cell · doi:10.1016/j.cell.2008.01.033 · Cited by 3,007

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480

Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model

Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014

Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821

Transmission and spreading of tauopathy in transgenic mouse brain

Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803

Inhibition of the Aggregation and Toxicity of the Minimal Amyloidogenic Fragment of Tau by Its Pro‐Substituted Analogues

Chemerovski‐Glikman, M., Frenkel‐Pinter, M., Mdah, R., Abu‐Mokh, A., Gazit, E., & Segal, D. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201701218 · Cited by 35

14-3-3 Proteins are Potential Regulators of Liquid–Liquid Phase Separation

Huang, X., Zheng, Z., Wu, Y., Gao, M., Su, Z., & Huang, Y. (2022) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-022-01067-3 · Cited by 35

Beyond Amyloid

Lane, R. F., Shineman, D. W., Steele, J., Lee, L. H., & Fillit, H. M. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-394816-8.00007-6 · Cited by 35

Usp14 Deficiency Increases Tau Phosphorylation without Altering Tau Degradation or Causing Tau-Dependent Deficits

Jin, Y. N., Chen, P., Watson, J. A., Walters, B. J., Phillips, S. E., Green, K., Schmidt, R. E., Wilson, J. A., Johnson, G. V. W., Roberson, E. D., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047884 · Cited by 34

Phosphorylation of the Usher syndrome 1G protein SANS controls Magi2-mediated endocytosis

Bauß, K., Knapp, B., Jores, P., Roepman, R., Kremer, H., van Wijk, E., Märker, T., & Uwe Wolfrum, B. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu104 · Cited by 34

Biphasic Alteration of the Inhibitory Synapse Scaffold Protein Gephyrin in Early and Late Stages of an Alzheimer Disease Model

Kiss, É., Gorgas, K., Schlicksupp, A., Groß, D., Kins, S., Kirsch, J., & Kuhse, J. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.05.013 · Cited by 34

Whole Genome Expression Analysis in a Mouse Model of Tauopathy Identifies MECP2 as a Possible Regulator of Tau Pathology

Maphis, N. M., Jiang, S., Binder, J., Wright, C., Gopalan, B., Lamb, B. T., & Bhaskar, K. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00069 · Cited by 33

Tau as a mediator of neurotoxicity associated to cerebral amyloid angiopathy

You, Y., Perkins, A., Cisternas, P., Muñoz, B., Taylor, X., You, Y., Garringer, H. J., Oblak, A. L., Atwood, B. K., Vidal, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0680-z · Cited by 33

Modification of the Drosophila model of in vivo Tau toxicity reveals protective phosphorylation by GSK3β

Povellato, G., Tuxworth, R. I., Hanger, D. P., & Tear, G. (2013) · Biology Open · doi:10.1242/bio.20136692 · Cited by 35

Frontotemporal dementia with Parkinsonism linked to chromosome-17 mutations enhance tau oligomer formation

Maeda, S., Sato, Y., & Takashima, A. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.04.014 · Cited by 33

Multi-site dynamic recording for Aβ oligomers-induced Alzheimer's disease in vitro based on neuronal network chip

Gao, F., Gao, K., He, C., Liu, M., Wan, H., & Wang, P. (2019) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2019.03.025 · Cited by 35

Relationship Between Tau and Cognition in the Evolution of Alzheimer’s Disease: New Insights from Tau PET

Tanner, J. A., & Rabinovici, G. D. (2020) · Journal of Nuclear Medicine · doi:10.2967/jnumed.120.257824 · Cited by 35

MMP-9 and MMP-2 Contribute to Neuronal Cell Death in iPSC Models of Frontotemporal Dementia with MAPT Mutations

Biswas, M. H. U., Almeida, S., Lopez-Gonzalez, R., Mao, W., Zhang, Z., Karydas, A., Geschwind, M. D., Biernat, J., Mandelkow, E., Futai, K., et al. (2016) · Stem Cell Reports · doi:10.1016/j.stemcr.2016.08.006 · Cited by 33

SSNA1 stabilizes dynamic microtubules and detects microtubule damage

Lawrence, E. J., Arnaiz, C., Arpağ, G., & Žanić, M. (2021) · eLife · doi:10.7554/elife.67282 · Cited by 35

NMDA and AMPA Receptors at Synapses: Novel Targets for Tau and α-Synuclein Proteinopathies

Italia, M., Ferrari, E. S., Luca, M. D., & Gardoni, F. (2022) · Biomedicines · doi:10.3390/biomedicines10071550 · Cited by 33

