Animal models of neurodegenerative 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

α-Synuclein in Lewy bodies

Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576

Prions

Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373

Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALS

DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936 · cited 1×

A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD

Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409

Meta-Analysis of 74,046 Individuals Identifies 11 New Susceptibility Loci for Alzheimer’s Disease

(EADI), E. A. D. I., Lambert, J.-C., (GERAD), G. A. E. R. I. A. D., Alzheimer's Disease Genetic Consortium (ADGC), (CHARGE), C. F. H. A. A. R. I. G. E., Ibrahim-Verbaas, C. A., Harold, D., Naj, A. C., Sims, R., Bellenguez, C., et al. (2013) · Nature Genetics · doi:10.1038/ng.2802 · Cited by 4,336

Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation

Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126

Statistical tests, P values, confidence intervals, and power: a guide to misinterpretations

Greenland, S., Senn, S. J., Rothman, K. J., Carlin, J. B., Poole, C., Goodman, S. N., & Altman, D. G. (2016) · European Journal of Epidemiology · doi:10.1007/s10654-016-0149-3 · Cited by 3,200

Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563

Decoding ALS: from genes to mechanism

Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,120

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

A/T/N: An unbiased descriptive classification scheme for Alzheimer disease biomarkers

Jack, C. R., Bennett, D. A., Blennow, K., Carrillo, M. C., Feldman, H. H., Frisoni, G. B., Hampel, H., Jagust, W. J., Johnson, K. A., Knopman, D. S., et al. (2016) · Neurology · doi:10.1212/wnl.0000000000002923 · Cited by 1,864

Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP

Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526

ALS: A Disease of Motor Neurons and Their Nonneuronal Neighbors

Boillée, S., Velde, C. V., & Cleveland, D. W. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.018 · Cited by 1,476

Genetics of Parkinson's DiseasePreprint

Klein, C., & Westenberger, A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a008888 · Cited by 1,446

Propagation of Tau Pathology in a Model of Early Alzheimer's Disease

de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427

Alzheimer’s Disease: The Challenge of the Second Century

Holtzman, D. M., Morris, J. C., & Goate, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002369 · Cited by 1,424

Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein

Lewis, J., McGowan, E., Rockwood, J., Melrose, H., Nacharaju, P., Van Slegtenhorst, M., Gwinn-Hardy, K., Murphy, M. P., Baker, M., Yu, X., et al. (2000) · Nature Genetics · doi:10.1038/78078 · Cited by 1,371

Single App knock-in mouse models of Alzheimer’s disease

Saito, T., Matsuba, Y., Mihira, N., Takano, J., Nilsson, P., Itohara, S., Iwata, N., & Saido, T. C. (2014) · Nature Neuroscience · doi:10.1038/nn.3697 · Cited by 1,366

Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury

Reaume, A. G., Elliott, J. L., Hoffman, E. K., Kowall, N. W., Ferrante, R. J., Siwek, D. F., Wilcox, H. M., Flood, D. G., Beal, M. F., Brown, R. H., et al. (1996) · Nature Genetics · doi:10.1038/ng0596-43 · Cited by 1,285

3,4-Dihydroxyphenylalanine and 5-Hydroxytryptophan as Reserpine Antagonists

Carlsson, A., Lindqvist, M., & Magnusson, T. (1957) · Nature · doi:10.1038/1801200a0 · Cited by 1,272

Block of A1 astrocyte conversion by microglia is neuroprotective in models of Parkinson’s disease

Yun, S. P., Kam, T.-I., Panicker, N., Kim, S., Oh, Y., Park, J.-S., Kwon, S.-H., Park, Y. J., Karuppagounder, S. S., Park, H., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0051-5 · Cited by 1,123

A meta-analysis of genome-wide association studies identifies 17 new Parkinson's disease risk loci

Chang, D., Nalls, M. A., Hallgrímsdóttir, I. B., Hunkapiller, J., van der Brug, M., Cai, F., International Parkinson's Disease Genomics Consortium, 23andMe Research Team, Kerchner, G. A., Ayalon, G., et al. (2017) · Nature Genetics · doi:10.1038/ng.3955 · Cited by 1,112

TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration

Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021

Non–cell autonomous toxicity in neurodegenerative disorders: ALS and beyond

Ilieva, H., Polymenidou, M., & Cleveland, D. W. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908164 · Cited by 1,008

PARIS (ZNF746) Repression of PGC-1α Contributes to Neurodegeneration in Parkinson's Disease

Shin, J.-H., Ko, H. S., Kang, H., Lee, Y., Lee, Y.-I., Pletinkova, O., Troconso, J. C., Dawson, V. L., & Dawson, T. M. (2011) · Cell · doi:10.1016/j.cell.2011.02.010 · Cited by 953

Genetic Animal Models of Parkinson's Disease

Dawson, T. M., Ko, H. S., & Dawson, V. L. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.034 · Cited by 866

APP mouse models for Alzheimer’s disease preclinical studies.

