Retromer deficiency observed in Alzheimer's disease causes hippocampal dysfunction, neurodegeneration, and Aβ accumulation

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864

Targeted gene expression as a means of altering cell fates and generating dominant phenotypes

Brand, A. H., & Perrimon, N. (1993) · Development · doi:10.1242/dev.118.2.401 · Cited by 9,510

Genome-wide atlas of gene expression in the adult mouse brain

Lein, E. S., Hawrylycz, M. J., Ao, N., Ayres, M., Bensinger, A., Bernard, A., Boe, A. F., Boguski, M. S., Brockway, K. S., Byrnes, E. J., et al. (2007) · Nature · doi:10.1038/nature05453 · Cited by 5,572

High-Level Neuronal Expression of Aβ1–42in Wild-Type Human Amyloid Protein Precursor Transgenic Mice: Synaptotoxicity without Plaque Formation

Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856

Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease

Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530

The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease

Rogaeva, E., Meng, Y., Lee, J. H., Gu, Y., Kawarai, T., Zou, F., Katayama, T., Baldwin, C. T., Cheng, R., Hasegawa, H., et al. (2007) · Nature Genetics · doi:10.1038/ng1943 · Cited by 1,167

Evolution of the neuropathology of Alzheimer's disease

Braak, H., & Braak, E. (1996) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.1996.tb05866.x · Cited by 710

Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo

Noble, W., Planel, E., Zehr, C., Olm, V., Meyerson, J., Suleman, F., Gaynor, K., Wang, L., LaFrancois, J., Feinstein, B., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500466102 · Cited by 709

Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein

Andersen, O. M., Reiche, J., Schmidt, V., Gotthardt, M., Spoelgen, R., Behlke, J., von Arnim, C. A. F., Breiderhoff, T., Jansen, P., Wu, X., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503689102 · Cited by 655

Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer

Seaman, M. N. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200312034 · Cited by 624

Genetics of Parkinson's DiseasePreprint

Klein, C., & Westenberger, A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a008888 · Cited by 1,441

VPS35 mutations in Parkinson disease

Vilariño-Güell, C., Wider, C., Ross, O. A., Dachsel, J. C., Kachergus, J. M., Lincoln, S. J., Soto-Ortolaza, A. I., Cobb, S. A., Wilhoite, G. J., Bacon, J. A., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.06.001 · Cited by 800

The endosomal-lysosomal system: from acidification and cargo sorting to neurodegeneration

Hu, Y.-B., Dammer, E. B., Ren, R., & Wang, G. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0041-1 · Cited by 710

Amyloid-β-independent regulators of tau pathology in Alzheimer disease

van der Kant, R., Goldstein, L. S. B., & Ossenkoppele, R. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-019-0240-3 · Cited by 580

Linking Aβ and Tau in Late-Onset Alzheimer's Disease: A Dual Pathway Hypothesis

Small, S. A., & Duff, K. (2008) · Neuron · doi:10.1016/j.neuron.2008.11.007 · Cited by 546

RAB7L1 Interacts with LRRK2 to Modify Intraneuronal Protein Sorting and Parkinson’s Disease Risk

MacLeod, D. A., Rhinn, H., Kuwahara, T., Zolin, A., Di Paolo, G., McCabe, B. D., Marder, K. S., Honig, L. S., Clark, L. N., Small, S. A., et al. (2013) · Neuron · doi:10.1016/j.neuron.2012.11.033 · Cited by 516

The retromer complex – endosomal protein recycling and beyond

Seaman, M. N. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.103440 · Cited by 329

Retromer: A Master Conductor of Endosome Sorting

Burd, C., & Cullen, P. J. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016774 · Cited by 435

Systems biology and gene networks in neurodevelopmental and neurodegenerative disorders

Parikshak, N. N., Gandal, M. J., & Geschwind, D. H. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3934 · Cited by 430

Amyloid precursor protein and endosomal-lysosomal dysfunction in Alzheimer's disease: inseparable partners in a multifactorial disease

Nixon, R. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700359 · Cited by 400

Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5

Seaman, M. N. J., Harbour, M. E., Tattersall, D., Read, E., & Bright, N. (2009) · Journal of Cell Science · doi:10.1242/jcs.048686 · Cited by 375

Impaired autophagy and APP processing in Alzheimer's disease: The potential role of Beclin 1 interactome

Salminen, A., Kaarniranta, K., Kauppinen, A., Ojala, J. O., Haapasalo, A., Soininen, H. S., & Hiltunen, M. O. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.06.002 · Cited by 371

Sorting nexins provide diversity for retromer-dependent trafficking events

Cullen, P. J., & Korswagen, H. C. (2012) · Nature Cell Biology · doi:10.1038/ncb2374 · Cited by 330

The Allen Brain Atlas: 5 years and beyond

Jones, A. R., Overly, C. C., & Sunkin, S. M. (2009) · Nature reviews. Neuroscience · doi:10.1038/nrn2722 · Cited by 333

