AZP2006, a new promising treatment for Alzheimer’s and related diseases

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works

The ARRIVE guidelines 2.0: Updated guidelines for reporting animal research

Percie du Sert, N., Hurst, V., Ahluwalia, A., Alam, S., Avey, M. T., Baker, M., Browne, W. J., Clark, A., Cuthill, I. C., Dirnagl, U., et al. (2020) · PLOS Biology · doi:10.1371/journal.pbio.3000410 · Cited by 5,939 · see citing works

Mechanisms underlying inflammation in neurodegeneration

Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., & Gage, F. H. (2010) · Cell · doi:10.1016/j.cell.2010.02.016 · Cited by 3,580 · see citing works

The ARRIVE guidelines 2.0: Updated guidelines for reporting animal research

du Sert, N. P., Hurst, V., Ahluwalia, A., Alam, S., Avey, M. T., Baker, M., Browne, W. J., Clark, A., Cuthill, I. C., Dirnagl, U., et al. (2020) · Experimental Physiology · doi:10.1113/ep088870 · Cited by 3,538 · see citing works

Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation

Kyriakis, J. M., & Avruch, J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.807 · Cited by 3,369 · see citing works

Toll-Like Receptor Signaling Pathways

Kawasaki, T., & Kawai, T. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00461 · Cited by 3,250 · see citing works

Alzheimer's disease

Lane, C. A., Hardy, J., & Schott, J. M. (2018) · European Journal of Neurology · doi:10.1111/ene.13439 · Cited by 2,616 · see citing works

Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17

Baker, M., Mackenzie, I. R., Pickering-Brown, S. M., Gass, J., Rademakers, R., Lindholm, C., Snowden, J., Adamson, J., Sadovnick, A. D., Rollinson, S., et al. (2006) · Nature · doi:10.1038/nature05016 · Cited by 2,058 · see citing works

Microglial physiology: unique stimuli, specialized responses

Ransohoff, R. M., & Perry, V. H. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132528 · Cited by 1,858 · see citing works

Microglia in neurodegenerative disease

Perry, V. H., Nicoll, J. A. R., & Holmes, C. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.17 · Cited by 1,543 · see citing works

PHARMACOLOGICAL EFFECTS PRODUCED BY INTRACEREBRAL INJECTION OF DRUGS IN THE CONSCIOUS MOUSE

Haley, T. J., & McCormick, W. (1957) · British Journal of Pharmacology and Chemotherapy · doi:10.1111/j.1476-5381.1957.tb01354.x · Cited by 1,535 · see citing works

Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21

Cruts, M., Gijselinck, I., van der Zee, J., Engelborghs, S., Wils, H., Pirici, D., Rademakers, R., Vandenberghe, R., Dermaut, B., Martin, J.-J., et al. (2006) · Nature · doi:10.1038/nature05017 · Cited by 1,512 · see citing works

Untitled work

Binder (2004) · doi:10.1080/08977190410001723308 · Cited by 1,481 · see citing works

Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer’s disease

Reddy, P. H., & Beal, M. F. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.002 · Cited by 975 · see citing works

Review: Activation patterns of microglia and their identification in the human brain

Boche, D., Perry, V. H., & Nicoll, J. A. R. (2012) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12011 · Cited by 911 · see citing works

The Genetics of Alzheimer's Disease

Bertram, L., & Tanzi, R. E. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00008-4 · Cited by 784 · see citing works

The genetics of Alzheimer disease

Tanzi, R. E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006296 · Cited by 727 · see citing works

Amyloid-Beta and Phosphorylated Tau Accumulations Cause Abnormalities at Synapses of Alzheimer’s disease Neurons

Rajmohan, R., & Reddy, P. H. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160612 · Cited by 695 · see citing works

Neuroinflammation Induces Neurodegeneration.

Kempuraj, D., Thangavel, R., Natteru, P., Selvakumar, G. P., Saeed, D., Zahoor, H., Zaheer, S., Iyer, S. S., & Zaheer, A. (2016) · PubMed · Cited by 672 · see citing works

Mutations in progranulin are a major cause of ubiquitin-positive frontotemporal lobar degeneration

Gass, J. M., Cannon, A. D., Mackenzie, I. R., Boeve, B. F., Baker, M. C., Adamson, J. L., Crook, R., Melquist, S., Kuntz, K., Petersen, R. C., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl241 · Cited by 574 · see citing works

Sortilin-Mediated Endocytosis Determines Levels of the Frontotemporal Dementia Protein, Progranulin