SIL1 Rescued Bip Elevation-Related Tau Hyperphosphorylation in ER Stress

Liu, Z.-C., Chu, J., Li, L., Song, J., Ning, L., Luo, H., Yang, S., Shi, Y., Wang, Q., Qu, N., et al. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-9039-4 · Cited by 32

The therapeutic potential of cell identity reprogramming for the treatment of aging-related neurodegenerative disorders

Smith, D. K., He, M., Zhang, C., & Zheng, J. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.01.006 · Cited by 34

Cerebral Waste Accumulation and Glymphatic Clearance as Mechanisms of Human Neurological Diseases

Janigro, D. (2016) · Journal of Neurology and Neuromedicine · doi:10.29245/2572.942x/2016/7.1082 · Cited by 32

Tau Filaments and the Development of Positron Emission Tomography Tracers

Goedert, M., Yamaguchi, Y., Mishra, S. K., Higuchi, M., & Sahara, N. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00070 · Cited by 32

Disrupting Neurons and Glial Cells Oneness in the Brain—The Possible Causal Role of Herpes Simplex Virus Type 1 (HSV-1) in Alzheimer’s Disease

Mielcarska, M. B., Skowrońska, K., Wyżewski, Z., & Toka, F. N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010242 · Cited by 32

Tau suppresses microtubule-regulated pancreatic insulin secretion

Mangiafico, S. P., Tuo, Q., Li, X.-L., Liu, Y., Haralambous, C., Ding, X., Ayton, S., Wang, Q., Laybutt, D. R., Chan, J. Y., et al. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02267-w · Cited by 35

Protein Disulfide Isomerase Interacts with Tau Protein and Inhibits Its Fibrillization

Xu, L.-R., Liu, X., Chen, J., & Liang, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076657 · Cited by 32

Tolfenamic acid reduces tau and CDK 5 levels: implications for dementia and tauopathies

Adwan, L. I., Subaiea, G. M., Basha, R. M., & Zawia, N. H. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12960 · Cited by 34

Effects of sub-chronic donepezil on brain Abeta and cognition in a mouse model of Alzheimer’s disease

Easton, A. E., Sankaranarayanan, S., Tanghe, A., Terwel, D., Lin, A., Hoque, N., Bourin, C., Gu, H., Ahlijanian, M. K., & Bristow, L. J. (2013) · Psychopharmacology · doi:10.1007/s00213-013-3152-3 · Cited by 33

Amyloid-β with isomerized Asp7 cytotoxicity is coupled to protein phosphorylation

Zatsepina, O. G., Kechko, O. I., Mitkevich, V. A., Kozin, S. A., Yurinskaya, M. M., Винокуров, М. Г., Serebryakova, M. V., Rezvykh, A. P., Evgen’ev, M. B., & Makarov, A. А. (2018) · Scientific Reports · doi:10.1038/s41598-018-21815-x · Cited by 33

Asparagus cochinchinensis stimulates release of nerve growth factor and abrogates oxidative stress in the Tg2576 model for Alzheimer’s disease

Lee, H. A., Kim, J. E., Sung, J. E., Yun, W. B., Kim, D. S., Lee, H. S., Hong, J. T., & Hwang, D. Y. (2018) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-017-1775-3 · Cited by 31

ATM-associated signalling triggers the unfolded protein response and cell death in response to stress

Hotokezaka, Y., Katayama, I., & Nakamura, T. (2020) · Communications Biology · doi:10.1038/s42003-020-1102-2 · Cited by 33

Tau immunization: a cautionary tale?

Mably, A. J., Kanmert, D., Donald, J. M. M., Liu, W., Caldarone, B. J., Lemere, C. A., O’Nuallain, B., Kosik, K. S., & Walsh, D. M. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.11.022 · Cited by 32

Cyclin-dependent kinase 5, a node protein in diminished tauopathy: a systems biology approach

Castro-Álvarez, J. F., Uribe‐Arias, A., Mejía-Raigosa, D., & Cardona‐Gómez, G. P. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00232 · Cited by 34

Lipid-dependent deposition of alpha-synuclein and Tau on neuronal Secretogranin II-positive vesicular membranes with age

Brekk, O. R., Moskites, A., Ole Isacson, A., & Hallett, P. J. (2018) · Scientific Reports · doi:10.1038/s41598-018-33474-z · Cited by 33

Metformin protects against neuroinflammation through integrated mechanisms of miR-141 and the NF-ĸB-mediated inflammasome pathway in a diabetic mouse model

Docrat, T. F., Nagiah, S., & Chuturgoon, A. A. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174146 · Cited by 31