Sasaguri, H., Nilsson, P., Hashimoto, S., Nagata, K., Saito, T., De Strooper, B., Hardy, J., Vassar, R., Winblad, B., & Saido, T. C. (2017) · The EMBO Journal · doi:10.15252/embj.201797397 · Cited by 793

Spreading of pathology in neurodegenerative diseases: a focus on human studies

Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3887 · Cited by 790

Prion-like transmission of protein aggregates in neurodegenerative diseases

Brundin, P., Melki, R., & Kopito, R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2873 · Cited by 778

The A4 Study: Stopping AD Before Symptoms Begin?

Sperling, R. A., Rentz, D. M., Johnson, K. A., Karlawish, J. H., Donohue, M., Salmon, D. P., & Aisen, P. S. S. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3007941 · Cited by 778

Clinical genetics of amyotrophic lateral sclerosis: what do we really know?

Andersen, P. M., & Al-Chalabi, A. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.150 · Cited by 687

Diagnosis and treatment of Parkinson disease: molecules to medicine

Savitt, J. M. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29178 · Cited by 660

Benefit of vitamin E, riluzole, and gababapentin in a transgenic model of familial amyotrophic lateral sclerosis

Gurney, M. E., Cutting, F. B., Zhai, P., Doble, A., Taylor, C. P., Andrus, P. K., & Hall, E. D. (1996) · Annals of Neurology · doi:10.1002/ana.410390203 · Cited by 647

Amyloid-β plaques enhance Alzheimer's brain tau-seeded pathologies by facilitating neuritic plaque tau aggregation

He, Z., Guo, J. L., McBride, J. D., Narasimhan, S., Kim, H., Changolkar, L., Zhang, B., Gathagan, R. J., Yue, C., Dengler, C., et al. (2018) · Nature Medicine · doi:10.1038/nm.4443 · Cited by 645

Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases

Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641

Propagation of Tau aggregates and neurodegeneration

Goedert, M., Eisenberg, D. S., & Crowther, R. A. (2017) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-072116-031153 · Cited by 632

An antisense oligonucleotide against SOD1 delivered intrathecally for patients with SOD1 familial amyotrophic lateral sclerosis: a phase 1, randomised, first-in-man study

Miller, T. M., Pestronk, A., David, W., Rothstein, J., Simpson, E., Appel, S. H., Andres, P. L., Mahoney, K., Allred, P., Alexander, K., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70061-9 · Cited by 617

Peripherally Applied Aβ-Containing Inoculates Induce Cerebral β-Amyloidosis

Eisele, Y. S., Obermüller, U., Heilbronner, G., Baumann, F., Kaeser, S. A., Wolburg, H., Walker, L. C., Staufenbiel, M., Heikenwalder, M., & Jucker, M. (2010) · Science · doi:10.1126/science.1194516 · Cited by 568

Haploinsufficiency leads to neurodegeneration in C9ORF72 ALS/FTD human induced motor neurons

Shi, Y., Lin, S., Staats, K. A., Li, Y., Chang, W.-H., Hung, S.-T., Hendricks, E., Linares, G. R., Wang, Y., Son, E. Y., et al. (2018) · Nature Medicine · doi:10.1038/nm.4490 · Cited by 566

Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice

McGowan, E., Pickford, F., Kim, J., Onstead, L., Eriksen, J., Yu, C., Skipper, L., Murphy, M. P., Beard, J., Das, P., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.030 · Cited by 565

C9orf72 is required for proper macrophage and microglial function in mice

O’Rourke, J. G., Bogdanik, L., Yáñez, A., Lall, D., Wolf, A. J., Muhammad, A. K. M. G., Ho, R., Carmona, S., Vit, J. P., Zarrow, J., et al. (2016) · Science · doi:10.1126/science.aaf1064 · Cited by 550

Gain of toxicity from ALS/FTD-linked repeat expansions in C9ORF72 is alleviated by antisense oligonucleotides targeting GGGGCC-containing RNAs

Jiang, J., Zhu, Q., Gendron, T. F., Saberi, S., McAlonis-Downes, M., Seelman, A., Stauffer, J. E., Jafar-nejad, P., Drenner, K., Schulte, D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.006 · Cited by 536

Parkinson’s disease: animal models and dopaminergic cell vulnerability

Blesa, J., & Przedborski, S. (2014) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2014.00155 · Cited by 515

Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms

Andorfer, C., Acker, C. M., Kress, Y., Hof, P. R., Duff, K., & Davies, P. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4637-04.2005 · Cited by 511 · cited 1×

ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43

Arnold, E. S., Ling, S., Huelga, S. C., Lagier‐Tourenne, C., Polymenidou, M., Ditsworth, D., Kordasiewicz, H. B., McAlonis‐Downes, M., Platoshyn, O., Parone, P. A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222809110 · Cited by 508