Hu, F., Padukkavidana, T., Vægter, C. B., Brady, O. A., Zheng, Y., Mackenzie, I. R., Feldman, H., Nykjær, A., & Strittmatter, S. M. (2010) · Neuron · doi:10.1016/j.neuron.2010.09.034 · Cited by 545 · see citing works

Amnesia induced in mice by centrally administered β-amyloid peptides involves cholinergic dysfunction

Maurice, T., Lockhart, B. P., & Privat, A. (1996) · Brain Research · doi:10.1016/0006-8993(95)01032-7 · Cited by 524 · see citing works

Quantification of lipid peroxidation in tissue extracts based on Fe(III)xylenol orange complex formation

Hermes‐Lima, M., Willmore, W. G., & Storey, K. B. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00020-x · Cited by 523 · see citing works

A Cell Surface Receptor Complex for Fibrillar β-Amyloid Mediates Microglial Activation

Bamberger, M. E., Harris, M. E., McDonald, D. R., Husemann, J., & Landreth, G. E. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-07-02665.2003 · Cited by 501 · see citing works

Toll‐like receptor 9 binds single‐stranded CpG‐DNA in a sequence‐ and pH‐dependent manner

Rutz, M., Metzger, J., Gellert, T., Luppa, P. B., Lipford, G. B., Wagner, H., & Bauer, S. (2004) · European Journal of Immunology · doi:10.1002/eji.200425218 · Cited by 499 · see citing works

Progranulin is a mediator of the wound response

He, Z., Ong, C. H. P., Halper, J., & Bateman, A. (2003) · Nature Medicine · doi:10.1038/nm816 · Cited by 490 · see citing works

Strikingly Different Clinicopathological Phenotypes Determined by Progranulin-Mutation Dosage

Smith, K. R., Damiano, J., Franceschetti, S., Carpenter, S., Canafoglia, L., Morbin, M., Rossi, G., Pareyson, D., Mole, S. E., Staropoli, J. F., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2012.04.021 · Cited by 489 · see citing works

Inflammatory Mechanisms in Alzheimer's Disease: Inhibition of β-Amyloid-Stimulated Proinflammatory Responses and Neurotoxicity by PPARγ Agonists

Combs, C. K., Johnson, D. E., Karlo, J. C., Cannady, S. B., & Landreth, G. E. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-02-00558.2000 · Cited by 483 · see citing works

MEMBRANE-ASSOCIATED GUANYLATE KINASES REGULATE ADHESION AND PLASTICITY AT CELL JUNCTIONS

Funke, L., Dakoji, S., & Bredt, D. S. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133339 · Cited by 469 · see citing works

Progranulin functions as a neurotrophic factor to regulate neurite outgrowth and enhance neuronal survival

Damme, P. V., Hoecke, A. V., Lambrechts, D., Vanacker, P., Bogaert, E., Swieten, J. C. V., Carmeliet, P., Bosch, L. V. D., & Robberecht, W. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200712039 · Cited by 421 · see citing works

Toll‐like receptors in central nervous system glial inflammation and homeostasis

Kielian, T. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20767 · Cited by 363 · see citing works

Cellular Localization of Gene Expression for Progranulin

DANIEL, R. L., He, Z., Carmichael, K. P., Halper, J. T., & Bateman, A. (2000) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540004800713 · Cited by 346 · see citing works

Saposin proteins: structure, function, and role in human lysosomal storage disorders

O’Brien, J. S., & Kishimoto, Y. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.3.2001789 · Cited by 331 · see citing works

Sigma1 (σ1) receptor agonists and neurosteroids attenuate β25–35-amyloid peptide-induced amnesia in mice through a common mechanism

Maurice, T., Su, T., & Privat, A. (1998) · Neuroscience · doi:10.1016/s0306-4522(97)00405-3 · Cited by 291 · see citing works

The anti‐amnesic and neuroprotective effects of donepezil against amyloid β25‐35peptide‐induced toxicity in mice involve an interaction with theσ1receptor

Meunier, J., Ieni, J. R., & Maurice, T. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706927 · Cited by 289 · see citing works

SR Proteins: Binders, Regulators, and Connectors of RNA

Jeong-Yu, S. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.2319 · Cited by 270 · see citing works

Synaptic Changes in Alzheimer's Disease

Gylys, K. H., Fein, J. A., Yang, F., Wiley, D. J., Miller, C. A., & Cole, G. M. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63436-0 · Cited by 253 · see citing works