Hyperphosphorylated Human Tau Accumulates at the Synapse, Localizing on Synaptic Mitochondrial Outer Membranes and Disrupting Respiration in a Mouse Model of Tauopathy

Trease, A. J., George, J. W., Roland, N. J., Lichter, E. Z., Emanuel, K. M., Totusek, S., Fox, H. S., & Stauch, K. L. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.852368 · Cited by 31

Phosphorylation of Tau Protein Associated as a Protective Mechanism in the Presence of Toxic, C-Terminally Truncated Tau in Alzheimer's Disease

Luna‐Muñoz, J., Charles, R., Claude, M., Flores-Rodríguez, P., Ávila, J., Sergio, R., de la Cruz, F., Mena, R., Meraz‐Ríos, M. A., & Florán, B. (2013) · InTech eBooks · doi:10.5772/54228 · Cited by 43

α-Isocubebenol alleviates scopolamine-induced cognitive impairment by repressing acetylcholinesterase activity

Song, S. H., Choi, S. M., Kim, J. E., Sung, J. E., Lee, H. A., Choi, Y. H., Bae, C. J., Choi, Y. W., & Hwang, D. Y. (2016) · Neuroscience Letters · doi:10.1016/j.neulet.2016.12.012 · Cited by 31

Designing of dual inhibitors for GSK-3β and CDK5: Virtual screening andin vitrobiological activities study

Xie, H., Wen, H., Zhang, D., Liu, L., Liu, B., Liu, Q., Jin, Q., Ke, K., Hu, M., & Chen, X. (2017) · Oncotarget · doi:10.18632/oncotarget.15085 · Cited by 32

Electrostatics of Tau Protein by Molecular Dynamics

Castro, T. G., Munteanu, F., & Cavaco-Paulo, A. M. (2019) · Biomolecules · doi:10.3390/biom9030116 · Cited by 32

Liquid − liquid phase separation of tau: Driving forces, regulation, and biological implications

Li, P., Chen, J., Wang, X., Su, Z., Gao, M., & Huang, Y. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106167 · Cited by 30

Modulation of Microtubule Properties and Functions by Encapsulation of Nanomaterials Using a Tau-Derived Peptide

Inaba, H., & Matsuura, K. (2021) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.20210202 · Cited by 31

Alzheimer’s Amyloid-β Oligomers Rescue Cellular Prion Protein Induced Tau Reduction via the Fyn Pathway

Chen, R.-J., Chang, W.-W., Lin, Y., Cheng, P., & Chen, Y. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn400085q · Cited by 30

Toxic oligomer species of amyloid-β in Alzheimer's disease, a timing issue

Lesné, S. (2014) · Swiss Medical Weekly · doi:10.4414/smw.2014.14021 · Cited by 36

Mechanisms of disordered neurodegenerative function: concepts and facts about the different roles of the protein kinase RNA-like endoplasmic reticulum kinase (PERK)

Taalab, Y. M., Ibrahim, N., Maher, A., Hassan, M., Mohamed, W. M. Y., Moustafa, A. A., Salama, M., Johar, D., & Bernstein, L. H. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0071 · Cited by 30

Autophagy in Disease Onset and Progression

Wang, H., Li, X., Zhang, Q., Fu, C., Jiang, W., Xue, J., Liu, S., Meng, Q., Ai, L., Zhi, X., et al. (2023) · Aging and Disease · doi:10.14336/ad.2023.0815 · Cited by 29

Blood and cerebrospinal fluid biomarkers

Kawata, K., Tierney, R., & Langford, D. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-63954-7.00022-7 · Cited by 29

Specific Degradation of Endogenous Tau Protein and Inhibition of Tau Fibrillation by Tanshinone IIA through the Ubiquitin–Proteasome Pathway

Cai, N., Chen, J., Bi, D., Gu, L., Yao, L., Li, X., Li, H., Xu, H. Y., Hu, Z., Liu, Q., et al. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b07022 · Cited by 29

Cognitive Enhancers (Nootropics). Part 3: Drugs Interacting with Targets other than Receptors or Enzymes. Disease-modifying Drugs

Froestl, W., Pfeifer, A., & Muhs, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121729 · Cited by 27

The physiological phosphorylation of tau is critically changed in fetal brains of individuals with Down syndrome

Milenković, I., Jarc, J., Dassler, E., Aronica, E., Iyer, A. M., Adle‐Biassette, H., Scharrer, A., Reischer, T., Hainfellner, J. A., & Kovács, G. G. (2017) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12406 · Cited by 29