Design, power, and interpretation of studies in the standard murine model of ALS

Scott, S., Kranz, J. E., Cole, J., Lincecum, J. M., Thompson, K., Kelly, N., Bostrom, A., Theodoss, J., Al‐Nakhala, B. M., Vieira, F. G., et al. (2008) · Amyotrophic Lateral Sclerosis · doi:10.1080/17482960701856300 · Cited by 504

LRRK2 Inhibition Attenuates Microglial Inflammatory Responses

Moehle, M. S., Webber, P. J., Tse, T., Sukar, N., Standaert, D. G., DeSilva, T. M., Cowell, R. M., & West, A. B. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5601-11.2012 · Cited by 463

Recent Advances in the Genetics of Parkinson's Disease

Martin, I., Dawson, V. L., & Dawson, T. M. (2011) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-082410-101440 · Cited by 451

Tau prion strains dictate patterns of cell pathology, progression rate, and regional vulnerability in vivo

Kaufman, S. K., Sanders, D. W., Thomas, T. L., Ruchinskas, A. J., Vaquer-Alicea, J., Sharma, A. M., Miller, T. M., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.055 · Cited by 450

Drosophila as a Model for Human Neurodegenerative Disease

Bilen, J., & Bonini, N. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095804 · Cited by 431

C9ORF72 repeat expansions in mice cause TDP-43 pathology, neuronal loss, and behavioral deficits

Chew, J., Gendron, T. F., Prudencio, M., Sasaguri, H., Zhang, Y., Castanedes‐Casey, M., Lee, C. W., Jansen‐West, K. R., Kurti, A., Murray, M. E., et al. (2015) · Science · doi:10.1126/science.aaa9344 · Cited by 426

Animal Models of Alzheimer Disease

LaFerla, F. M., & Green, K. N. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006320 · Cited by 419

Probing the biology of Alzheimer’s disease in mice

Ashe, K. H., & Zahs, K. R. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.031 · Cited by 413

ALZHEIMER'S DISEASE: Genetic Studies and Transgenic Models

Price, D. L., Tanzi, R. E., Borchelt, D. R., & Sisodia, S. S. (1998) · Annual Review of Genetics · doi:10.1146/annurev.genet.32.1.461 · Cited by 406

Comparative transcriptomics in human and mouse

Breschi, A., Gingeras, T., & Guigó, R. (2017) · Nature Reviews Genetics · doi:10.1038/nrg.2017.19 · Cited by 389

The Presenilins in Alzheimer's Disease--Proteolysis Holds the Key

Haass, C., & Strooper, B. D. (1999) · Science · doi:10.1126/science.286.5441.916 · Cited by 388

Anti-Aβ Therapeutics in Alzheimer's Disease: The Need for a Paradigm Shift

Golde, T. E., Schneider, L. S., & Koo, E. H. (2011) · Neuron · doi:10.1016/j.neuron.2011.01.002 · Cited by 382

Neuropathological Staging of Brain Pathology in Sporadic Parkinson’s disease: Separating the Wheat from the Chaff

Braak, H., & Del Tredici, K. (2017) · Journal of Parkinson’s Disease · doi:10.3233/jpd-179001 · Cited by 372

TDP-43 Is a Developmentally Regulated Protein Essential for Early Embryonic Development

Sephton, C. F., Good, S. K., Atkin, S., Dewey, C. M., Mayer, P., Herz, J., & Yu, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.061846 · Cited by 370

C9orf72 BAC Mouse Model with Motor Deficits and Neurodegenerative Features of ALS/FTD

Liu, Y., Pattamatta, A., Zu, T., Reid, T. S., Bardhi, O., Borchelt, D., Yachnis, A. T., & Ranum, L. P. W. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.005 · Cited by 368

Neurodegenerative Diseases: Expanding the Prion Concept

Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361

Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis

Kraemer, B. C., Schuck, T., Wheeler, J. M., Robinson, L. C., Trojanowski, J. Q., Lee, V. M. Y., & Schellenberg, G. D. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0659-0 · Cited by 350

Functional recovery in new mouse models of ALS/FTLD after clearance of pathological cytoplasmic TDP-43

Walker, A. K., Spiller, K. J., Ge, G., Zheng, A., Xu, Y., Zhou, M. S., Tripathy, K., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1460-x · Cited by 343

Pathological Changes in Dopaminergic Nerve Cells of the Substantia Nigra and Olfactory Bulb in Mice Transgenic for Truncated Human α-Synuclein(1–120): Implications for Lewy Body Disorders

Tofaris, G. K., Garcia-Reitboeck, P., Humby, T., Lambourne, S. L., O’Connell, M. T., Ghetti, B. F., Gossage, H., Emson, P. C., Wilkinson, L. S., Goedert, M., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4965-05.2006 · Cited by 335