Neuronal damage in brain inflammation

Aktas, O., Ullrich, O., Infante-Duarte, C., Nitsch, R., & Zipp, F. (2007) · Archives of Neurology · doi:10.1001/archneur.64.2.185 · Cited by 249 · see citing works

Evidence for a role of the rare p.A152T variant in MAPT in increasing the risk for FTD-spectrum and Alzheimer's diseases

Coppola, G., Chinnathambi, S., Lee, J. J., Dombroski, B. A., Baker, M. C., Soto-Ortolaza, A. I., Lee, S. E., Klein, E., Huang, A. Y., Sears, R., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds161 · Cited by 240 · see citing works

Progranulin protects against amyloid β deposition and toxicity in Alzheimer's disease mouse models

Minami, S. S., Min, S.-W., Krabbe, G., Wang, C., Zhou, Y., Asgarov, R., Li, Y., Martens, L. H., Elia, L. P., Ward, M. E., et al. (2014) · Nature Medicine · doi:10.1038/nm.3672 · Cited by 237 · see citing works

Mechanisms of neuroimmune gene induction in alcoholism

Crews, F. T., & Vetreno, R. P. (2016) · Psychopharmacology · doi:10.1007/s00213-015-3906-1 · Cited by 232 · see citing works

The lysosomal function of progranulin, a guardian against neurodegeneration

Paushter, D. H., Du, H., Feng, T., & Hu, F. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1861-8 · Cited by 230 · see citing works

Molecular and Cellular Basis of Neurodegeneration in Alzheimer’s Disease

Jeong, S. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.0096 · Cited by 230 · see citing works

Granulins, a novel class of peptide from leukocytes

Bateman, A., Belcourt, D., Bennett, H. P. J., Lazure, C., & Solomon, S. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)80908-8 · Cited by 206 · see citing works

Targeted Delivery of siRNA

Oliveira, S., Storm, G., & Schiffelers, R. M. (2006) · BioMed Research International · doi:10.1155/jbb/2006/63675 · Cited by 206 · see citing works

Prosaposin facilitates sortilin-independent lysosomal trafficking of progranulin

Zhou, X., Sun, L., de Oliveira, F. M. B., Qi, X., Brown, W. J., Smolka, M. B., Sun, Y., & Hu, F. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201502029 · Cited by 201 · see citing works

Biological activities and signaling pathways of the granulin/epithelin precursor.

Zanocco‐Marani, T., Bateman, A., Romano, G., Valentinis, B., He, Z., & Baserga, R. (1999) · PubMed · Cited by 185 · see citing works

Granulin Is a Soluble Cofactor for Toll-like Receptor 9 Signaling

Park, B., Buti, L., Lee, S., Matsuwaki, T., Spooner, E., Brinkmann, M. M., Nishihara, M., & Ploegh, H. L. (2011) · Immunity · doi:10.1016/j.immuni.2011.01.018 · Cited by 176 · see citing works

SAMP8 mice as a neuropathological model of accelerated brain aging and dementia: Toshio Takeda's legacy and future directions

Akiguchi, I., Pallàs, M., Budka, H., Akiyama, H., Ueno, M., Han, J., Yagi, H., Tomohumi, N., Chiba, Y., Sugiyama, H., et al. (2017) · Neuropathology · doi:10.1111/neup.12373 · Cited by 175 · see citing works

Studying small molecule–aptamer interactions using MicroScale Thermophoresis (MST)

Entzian, C., & Schubert, T. E. O. (2015) · Methods · doi:10.1016/j.ymeth.2015.08.023 · Cited by 173 · see citing works

Genetic variability in progranulin contributes to risk for clinically diagnosed Alzheimer disease

Brouwers, N., Sleegers, K., Engelborghs, S., Maurer‐Stroh, S., Gijselinck, I., van der Zee, J., Pickut, B. A., den Broeck, M. V., Mattheijssens, M., Peeters, K., et al. (2008) · Neurology · doi:10.1212/01.wnl.0000319688.89790.7a · Cited by 162 · see citing works

Progranulin (PC-cell-derived growth factor/acrogranin) regulates invasion and cell survival.