Structure-based mechanism of preferential complex formation by apoptosis signal–regulating kinases

Trevelyan, S. J., Brewster, J. L., Burgess, A. E., Crowther, J. M., Cadell, A. L., Parker, B. L., Croucher, D. R., Dobson, R. C. J., Murphy, J. M., & Mace, P. D. (2020) · Science Signaling · doi:10.1126/scisignal.aay6318 · Cited by 27

Pathological Impact of Redox Post-Translational Modifications

Chahla, C., Kovacic, H., Ferhat, L., & Leloup, L. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0252 · Cited by 31

Protein aggregate formation in oligodendrocytes: tau and the cytoskeleton at the intersection of neuroprotection and neurodegeneration

Richter‐Landsberg, C. (2015) · Biological Chemistry · doi:10.1515/hsz-2015-0157 · Cited by 28

The misfolding mechanism of the key fragment R3 of tau protein: a combined molecular dynamics simulation and Markov state model study

Liu, H., Zhong, H., Xu, Z., Zhang, Q., Shah, S. J. A., Liu, H., & Yao, X. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp06954b · Cited by 28

Varenicline improved laparotomy-induced cognitive impairment by restoring mitophagy in aged mice

Wang, J., Zhu, S., Lü, W., Li, A., Zhou, Y., Chen, Y., Chen, M., Qian, C., Hu, X., Zhang, Y., et al. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174524 · Cited by 28

Friend or foe: role of pathological tau in neuronal death

Wu, M., Chen, Z., Jiang, M. H., Bao, B., Li, D., Yin, X., Wang, X., Liu, D., & Zhu, L. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02024-z · Cited by 28

Kinetic and thermodynamic study of beta-Boswellic acid interaction with Tau protein investigated by surface plasmon resonance and molecular modeling methods

Haghaei, H., Hosseini, S. R. A., Soltani, S., Fathi, F., Mokhtari, F., Karima, S., & Rashidi, M. (2019) · Bioimpacts · doi:10.15171/bi.2020.03 · Cited by 27

PET Imaging in Animal Models of Alzheimer’s Disease

Chen, B., Marquez-Nostra, B. V., Belitzky, E., Toyonaga, T., Tong, J., Huang, Y. H., & Cai, Z. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.872509 · Cited by 27

Pathological and physiological functional cross-talks of α-synuclein and tau in the central nervous system

Jin, M., Wang, S., Gao, X., Zou, Z., Hirotsune, S., & Sun, L. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382231 · Cited by 27

Cerebrospinal fluid biomarkers in neurological diseases in children

Shahim, P., Månsson, J., Darín, N., Zetterberg, H., & Mattsson, N. (2012) · European Journal of Paediatric Neurology · doi:10.1016/j.ejpn.2012.09.005 · Cited by 27

Maternal genotype influences behavioral development of 3×Tg-AD mouse pups

Blaney, C., Gunn, R. K., Stover, K. R., & Brown, R. E. (2013) · Behavioural Brain Research · doi:10.1016/j.bbr.2013.05.033 · Cited by 27

The Transcription Factor XBP1 in Memory and Cognition: implications in Alzheimer’s Disease

Cissé, M., Duplan, E., & Checler, F. (2016) · Molecular Medicine · doi:10.2119/molmed.2016.00229 · Cited by 28

Targeted protein degradation in CNS disorders: a promising route to novel therapeutics?

Kuemper, S., Cairns, A. G., Birchall, K., Yao, Z., & Large, J. M. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1370509 · Cited by 32

Induced pluripotent stem cell-based modeling of neurodegenerative diseases: a focus on autophagy

Jungverdorben, J., Till, A., & Brüstle, O. (2017) · Journal of Molecular Medicine · doi:10.1007/s00109-017-1533-5 · Cited by 27

Dynamical decoration of stabilized-microtubules by Tau-proteins

Hervy, J., & Bicout, D. (2019) · Scientific Reports · doi:10.1038/s41598-019-48790-1 · Cited by 27

Microtubule Dynamics and Neuronal Excitability: Advances on Cytoskeletal Components Implicated in Epileptic Phenomena

Gambino, G., Rizzo, V., Giglia, G., Ferraro, G., & Sardo, P. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00963-7 · Cited by 26

A common theme for axonopathies? The dependency cycle of local axon homeostasis

Prokop, A. (2021) · Cytoskeleton · doi:10.1002/cm.21657 · Cited by 24

The Structure Biology of Tau and Clue for Aggregation Inhibitor Design

Wang, D., Huang, X., Yan, L., Zhou, L., Chang, Y., Wu, J., Su, Z., & Huang, Y. (2021) · The Protein Journal · doi:10.1007/s10930-021-10017-6 · Cited by 27