Inhibitors of leucine-rich repeat kinase-2 protect against models of Parkinson's disease

Lee, B. D., Shin, J.-H., VanKampen, J., Petrucelli, L., West, A. B., Ko, H. S., Lee, Y.-I., Maguire-Zeiss, K. A., Bowers, W. J., Federoff, H. J., et al. (2010) · Nature Medicine · doi:10.1038/nm.2199 · Cited by 329

C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins

Zhang, Y., Gendron, T. F., Grima, J. C., Sasaguri, H., Jansen‐West, K. R., Xu, Y.-F., Katzman, R. B., Gass, J. M., Murray, M. E., Shinohara, M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4272 · Cited by 324

Guidelines for preclinical animal research in ALS/MND: A consensus meeting

Ludolph, A. C., Bendotti, C., Blaugrund, E., Chiò, A., Greensmith, L., Loeffler, J., Mead, R. J., Niessen, H. G., Petri, S., Pradat, P., et al. (2010) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482960903545334 · Cited by 320

Cell-to-cell transmission of non-prion protein aggregates

Lee, S., Desplats, P., Sigurdson, C. J., Tsigelny, I. F., & Masliah, E. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.145 · Cited by 317

Rodent Models of Amyotrophic Lateral Sclerosis

Philips, T., & Rothstein, J. D. (2015) · Current Protocols in Pharmacology · doi:10.1002/0471141755.ph0567s69 · Cited by 311

The DIAN‐TU Next Generation Alzheimer's prevention trial: Adaptive design and disease progression model

Bateman, R. J., Benzinger, T. L., Berry, S., Clifford, D. B., Duggan, C., Fagan, A. M., Fanning, K., Farlow, M. R., Hassenstab, J., McDade, E. M., et al. (2017) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.07.005 · Cited by 303

Microglia-mediated recovery from ALS-relevant motor neuron degeneration in a mouse model of TDP-43 proteinopathy

Spiller, K. J., Restrepo, C. R., Khan, T., Dominique, M. A., Fang, T. C., Canter, R. G., Roberts, C. J., Miller, K. R., Ransohoff, R. M., Trojanowski, J. Q., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0083-7 · Cited by 301

Poly(GR) impairs protein translation and stress granule dynamics in C9orf72-associated frontotemporal dementia and amyotrophic lateral sclerosis

Zhang, Y., Gendron, T. F., Ebbert, M., O’Raw, A. D., Yue, M., Jansen‐West, K. R., Zhang, X., Prudencio, M., Chew, J., Cook, C. N., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0071-1 · Cited by 299

C9orf72 BAC Transgenic Mice Display Typical Pathologic Features of ALS/FTD

O’Rourke, J. G., Bogdanik, L., Muhammad, A. K. M. G., Gendron, T. F., Kim, K. J., Austin, A., Cady, J., Liu, E. Y., Zarrow, J., Grant, S., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.10.027 · Cited by 298

Serial propagation of distinct strains of Aβ prions from Alzheimer’s disease patients

Watts, J. C., Condello, C., Stöhr, J., Oehler, A., Lee, J., DeArmond, S. J., Lannfelt, L., Ingelsson, M., Giles, K., & Prusiner, S. B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408900111 · Cited by 291

Modeling human diseases with induced pluripotent stem cells: from 2D to 3D and beyond

Liu, C., Oikonomopoulos, A., Sayed, N., & Wu, J. C. (2018) · Development · doi:10.1242/dev.156166 · Cited by 290

TDP-43 gains function due to perturbed autoregulation in a Tardbp knock-in mouse model of ALS-FTD

White, M. A., Kim, E., Duffy, A., Adalbert, R., Phillips, B. U., Peters, O. M., Stephenson, J., Yang, S., Massenzio, F., Lin, Z., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0113-5 · Cited by 289

A decade of modeling Alzheimer's disease in transgenic mice

MCGOWAN, E., ERIKSEN, J., & HUTTON, M. (2006) · Trends in Genetics · doi:10.1016/j.tig.2006.03.007 · Cited by 287

Induction of Tau Pathology by Intracerebral Infusion of Amyloid-β-Containing Brain Extract and by Amyloid-β Deposition in APP × Tau Transgenic Mice

Bolmont, T., Clavaguera, F., Meyer-Luehmann, M., Herzig, M. C., Radde, R., Staufenbiel, M., Lewis, J., Hutton, M., Tolnay, M., & Jucker, M. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070403 · Cited by 281

Human C9ORF72 Hexanucleotide Expansion Reproduces RNA Foci and Dipeptide Repeat Proteins but Not Neurodegeneration in BAC Transgenic Mice

Peters, O. M., Cabrera, G. T., Tran, H., Gendron, T. F., McKeon, J. E., Metterville, J., Weiss, A., Wightman, N., Salameh, J. S., Kim, J., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.11.018 · Cited by 278