He, Z., Ismail, A., Kriazhev, L., Sadvakassova, G., & Bateman, A. (2002) · PubMed · Cited by 153 · see citing works

Alzheimer and Parkinson Diagnoses in Progranulin Null Mutation Carriers in an Extended Founder Family

Brouwers, N., Nuytemans, K., van der Zee, J., Gijselinck, I., Engelborghs, S., Theuns, J., Kumar‐Singh, S., Pickut, B. A., Pals, P., Dermaut, B., et al. (2007) · Archives of Neurology · doi:10.1001/archneur.64.10.1436 · Cited by 150 · see citing works

Mediation of estrogen mitogenic effect in human breast cancer MCF-7 cells by PC-cell-derived growth factor (PCDGF/granulin precursor)

Lu, R., & Serrero, G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.142 · Cited by 146 · see citing works

Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies

Strang, K. H., Croft, C. L., Sorrentino, Z. A., Chakrabarty, P., Golde, T. E., & Giasson, B. I. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815357 · Cited by 144 · see citing works

Assessment of ZnT3 and PSD95 protein levels in Lewy body dementias and Alzheimer's disease: association with cognitive impairment

Whitfield, D., Vallortigara, J., Alghamdi, A., Howlett, D. R., Hortobágyi, T., Johnson, M., Attems, J., Newhouse, S., Ballard, C. G., Thomas, A. J., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.06.015 · Cited by 141 · see citing works

Progranulin: a new avenue towards the understanding and treatment of neurodegenerative disease

Chitramuthu, B. P., Bennett, H. P. J., & Bateman, A. (2017) · Brain · doi:10.1093/brain/awx198 · Cited by 138 · see citing works

TLR signaling adaptor protein MyD88 in primary sensory neurons contributes to persistent inflammatory and neuropathic pain and neuroinflammation

Liu, X., Liu, T., Chen, G., Wang, B., Yu, X., Cui, Y., & Ji, R. (2016) · Scientific Reports · doi:10.1038/srep28188 · Cited by 130 · see citing works

Mutations other than null mutations producing a pathogenic loss of progranulin in frontotemporal dementia

van der Zee, J., Ber, I. L., Maurer‐Stroh, S., Engelborghs, S., Gijselinck, I., Camuzat, A., Brouwers, N., Vandenberghe, R. R., Sleegers, K., Hannequin, D., et al. (2007) · Human Mutation · doi:10.1002/humu.9484 · Cited by 123 · see citing works

Key Aging-Associated Alterations in Primary Microglia Response to Beta-Amyloid Stimulation

Caldeira, C., Cunha, C., Vaz, A. R., Falcão, A. S., Barateiro, A., Seixas, E., Fernandes, A., & Brites, D. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00277 · Cited by 117 · see citing works

Extracellular progranulin protects cortical neurons from toxic insults by activating survival signaling

Xu, J., Xilouri, M., Bruban, J., Shioi, J., Shao, Z., Papazoglou, I., Vekrellis, K., & Robakis, N. K. R. K. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.06.017 · Cited by 107 · see citing works

Progranulin locus deletion in frontotemporal dementia

Gijselinck, I., van der Zee, J., Engelborghs, S., Goossens, D., Peeters, K., Mattheijssens, M., Corsmit, E., Del‐Favero, J., Deyn, P. P. D., Broeckhoven, C. V., et al. (2007) · Human Mutation · doi:10.1002/humu.20651 · Cited by 94 · see citing works

Restoring neuronal progranulin reverses deficits in a mouse model of frontotemporal dementia

Arrant, A. E., Filiano, A. J., Unger, D. E., Young, A. H., & Roberson, E. D. (2017) · Brain · doi:10.1093/brain/awx060 · Cited by 86 · see citing works

Lysosomal processing of progranulin

Zhou, X., Paushter, D. H., Feng, T., Sun, L., Reinheckel, T., & Hu, F. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0205-9 · Cited by 83 · see citing works

Necrosis, apoptosis, necroptosis, three modes of action of dopaminergic neuron neurotoxins

Callizot, N., Combes, M., Henriques, A., & Poindron, P. (2019) · PLoS ONE · doi:10.1371/journal.pone.0215277 · Cited by 81 · see citing works

Differential expression of PSD proteins in age-related spatial learning impairments

Nyffeler, M., Zhang, W., Feldon, J., & Knuesel, I. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.11.003 · Cited by 72 · see citing works

Neuroprotective effect of a new photobiomodulation technique against Aβ 25–35 peptide–induced toxicity in mice: Novel hypothesis for therapeutic approach of Alzheimer's disease suggested

Blivet, G., Meunier, J., Roman, F. J., & Touchon, J. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2017.12.003 · Cited by 66 · see citing works