Drosophila as an In Vivo Model for Human Neurodegenerative Disease

McGurk, L., Berson, A., & Bonini, N. M. (2015) · Genetics · doi:10.1534/genetics.115.179457 · Cited by 333

Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: Structures, functions and roles in disease

Teasdale, R. D., & Collins, B. M. (2012) · Biochemical Journal · doi:10.1042/bj20111226 · Cited by 281

VPS35 Deficiency or Mutation Causes Dopaminergic Neuronal Loss by Impairing Mitochondrial Fusion and Function

Tang, F., Liu, W., Hu, J.-X., Erion, J., Ye, J., Mei, L., & Xiong, W. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.08.001 · Cited by 283

VPS35 haploinsufficiency increases Alzheimer’s disease neuropathology

Wen, L., Tang, F.-L., Hong, Y., Luo, S.-W., Wang, C.-L., He, W., Shen, C., Jung, J.-U., Xiong, F., Lee, D.-H., et al. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201105109 · Cited by 270

Retromer Binds the FANSHY Sorting Motif in SorLA to Regulate Amyloid Precursor Protein Sorting and Processing

Fjorback, A. W., Seaman, M., Gustafsen, C., Mehmedbasic, A., Gokool, S., Wu, C., Militz, D., Schmidt, V., Madsen, P., Nyengaard, J. R., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.2272-11.2012 · Cited by 253

Structure, function, and regulation of mitofusin‐2 in health and disease

Chandhok, G., Lazarou, M., & Neumann, B. (2017) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12378 · Cited by 259

VPS10P-domain receptors — regulators of neuronal viability and function

Willnow, T. E., Petersen, C. M., & Nykjær, A. (2008) · Nature reviews. Neuroscience · doi:10.1038/nrn2516 · Cited by 263

Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down’s syndrome

Wang, X., Zhao, Y., Zhang, X., Badie, H., Zhou, Y., Mu, Y., Loo, L. S., Cai, L., Thompson, R. C., Yang, B., et al. (2013) · Nature Medicine · doi:10.1038/nm.3117 · Cited by 220

Retromer in Alzheimer disease, Parkinson disease and other neurological disorders

Small, S. A., & Petsko, G. A. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3896 · Cited by 227

Retromer and sorting nexins in endosomal sorting

Gallon, M., & Cullen, P. J. (2015) · Biochemical Society Transactions · doi:10.1042/bst20140290 · Cited by 244

Pharmacological chaperones stabilize retromer to limit APP processing

Mecozzi, V. J., Berman, D. E., Simoes, S., Vetanovetz, C., Awal, M. R., Patel, V. M., Schneider, R. T., Petsko, G. A., Ringe, D., & Small, S. A. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1508 · Cited by 216

Phosphatidylinositol-3-phosphate regulates sorting and processing of amyloid precursor protein through the endosomal system

Morel, E., Chamoun, Z., Lasiecka, Z. M., Chan, R. B., Williamson, R. L., Vetanovetz, C., Dall’Armi, C., Simoes, S., Point Du Jour, K. S., McCabe, B. D., et al. (2013) · Nature Communications · doi:10.1038/ncomms3250 · Cited by 222

ACAT1 gene ablation increases 24(S)-hydroxycholesterol content in the brain and ameliorates amyloid pathology in mice with AD

Bryleva, E. Y., Rogers, M. A., Chang, C. C. Y., Buen, F., Harris, B. T., Rousselet, E., Seidah, N. G., Oddo, S., LaFerla, F. M., Spencer, T. A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913828107 · Cited by 209

SNX17 protects integrins from degradation by sorting between lysosomal and recycling pathways

Steinberg, F., Heesom, K. J., Bass, M. D., & Cullen, P. J. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201111121 · Cited by 206

VPS35 dysfunction impairs lysosomal degradation of α-synuclein and exacerbates neurotoxicity in a Drosophila model of Parkinson's disease

Miura, E., Hasegawa, T., Konno, M., Suzuki, M., Sugeno, N., Fujikake, N., Geisler, S., Tabuchi, M., Oshima, R., Kikuchi, A., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.014 · Cited by 203

Neuronal ROS-Induced Glial Lipid Droplet Formation is Altered by Loss of Alzheimer's Disease-Associated Genes

Moulton, M. J., Barish, S., Ralhan, I., Chang, J., Goodman, L. D., Harland, J. G., Marcogliese, P. C., Johansson, J. O., Ioannou, M. S., & Bellen, H. J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2112095118 · Cited by 180

A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer

Gallon, M., Clairfeuille, T., Steinberg, F., Mas, C., Ghai, R., Sessions, R. B., Teasdale, R. D., Collins, B. M., & Cullen, P. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410552111 · Cited by 182