Absence of nigral degeneration in aged parkin/DJ‐1/PINK1 triple knockout mice

Kitada, T., Tong, Y., Gautier, C., & Shen, J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06350.x · Cited by 271

Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments

Swarup, V., Phaneuf, D., Bareil, C., Robertson, J., Rouleau, G. A., Križ, J., & Julien, J. (2011) · Brain · doi:10.1093/brain/awr159 · Cited by 270

Loss-of-function mutations in the C9ORF72 mouse ortholog cause fatal autoimmune disease

Burberry, A., Suzuki, N., Wang, J.-Y., Moccia, R., Mordes, D. A., Stewart, M. H., Suzuki-Uematsu, S., Ghosh, S., Singh, A., Merkle, F. T., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf6038 · Cited by 269

Tau Pathology Induces Excitatory Neuron Loss, Grid Cell Dysfunction, and Spatial Memory Deficits Reminiscent of Early Alzheimer’s Disease

Fu, H., Rodriguez, G. A., Herman, M., Emrani, S., Nahmani, E., Barrett, G., Figueroa, H. Y., Goldberg, E., Hussaini, S. A., & Duff, K. E. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.023 · Cited by 264

C9orf72 ablation causes immune dysregulation characterized by leukocyte expansion, autoantibody production and glomerulonephropathy in mice

Atanasio, A., Decman, V., White, D., Ramos, M., Ikiz, B., Lee, H.-C., Siao, C.-J., Brydges, S., LaRosa, E., Bai, Y., et al. (2016) · Scientific Reports · doi:10.1038/srep23204 · Cited by 263

TDP‐43, a neuro‐pathosignature factor, is essential for early mouse embryogenesis

Wu, L., Cheng, W., Hou, S., Yan, Y., Jiang, S., & Shen, C. ‐. J. (2010) · genesis · doi:10.1002/dvg.20584 · Cited by 256

Animal models of α-synucleinopathy for Parkinson disease drug development

Koprich, J. B., Kalia, L. V., & Brotchie, J. M. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.75 · Cited by 241

Mammalian prions and their wider relevance in neurodegenerative diseases

Collinge, J. (2016) · Nature · doi:10.1038/nature20415 · Cited by 238

Drosophila melanogaster as a model organism for Alzheimer’s disease

Prüßing, K., Voigt, A., & Schulz, J. B. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-35 · Cited by 235

Mechanisms of Protein Seeding in Neurodegenerative Diseases

Walker, L. C., Diamond, M. I., Duff, K. E., & Hyman, B. T. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.1453 · Cited by 226

PINK1 Primes Parkin-Mediated Ubiquitination of PARIS in Dopaminergic Neuronal Survival

Lee, Y., Stevens, D. A., Kang, S.-U., Jiang, H., Lee, Y.-I., Ko, H. S., Scarffe, L. A., Umanah, G. K. E., Kang, H., Ham, S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.090 · Cited by 214

Parthanatos mediates AIMP2-activated age-dependent dopaminergic neuronal loss

Lee, Y., Karuppagounder, S. S., Shin, J.-H., Lee, Y.-I., Ko, H. S., Swing, D., Jiang, H., Kang, S.-U., Lee, B. D., Kang, H. C., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3500 · Cited by 214

Treatment with edaravone, initiated at symptom onset, slows motor decline and decreases SOD1 deposition in ALS mice

Ito, H., Wate, R., Zhang, J., Ohnishi, S., Kaneko, S., Ito, H., Nakano, S., & Kusaka, H. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.07.017 · Cited by 205

Animal models of Parkinson's disease: Limits and relevance to neuroprotection studies

Bézard, E., Yue, Z., Kirik, D., & Spillantini, M. G. (2012) · Movement Disorders · doi:10.1002/mds.25108 · Cited by 193

Conditional Expression of Parkinson's Disease-Related Mutant -Synuclein in the Midbrain Dopaminergic Neurons Causes Progressive Neurodegeneration and Degradation of Transcription Factor Nuclear Receptor Related 1

Lin, X. Z., Parisiadou, L., Sgobio, C., Liu, G., Yu, J. H., Sun, L., Shim, H., Gu, X., Luo, J., Long, C., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1731-12.2012 · Cited by 192

Bacterial Artificial Chromosome Transgenic Mice Expressing a Truncated Mutant Parkin Exhibit Age-Dependent Hypokinetic Motor Deficits, Dopaminergic Neuron Degeneration, and Accumulation of Proteinase K-Resistant α-Synuclein

Lu, X., Fleming, S. M., Meurers, B. H., Ackerson, L. C., Mortazavi, F., Lo, V., Hernandez, D., Sulzer, D., Jackson, G. R., Maidment, N. T., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5351-08.2009 · Cited by 181

α-Synuclein-Based Animal Models of Parkinson's Disease: Challenges and Opportunities in a New Era