Expression of the Growth Factor Progranulin in Endothelial Cells Influences Growth and Development of Blood Vessels: A Novel Mouse Model

Toh, H., Cao, M., Daniels, E., & Bateman, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064989 · Cited by 62 · see citing works

Dysregulations of mitochondrial quality control and autophagic flux at an early age lead to progression of sarcopenia in Samp8 mice

Liu, H.-W., Chang, Y.-C., Chan, Y.-C., Hu, S.-H., Liu, M.-Y., & Chang, S.-J. (2020) · Biogerontology · doi:10.1007/s10522-020-09867-x · Cited by 60 · see citing works

Tau Phosphorylation, Aggregation, and Cell Toxicity

Ávila, J., Santa‐María, I., Pérez, M., Hernández, F., & Moreno, F. J. (2006) · BioMed Research International · doi:10.1155/jbb/2006/74539 · Cited by 59 · see citing works

Progranulin enhances neural progenitor cell proliferation through glycogen synthase kinase 3β phosphorylation

Nedachi, T., Kawai, T., Matsuwaki, T., Yamanouchi, K., & Nishihara, M. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.04.037 · Cited by 55 · see citing works

Dynorphin A-(1–13) markedly improves scopolamine-induced impairment of spontaneous alternation performance in mice

Itoh, J., Ukai, M., & Kameyama, T. (1993) · European Journal of Pharmacology · doi:10.1016/0014-2999(93)90469-x · Cited by 53 · see citing works

Nociceptin/orphanin FQ and nocistatin on learning and memory impairment induced by scopolamine in mice

Hiramatsu, M., & Inoue, K. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702595 · Cited by 52 · see citing works

Tumor necrosis factor-α enhances voltage-gated Na+ currents in primary culture of mouse cortical neurons

Chen, W., Sheng, J., Guo, J., Gao, F., Zhao, X., Dai, J., Wang, G., & Li, K. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0349-x · Cited by 48 · see citing works

The interaction between progranulin and prosaposin is mediated by granulins and the linker region between saposin B and C

Zhou, X., Sullivan, P. M., Sun, L., & Hu, F. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14110 · Cited by 44 · see citing works

The γ-secretase inhibitor 2-[(1R)-1-[(4-chlorophenyl)sulfonyl](2,5-difluorophenyl) amino]ethyl-5-fluorobenzenebutanoic acid (BMS-299897) alleviates Aβ1–42 seeding and short-term memory deficits in the Aβ25–35 mouse model of Alzheimer's disease

Meunier, J., Villard, V., Givalois, L., & Maurice, T. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.10.033 · Cited by 41 · see citing works

Role for the microtubule-associated protein tau variant p.A152T in risk of α-synucleinopathies

Labbé, C., Ogaki, K., Lorenzo‐Betancor, O., Soto‐Ortolaza, A. I., Walton, R. L., Rayaprolu, S., Fujioka, S., Murray, M. E., Heckman, M. G., Puschmann, A., et al. (2015) · Neurology · doi:10.1212/wnl.0000000000001946 · Cited by 38 · see citing works

New piperazine multi-effect drugs prevent neurofibrillary degeneration and amyloid deposition, and preserve memory in animal models of Alzheimer's disease

Sergeant, N., Vingtdeux, V., Eddarkaoui, S., Gay, M., Evrard, C., Fur, N. L., Laurent, C., Caillierez, R., Obriot, H., Larchanché, P.-E., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.028 · Cited by 34 · see citing works

Reduced serum progranulin level might be associated with Parkinson's disease risk

Mateo, I., Aramburu, I. G., Pozueta, A., Vázquez‐Higuera, J. L., Rodríguez‐Rodríguez, E., Sánchez‐Juan, P., Calero, M., Dobato, J. L., Infante, J., Berciano, J., et al. (2013) · European Journal of Neurology · doi:10.1111/ene.12090 · Cited by 30 · see citing works

Chloroquine and Chloroquinoline Derivatives as Models for the Design of Modulators of Amyloid Peptide Precursor Metabolism

Melnyk, P., Vingtdeux, V., Burlet, S., Eddarkaoui, S., Grosjean, M., Larchanché, P.-E., Hochart, G., Sergheraert, C., Estrella, C., Barrier, M., et al. (2015) · ACS Chemical Neuroscience · doi:10.1021/cn5003013 · Cited by 30 · see citing works