The Many Faces of Post-Ischemic Tau Protein in Brain Neurodegeneration of the Alzheimer’s Disease Type

Pluta, R. M., Czuczwar, S. J., Januszewski, S., & Jabłoński, M. (2021) · Cells · doi:10.3390/cells10092213 · Cited by 24

Alternative Conformations of the Tau Repeat Domain in Complex with an Engineered Binding Protein

Grüning, C. S. R., Mirecka, E. A., Klein, A. N., Mandelkow�, E., Willbold, D., Marino, S. F., Stoldt, M., & Hoyer, W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.560920 · Cited by 27

Isolation and characterization of antibody fragments selective for toxic oligomeric tau

Tian, H., Davidowitz, E. J., Lopez, P. L. D. C., He, P., Schulz, P., Moe, J. G., & Sierks, M. R. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.12.002 · Cited by 27

Neurodegeneration in a Drosophila Model for the Function of TMCC2, an Amyloid Protein Precursor-Interacting and Apolipoprotein E-Binding Protein

Hopkins, P. C. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055810 · Cited by 26

Cerebrospinal Fluid Biomarkers in Alzheimer’s Disease—From Brain Starch to Bench and Bedside

Pawlowski, M., Meuth, S., & Duning, T. (2017) · Diagnostics · doi:10.3390/diagnostics7030042 · Cited by 25

Imaging glymphatic response to glioblastoma

Kaur, J., Ding, G., Zhang, L., Lu, Y., Luo, H., Li, L., Boyd, E., Li, Q., Wei, M., Zhang, Z., et al. (2023) · Cancer Imaging · doi:10.1186/s40644-023-00628-w · Cited by 27

Passive immunization against phosphorylated tau improves features of Huntington's disease pathology

Alpaugh, M., Masnata, M., de Rus Jacquet, A., Lepinay, E., Denis, H. L., Saint-Pierre, M., Davies, P., Planel, E., & Cicchetti, F. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.01.020 · Cited by 25

GSK-3β-dependent downregulation of γ-taxilin and αNAC merge to regulate ER stress responses

Hotokezaka, Y., Katayama, I., van Leyen, K., & Nakamura, T. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.90 · Cited by 25

The Cellular Distribution and Ser262 Phosphorylation of Tau Protein Are Regulated by BDNF In Vitro

Chen, Q., Zhou, Z., Zhang, L., Xu, S., Chen, C., & Yu, Z. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091793 · Cited by 26

STED imaging of tau filaments in Alzheimer’s disease cortical grey matter

Benda, A., Aitken, H., Davies, D., Whan, R. M., & Goldsbury, C. S. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.07.003 · Cited by 24

Mechanistic and Structural Origins of the Asymmetric Barrier to Prion-like Cross-Seeding between Tau-3R and Tau-4R

Kumar, H., & Udgaonkar, J. B. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.09.010 · Cited by 25

Interaction between a MAPT variant causing frontotemporal dementia and mutant APP affects axonal transport

Adalbert, R., Milde, S., Durrant, C. S., Ando, K., Stygelbout, V., Yilmaz, Z., Gould, S. A., Brion, J., & Coleman, M. P. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.03.033 · Cited by 25

The science and questions surrounding chronic traumatic encephalopathy

Ban, V. S., Madden, C. J., Bailes, J. E., Batjer, H. H., & Lonser, R. R. (2016) · Neurosurgical FOCUS · doi:10.3171/2016.2.focus15609 · Cited by 24

A double whammy effect of ethnicity and gender on consumer responses to management level service failures

Wu, L. L., Han, R., & Mattila, A. S. (2016) · Journal of service management · doi:10.1108/josm-03-2014-0092 · Cited by 24

Upregulated levels and pathological aggregation of abnormally phosphorylated Tau-protein in children with neurodevelopmental disorders

Rankovic, M., & Zweckstetter, M. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.12.014 · Cited by 25

Resveratrol targeting tau proteins, amyloid‐beta aggregations, and their adverse effects: An updated review

Ashrafizadeh, M., Zarrabi, A., Najafi, M., Samarghandian, S., Mohammadinejad, R., & Ahn, K. S. (2020) · Phytotherapy Research · doi:10.1002/ptr.6732 · Cited by 24

Transcriptional control of cell cycle-dependent kinase 4 by Smad proteins—implications for Alzheimer's disease

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