Visanji, N. P., Brotchie, J. M., Kalia, L. V., Koprich, J. B., Tandon, A., Watts, J. C., & Lang, A. E. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.09.003 · Cited by 174

Evaluation of Potential Infectivity of Alzheimer and Parkinson Disease Proteins in Recipients of Cadaver-Derived Human Growth Hormone

Irwin, D. J., Abrams, J. Y., Schonberger, L. B., Leschek, E., Mills, J. L., Lee, V. M. ‐., & Trojanowski, J. Q. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.1933 · Cited by 172

Nonhuman Primate Models of Alzheimer-Like Cerebral Proteopathy

Heuer, E., F. Rosen, R., Cintron, A., & C. Walker, L. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799315885 · Cited by 169

Modelling neurodegenerative diseases in Drosophila: a fruitful approach?

Muqit, M. M. K., & Feany, M. Β. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn751 · Cited by 168

From animal models to human disease: a genetic approach for personalized medicine in ALS

Picher‐Martel, V., Valdmanis, P. N., Gould, P. V., Julien, J., & Dupré, N. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0340-5 · Cited by 163

Alzheimer's Prevention Initiative: A Proposal to Evaluate Presymptomatic Treatments as Quickly as Possible

Reiman, E. M., Langbaum, J. B. S., & Tariot, P. N. (2010) · Biomarkers in Medicine · doi:10.2217/bmm.09.91 · Cited by 160

Animal models of the non-motor features of Parkinson's disease

McDowell, K. A., & Chesselet, M. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.040 · Cited by 158

Toward more predictive genetic mouse models of Alzheimer’s disease

Onos, K. D., Sukoff Rizzo, S. J., Howell, G. R., & Sasner, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2015.12.003 · Cited by 156

Pathogenesis of FUS-associated ALS and FTD: insights from rodent models

Nolan, M., Talbot, K., & Ansorge, O. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0358-8 · Cited by 151

The genetic landscape of Alzheimer disease

Carmona, S., Hardy, J., & Guerreiro, R. J. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-64076-5.00026-0 · Cited by 140

Tau: From research to clinical development

Holtzman, D. M., Carrillo, M. C., Hendrix, J. A., Bain, L. J., Catafau, A. M., Gault, L. M., Goedert, M., Mandelkow, E., Mandelkow, E., Miller, D. S., et al. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.03.018 · Cited by 139

Spinal poly-GA inclusions in a C9orf72 mouse model trigger motor deficits and inflammation without neuron loss

Schludi, M. H., Becker, L., Garrett, L., Gendron, T. F., Zhou, Q., Schreiber, F., Popper, B., Dimou, L., Strom, T. M., Winkelmann, J., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1711-0 · Cited by 137

Motor neuron intrinsic and extrinsic mechanisms contribute to the pathogenesis of FUS-associated amyotrophic lateral sclerosis

Scekic‐Zahirovic, J., Oussini, H. E., Mersmann, S., Drenner, K., Wagner, M., Sun, Y., Allmeroth, K., Dieterle, S., Sinniger, J., Dirrig‐Grosch, S., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1687-9 · Cited by 135

Animal Models of Parkinson's Disease: Vertebrate GeneticsPreprint

Lee, Y., Dawson, V. L., & Dawson, T. M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009324 · Cited by 134

The prion model for progression and diversity of neurodegenerative diseases

Stopschinski, B. E., & Diamond, M. I. (2017) · The Lancet Neurology · doi:10.1016/s1474-4422(17)30037-6 · Cited by 133

Age-Dependent Dopaminergic Neurodegeneration and Impairment of the Autophagy-Lysosomal Pathway in LRRK-Deficient Mice

Giaime, E., Tong, Y., Wagner, L. K., Yang, Y. H., Huang, G., & Shen, J. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.036 · Cited by 132

Mouse models of ALS: Past, present and future

Lutz, C. M. (2018) · Brain Research · doi:10.1016/j.brainres.2018.03.024 · Cited by 129

Thinking laterally about neurodegenerative proteinopathies

Golde, T. E., Borchelt, D., Giasson, B. I., & Lewis, J. M. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66029 · Cited by 126

Modeling neurodegenerative diseases in Caenorhabditis elegans

Li, J., & Le, W. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.09.024 · Cited by 125

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. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815357 · Cited by 124

Four pioneers of L‐dopa treatment: Arvid Carlsson, Oleh Hornykiewicz, George Cotzias, and Melvin Yahr

Lees, A. J., TOLOSA, E. S., & Olanow, C. W. (2014) · Movement Disorders · doi:10.1002/mds.26120 · Cited by 119

Humanized mutant FUS drives progressive motor neuron degeneration without aggregation in ‘FUSDelta14’ knockin mice

Devoy, A., Kalmár, B., Stewart, M. E., Park, H., Burke, B., Noy, S., Redhead, Y. T., Humphrey, J., Lo, K., Jaeger, J., et al. (2017) · Brain · doi:10.1093/brain/awx248 · Cited by 117