Operational dissection of β‐amyloid cytopathic effects on cultured neurons

Callizot, N., Combes, M., Steinschneider, R., & Poindron, P. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23193 · Cited by 29 · see citing works

Two heterozygous progranulin mutations in progressive supranuclear palsy

Yang, W., Deng, B., Huang, Y., Liu, J., Huang, Z., Chang, Z., Zhu, S., Chan, L. L., Chaudhuri, К. R., Tan, E., et al. (2020) · Brain · doi:10.1093/brain/awaa428 · Cited by 10 · see citing works

TLR9 sustains autophagic flux

Gough, N. R. (2016) · Science Signaling · doi:10.1126/scisignal.aah5146 · Cited by 4 · see citing works

Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets

Gao, C., Jiang, J., Tan, Y., & Chen, S. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01588-0 · Cited by 1,616 · see citing works

Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation

Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516 · see citing works

Microglial efferocytosis: Diving into the Alzheimer’s disease gene pool

Romero-Molina, C., Garretti, F., Andrews, S. J., Marcora, E., & Goate, A. M. (2022) · Neuron · doi:10.1016/j.neuron.2022.10.015 · Cited by 111 · see citing works

Neuroinflammation, Its Role in Alzheimer's Disease and Therapeutic Strategies

Király, M., Foss, J. F., & Giordano, T. (2023) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2023.109 · Cited by 103 · see citing works

TLR9: A friend or a foe

Saber, M. M., Monir, N., Awad, A. S., Elsherbiny, M. E., & Zaki, H. F. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120874 · Cited by 59 · see citing works

Mechanism of microglia-mediated neuroinflammation, associated cognitive dysfunction, and therapeutic updates in Alzheimer's disease

Ghimire, A., Rehman, S. A., Subhani, A., Khan, M. A., Rahman, Z., Iqubal, M. K., & Iqubal, A. (2025) · hLife · doi:10.1016/j.hlife.2024.11.006 · Cited by 30 · see citing works

Alzheimer's Disease and Frontotemporal Dementia: A Review of Pathophysiology and Therapeutic Approaches

Kelliny, S., Zhou, X., & Bobrovskaya, L. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70046 · Cited by 25 · see citing works

Pharmacotherapies for the Treatment of Progressive Supranuclear Palsy: A Narrative Review

Dunning, E. E., Decourt, B., Zawia, N. H., Shill, H. A., & Sabbagh, M. N. (2024) · Neurology and Therapy · doi:10.1007/s40120-024-00614-9 · Cited by 18 · see citing works

Role of Neuronal TRPC6 Channels in Synapse Development, Memory Formation and Animal Behavior

Zernov, N., & Александровна, П. Е. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015415 · Cited by 18 · see citing works

Progressive supranuclear palsy: Neuropathology, clinical presentation, diagnostic challenges, management, and emerging therapies

Derosier, F. J., Hibbs, C., Alessi, K., Padda, I., Rodriguez, J., Pradeep, S., & Parmar, M. S. (2024) · Disease-a-Month · doi:10.1016/j.disamonth.2024.101753 · Cited by 17 · see citing works

MAPT haplotype-associated transcriptomic changes in progressive supranuclear palsy

Ressler, H. W., Humphrey, J., Vialle, R. A., Babrowicz, B. M., Kandoi, S., Raj, T., Dickson, D. W., Ertekin‐Taner, N., Crary, J. F., & Farrell, K. W. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01839-3 · Cited by 17 · see citing works

Activation of innate immune receptor TLR9 by mitochondrial DNA plays essential roles in the chemical long-term depression of hippocampal neurons

Atarashi, N., Morishita, M., & Matsuda, S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105744 · Cited by 13 · see citing works

Analysis of changes in intercellular communications in Alzheimer’s disease reveals conserved changes in glutamatergic transmission in mice and humans

Bartas, K., Nguyen, M. H., Zhao, W., Hui, M., Nie, Q., & Beier, K. T. (2025) · Scientific Reports · doi:10.1038/s41598-025-10795-4 · Cited by 12 · see citing works

Amyloid-beta peptide toxicity in the aged brain is a one-way journey into Alzheimer’s disease

Culley, G. R., Henriques, A., Hardy, D., Wojcinski, A., Chabert, A., Waly, B. E., Poindron, P., & Callizot, N. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1569181 · Cited by 11 · see citing works

First-In-Human Safety, Tolerability, and Pharmacokinetics of Single and Multiple Doses of AZP2006, A Synthetic Compound for the Treatment of Alzheimer’s Disease and Related Diseases