Genetic risk for Alzheimer’s disease is concentrated in specific macrophage and microglial transcriptional networks

Tansey, K. E., Cameron, D., & Hill, M. J. (2018) · Genome Medicine · doi:10.1186/s13073-018-0523-8 · Cited by 115

Mutant PFN1 causes ALS phenotypes and progressive motor neuron degeneration in mice by a gain of toxicity

Yang, C., Danielson, E., Qiao, T., Metterville, J., Brown, R. H., Landers, J. E., & Xu, Z. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605964113 · Cited by 111

Neuronal Structure is Altered by Amyloid Plaques

Spires‐Jones, T. L., & Hyman, B. T. (2004) · Reviews in the Neurosciences · doi:10.1515/revneuro.2004.15.4.267 · Cited by 108

Protein folding diseases and neurodegeneration: Lessons learned from yeast

Winderickx, J., Delay, C., Vos, A. D., Klinger, H., Pellens, K., Vanhelmont, T., LEUVEN, F. V., & Zabrocki, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.020 · Cited by 108

Invertebrate models of Alzheimer's disease

Link, C. D. (2004) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2004.00105.x · Cited by 99

Motor neuron disease, TDP-43 pathology, and memory deficits in mice expressing ALS–FTD-linked UBQLN2 mutations

Le, N. T. T., Chang, L., Kovlyagina, I., Georgiou, P., Safren, N., Braunstein, K. E., Kvarta, M. D., Dyke, A. M. V., LeGates, T. A., Philips, T., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608432113 · Cited by 96

Robust kinase- and age-dependent dopaminergic and norepinephrine neurodegeneration in LRRK2 G2019S transgenic mice

Xiong, Y., Neifert, S., Karuppagounder, S. S., Liu, Q., Stankowski, J. N., Lee, B. D., Ko, H. S., Lee, Y., Grima, J. C., Mao, X., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1712648115 · Cited by 95

Analysis of tauopathies with transgenic mice

Hutton, M., Lewis, J., Dickson, D., Yen, S.-H., & McGowan, E. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02123-2 · Cited by 91

Mutant Profilin1 transgenic mice recapitulate cardinal features of motor neuron disease

Fil, D., DeLoach, A., Yadav, S., Alkam, D., MacNicol, M. C., Singh, A., Compadre, C. M., Goellner, J. J., O’Brien, C. A., Fahmi, T., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw429 · Cited by 88

Normal cognition in transgenic BRI2-Aβ mice

Kim, J., Chakrabarty, P., Hanna, A., March, A., Dickson, D. W., Borchelt, D. R., Golde, T., & Janus, C. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-15 · Cited by 83

Models of LRRK2-Associated Parkinson’s Disease

Xiong, Y., Dawson, T. M., & Dawson, V. L. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-49969-7_9 · Cited by 83

Viral Vector-Based Models of Parkinson’s Disease

der Perren, A. V., den Haute, C. V., & Baekelandt, V. (2014) · Current topics in behavioral neurosciences · doi:10.1007/7854_2014_310 · Cited by 74

Challenges in detecting disease modification in Parkinson's disease clinical trials

Athauda, D. S., & Foltynie, T. (2016) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2016.07.019 · Cited by 73

Trumping neurodegeneration: Targeting common pathways regulated by autosomal recessive Parkinson's disease genes

Scott, L., Dawson, V. L., & Dawson, T. M. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.04.008 · Cited by 72

FTD and ALS—translating mouse studies into clinical trials

Ittner, L. M., Halliday, G. M., Kril, J. J., Götz, J., Hodges, J. R., & Kiernan, M. C. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.65 · Cited by 70

LRRK2 mouse models: dissecting the behavior, striatal neurochemistry and neurophysiology of PD pathogenesis

Volta, M., & Melrose, H. L. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160238 · Cited by 63

Are rodent models of Parkinson’s disease behaving as they should?

Vingill, S., Connor‐Robson, N., & Wade‐Martins, R. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.10.021 · Cited by 63

Adenoviral-mediated expression of G2019S LRRK2 induces striatal pathology in a kinase-dependent manner in a rat model of Parkinson's disease

Tsika, E., Nguyen, A. P. T., Dusonchet, J., Colin, P., Schneider, B. L., & Moore, D. J. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.019 · Cited by 49

Pathogenic determinants and mechanisms of ALS/FTD linked to hexanucleotide repeat expansions in the C9orf72 gene

Wen, X., Westergard, T., Pasinelli, P., & Trotti, D. (2016) · Neuroscience Letters · doi:10.1016/j.neulet.2016.09.007 · Cited by 45

Transgenic Rodent Models to Study Alpha-Synuclein Pathogenesis, with a Focus on Cognitive Deficits

Hatami, A., & Chesselet, M. (2014) · Current topics in behavioral neurosciences · doi:10.1007/7854_2014_355 · Cited by 42

Of mice and CRISPR

Liu, E. T., Bolcun‐Filas, E., Grass, D., Lutz, C. M., Murray, S., Shultz, L., & Rosenthal, N. A. (2017) · EMBO Reports · doi:10.15252/embr.201643717 · Cited by 41

Simple, Efficient CRISPR-Cas9-Mediated Gene Editing in Mice: Strategies and Methods

Low, B. E., Kutny, P. M., & Wiles, M. V. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3661-8_2 · Cited by 38

Clinical approaches to the development of a neuroprotective therapy for PD

Olanow, C. W., Kieburtz, K. D., & Katz, R. G. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.06.018 · Cited by 38

Clinical Trial Designs in Amyotrophic Lateral Sclerosis: Does One Design Fit All?

Nicholson, K. A., Cudkowicz, M., & Berry, J. D. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0341-2 · Cited by 37

Mouse models of frontotemporal dementia: A comparison of phenotypes with clinical symptomatology

Ahmed, R. M., Irish, M., van Eersel, J., Ittner, A., Ke, Y. D., Volkerling, A. M., van der Hoven, J., Tanaka, K., Karl, T., Kassiou, M., et al. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2017.01.004 · Cited by 34

Non-prion-type transmission in A53T α-synuclein transgenic mice: a normal component of spinal homogenates from naïve non-transgenic mice induces robust α-synuclein pathology

Sacino, A. N., Ayers, J. I., Brooks, M., Chakrabarty, P., Hudson, V. J., Howard, J. K., Golde, T. E., Giasson, B. I., & Borchelt, D. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1505-1 · Cited by 23

Modeling LRRK2 Pathobiology in Parkinson’s Disease: From Yeast to Rodents

Daniel, G., & Moore, D. J. (2014) · Current topics in behavioral neurosciences · doi:10.1007/7854_2014_311 · Cited by 19

Predicting success: Optimizing phase II ALS trials for the transition to phase III

Berry, J. D., Cudkowicz, M., & Shefner, J. M. (2014) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.3109/21678421.2013.838969 · Cited by 14

Insights into LRRK2 function and dysfunction from transgenic and knockout rodent models

Sloan, M., Alegre‐Abarrategui, J., & Wade‐Martins, R. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120151 · Cited by 12

Alzheimer disease

Knopman, D. S., Amieva, H., Petersen, R. C., Chételat, G., Holtzman, D. M., Hyman, B. T., Nixon, R. A., & Jones, D. T. (2021) · Nature Reviews Disease Primers · doi:10.1038/s41572-021-00269-y · Cited by 2,606

The gut microbiota–brain axis in behaviour and brain disorders

Morais, L. H., Schreiber, H. L., & Mazmanian, S. K. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00460-0 · Cited by 2,149

Development of a Chimeric Model to Study and Manipulate Human Microglia In Vivo

Hasselmann, J., Coburn, M. A., England, W., Figueroa Velez, D. X., Kiani Shabestari, S., Tu, C. H., McQuade, A., Kolahdouzan, M., Echeverria, K., Claes, C., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.07.002 · Cited by 380

Microglia: Agents of the CNS Pro-Inflammatory Response

Rodríguez-Gómez, J. A., Kavanagh, E., Engskog-Vlachos, P., Engskog, M. K. R., Herrera, A. J., Espinosa-Oliva, A. M., Joseph, B., Hajji, N., Venero, J. L., & Burguillos, M. A. (2020) · Cells · doi:10.3390/cells9071717 · Cited by 365

Immune Signaling in Neurodegeneration

Hammond, T. R., Marsh, S. E., & Stevens, B. (2019) · Immunity · doi:10.1016/j.immuni.2019.03.016 · Cited by 336

Advancement in the animal model-based therapeutics in neurodegenerative diseases

Pal, D., Das, P., Ghosh, P., Gupta, S., Basak, P., & Nandi, S. K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-33877-9.00007-0 · Cited by 1

Transgenic animal models of neurodegeneration based on human genetic studies

Harvey, B. K., Richie, C. T., Hoffer, B. J., & Airavaara, M. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0476-6 · Cited by 38

Animal and Cell Models in Alzheimer’s and Parkinson’s Disease: Current Innovations Reviewed

Rejitha, C., & Babu, L. (2026) · Current Aging Science · doi:10.2174/0118746098403535251203121022 · Cited by 1

Progress in the modeling of neurodegenerative diseases in transgenic mice

Duff, K., & Rao, M. V. (2001) · Current Opinion in Neurology · doi:10.1097/00019052-200108000-00003 · Cited by 22

Animal models of Alzheimer's Parkinson's and Huntington's disease. A minireview.

Antal, A., & Bodis-Wollner, I. G. (1993) · PubMed