Verwaerde, P., Estrella, C., Burlet, S., Barrier, M., Marotte, A.-A., & Clincke, G. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-220883 · Cited by 10 · see citing works

Discovery of a novel piperazine derivative, cmp2: a selective TRPC6 activator suitable for treatment of synaptic deficiency in Alzheimer’s disease hippocampal neurons

Zernov, N., Ghamaryan, V., Melenteva, D., Makichyan, A. T., Hunanyan, L. S., & Александровна, П. Е. (2024) · Scientific Reports · doi:10.1038/s41598-024-73849-z · Cited by 10 · see citing works

Hypoxic Preconditioned Neural Stem Cell-Derived Extracellular Vesicles Contain Distinct Protein Cargo from Their Normal Counterparts

Gharbi, T., Liu, C., Khan, H. L., Zhang, Z., Yang, G., & Tang, Y. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45030127 · Cited by 7 · see citing works

A Polyaminobiaryl-Based β-secretase Modulator Alleviates Cognitive Impairments, Amyloid Load, Astrogliosis, and Neuroinflammation in APPSwe/PSEN1ΔE9 Mice Model of Amyloid Pathology

Tautou, M., Descamps, F., Larchanché, P.-E., Buée, L., Bakali, J. E., Melnyk, P., & Sergeant, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065285 · Cited by 7 · see citing works

Desmethylglycitein Attenuates Scopolamine-Induced Cognitive Deficits via Nrf-2 Activation and IL-1β Suppression

Dalal, D., Singh, L., & Singh, A. (2023) · Neurophysiology · doi:10.1007/s11062-025-09967-9 · Cited by 6 · see citing works

Prosaposin in CNS health and disease, metabolic stress and exercise adaptation

Taha, H. B., Zhu, S., & Wang, E. (2026) · Journal of Molecular Medicine · doi:10.1007/s00109-026-02643-3 · Cited by 5 · see citing works

AZP2006 (Ezeprogind®): a Promising New Drug Candidate in the Battle Against Neurodegenerative Diseases

Verwaerde, P., & Defert, O. (2025) · ChemMedChem · doi:10.1002/cmdc.202400891 · Cited by 4 · see citing works

Progranulin’s Protective Mechanisms and Therapeutic Potential in Cardiovascular Disease

Qiao, G., Lu, Y., Wu, J., Ren, C., Lin, R., & Zhang, C. (2025) · Cells · doi:10.3390/cells14110762 · Cited by 4 · see citing works

AZP2006 in Progressive Supranuclear Palsy: Outcomes from a Phase 2a Multicenter, Randomized Trial, and Open‐Label Extension on Safety, Biomarkers, and Disease Progression

Corvol, J., Obadia, M. A., Moreau, C., Mariani, L., Brandel, J., Devos, D., Sambin, S., Carrière, N., Höglinger, G. U., Lebouteux, M., et al. (2025) · Movement Disorders · doi:10.1002/mds.70049 · Cited by 4 · see citing works

Targeting alpha-synuclein or tau for treating neurodegenerative movement disorders

Cuina, M. L., & Meissner, W. G. (2022) · Revue Neurologique · doi:10.1016/j.neurol.2022.03.010 · Cited by 4 · see citing works

Targeting Granulin Haploinsufficiency in Frontotemporal Dementia: From Genetic Mechanisms to Therapeutics

Bagyinszky, E., & An, S. S. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26209960 · Cited by 3 · see citing works

Suspension Culture With Uniform Shear Stress in Brain Organoids‐on‐a‐Chip for Modelling Alzheimer's Disease

Liu, J., Li, Q., Zhu, H., Li, A., Geng, B., Li, Z. A., & Tian, T. (2026) · Advanced Healthcare Materials · doi:10.1002/adhm.202503966 · Cited by 3 · see citing works

Central Role of Toll-like Receptor-9 Gene Function in Inflammation-Mediated Neuronal Plasticity: Implications for Long-Term Memory Development

Oyovwi, M. O., Emojevwe, V. O., Ben‐Azu, B., & Jeroh, E. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05446-8 · Cited by 2 · see citing works

Treatment options for Alzheimer’s Disease: An overview of the amyloid, tau, and alternate hypotheses

Eroltu, K. (2023) · Journal of High School Science · doi:10.64336/001c.89250 · Cited by 1 · see citing works

Pharmacomodulations around an anti-Alzheimer drug-candidate

Marc, S., Mésangeau, C., Coevoet, M., Barczyk, A., Burlet, S., Verwaerde, P., Estrella, C., Brantis, C., Sergeant, N., Carato, P., et al. (2021) · European Journal of Medicinal Chemistry Reports · doi:10.1016/j.ejmcr.2021.100020 · Cited by 1 · see citing works

AZP2006 in Progressive Supranuclear Palsy: A Multi-Centre, Randomized, Phase 2a Trial Assessing Safety and Biomarker OutcomesPreprint

Corvol, J., Obadia, M. A., Moreau, C., Mariani, L., Brandel, J., Devos, D., Sambin, S., Carrière, N., Lebouteux, M., Mangone, G., et al. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4799062

Piperazine Derivatives Attenuate Scopolamine‐Induced Memory Deficits by Modulating Neuroinflammation and Oxidative Stress via the NF‐κB/TNF‐α/COX‐2 Pathway

Fardoos, S., Kaleem, S., Masaud, S. M., Jahan, F., Nadeem, H., Afzal, M., Alrefaei, A. F., Alshehri, E., & Ali, S. (2025) · ChemistrySelect · doi:10.1002/slct.202501590

Additional file 1 of MAPT haplotype-associated transcriptomic changes in progressive supranuclear palsy

Ressler, H. W., Humphrey, J., Vialle, R. A., Babrowicz, B. M., Kandoi, S., Raj, T., Dickson, D. W., Ertekin-Taner, N., Crary, J., & Farrell, K. W. (2024) · Figshare · doi:10.6084/m9.figshare.26778049

Additional file 2 of MAPT haplotype-associated transcriptomic changes in progressive supranuclear palsy

Ressler, H. W., Humphrey, J., Vialle, R. A., Babrowicz, B. M., Kandoi, S., Raj, T., Dickson, D. W., Ertekin-Taner, N., Crary, J., & Farrell, K. W. (2024) · Figshare · doi:10.6084/m9.figshare.26778052

Toll-like receptor 9 contributes in microglial activation and lysosomal dysfunction to promote Alzheimer’s diseasePreprint

de Lavergne, M., Mazzola, L., Podsypanina, K., Estrella, C., Verwaerde, P., Evnouchidou, I., Darrasse-Jèze, G., Potier, M., Vyas, S., & Manoury, B. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.16.699962

Self-Emulsifying Formulation of Huperzia carinata Extract to Improve Huperzine A Solubility for Therapeutic Efficacy Enhancement in Parkinsonian Mice

Sermkaew, N., Songnaka, N., Masraksa, W., Jaisi, A., Yongyuen, Y., Buntha, P., Azman, N. S. N., Jomrit, J., & Boonruamkaew, P. (2026) · ACS Omega · doi:10.1021/acsomega.6c04075

AZP2006 in Parkinson’s disease models: A promising new neuroprotective treatment involving lysosomal homeostasis and the Progranulin/Prosaposin complex

Callizot, N., Culley, G. R., Flower, G., Rouvière, L., Conto, V. D., Wojcinski, A., Botto, C., Estrella, C., Henriques, A., & Verwaerde, P. (2026) · PLoS ONE · doi:10.1371/journal.pone.0359269

Effect of AZP2006, a new treatment for Alzheimer’s Disease and Progressive Supranuclear Palsy, in the Restoration of Lysosomal Homeostasis via the Progranulin‐Prosaposin Axis

Callizot, N., Estrella, C., Henriques, A., & Verwaerde, P. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.076821

Progranulin gene delivery reduces plaque burden and synaptic atrophy in a mouse model of Alzheimer's disease

Kampen, J. M. V., & Kay, D. G. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182896 · Cited by 47 · see citing works

O4‐08‐08: Progranulin gene therapy prevents plaque formation and synapse loss in a rodent model of AD

Kampen, J. M. V., & Kay, D. G. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.09.021

Progranulin protects against amyloid β deposition and toxicity in Alzheimer's disease mouse models

Minami, S. S., Min, S.-W., Krabbe, G., Wang, C., Zhou, Y., Asgarov, R., Li, Y., Martens, L. H., Elia, L. P., Ward, M. E., et al. (2014) · Nature Medicine · doi:10.1038/nm.3672 · Cited by 237 · see citing works

Progranulin as a therapeutic target in neurodegenerative diseases

Rhinn, H., Tatton, N., McCaughey, S., Kurnellas, M., & Rosenthal, A. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.11.015 · Cited by 208 · see citing works