SNX–BAR proteins in phosphoinositide-mediated, tubular-based endosomal sorting

van Weering, J. R. T., Verkade, P., & Cullen, P. J. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2009.11.009 · Cited by 175

Lysosomal Sorting of Amyloid-β by the SORLA Receptor Is Impaired by a Familial Alzheimer’s Disease Mutation

Caglayan, S., Takagi-Niidome, S., Liao, F., Carlo, A.-S., Schmidt, V., Burgert, T., Kitago, Y., Füchtbauer, E.-M., Füchtbauer, A., Holtzman, D. M., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3007747 · Cited by 166

Diabetes-Associated SorCS1 Regulates Alzheimer's Amyloid-β Metabolism: Evidence for Involvement of SorL1 and the Retromer Complex

Lane, R. F., Raines, S. M., Steele, J. W., Ehrlich, M. E., Lah, J. A., Small, S. A., Tanzi, R. E., Attie, A. D., & Gandy, S. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3872-10.2010 · Cited by 143

Identification of Alzheimer disease-associated variants in genes that regulate retromer function

Vardarajan, B. N., Bruesegem, S. Y., Harbour, M. E., George-Hyslop, P. S., Seaman, M. N. J., & Farrer, L. A. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.04.020 · Cited by 142

WNT secretion and signalling in human disease

Herr, P., Hausmann, G., & Basler, K. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.06.008 · Cited by 162

Polyamine pathway contributes to the pathogenesis of Parkinson disease

Lewandowski, N. M., Ju, S., Verbitsky, M., Ross, B., Geddie, M. L., Rockenstein, E. M., Adame, A., Muhammad, A., Vonsattel, J. P., Ringe, D., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011751107 · Cited by 156

International Union of Basic and Clinical Pharmacology. LXXXIV: Leukotriene Receptor Nomenclature, Distribution, and Pathophysiological Functions

Bäck, M., Dahlén, S., Drazen, J. M., Evans, J. F., Serhan, C. N., Shimizu, T., Yokomizo, T., & Rovati, G. E. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.004184 · Cited by 160

A molecular code for endosomal recycling of phosphorylated cargos by the SNX27–retromer complex

Clairfeuille, T., Mas, C., Chan, A. S. M., Yang, Z., Tello-Lafoz, M., Chandra, M., Widagdo, J., Kerr, M. C., Paul, B., Mérida, I., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3290 · Cited by 164

Retromer-dependent neurotransmitter receptor trafficking to synapses is altered by the Parkinson's disease VPS35 mutation p.D620N

Munsie, L. N., Milnerwood, A. J., Seibler, P., Beccano-Kelly, D. A., Tatarnikov, I., Khinda, J., Volta, M., Kadgien, C., Cao, L. P., Tapia, L., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddu582 · Cited by 134

Retrieval of the Alzheimer's amyloid precursor protein from the endosome to the TGN is S655 phosphorylation state-dependent and retromer-mediated

Vieira, S. I., Rebelo, S., Esselmann, H., Wiltfang, J., Lah, J. J., Lane, R. F., Small, S. A., Gandy, S., Silva, E. F. D. C. E., & Silva, O. A. B. D. C. E. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-40 · Cited by 149

Genetics of Parkinson disease

Domingo, A., & Klein, C. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-63233-3.00014-2 · Cited by 137

The location and trafficking routes of the neuronal retromer and its role in amyloid precursor protein transport

Bhalla, A., Vetanovetz, C. P., Morel, E., Chamoun, Z., Di Paolo, G., & Small, S. A. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.030 · Cited by 130

Dysregulation of protein trafficking in neurodegeneration

Wang, X., Huang, T., Bu, G., & Xu, H. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-31 · Cited by 125

Sorting receptor SORLA – a trafficking path to avoid Alzheimer disease

Willnow, T. E., & Andersen, O. M. (2013) · Journal of Cell Science · doi:10.1242/jcs.125393 · Cited by 121

Proteogenomic analysis of human cerebrospinal fluid identifies neurologically relevant regulation and implicates causal proteins for Alzheimer’s disease

Western, D., Timsina, J., Wang, L., Wang, C., Yang, C., Phillips, B., Wang, Y., Liu, M., Ali, M., Beric, A., et al. (2024) · Nature Genetics · doi:10.1038/s41588-024-01972-8 · Cited by 111

Transgenic Drosophila models of Alzheimer’s disease and tauopathies

Iijima‐Ando, K., & Iijima, K. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0234-4 · Cited by 117

BACE1 Retrograde Trafficking Is Uniquely Regulated by the Cytoplasmic Domain of Sortilin

Finan, G. M., Okada, H., & Kim, T.-W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.170217 · Cited by 104

De novo deleterious genetic variations target a biological network centered on Aβ peptide in early-onset Alzheimer disease

Rovelet-Lecrux, A., Charbonnier, C., Wallon, D., Nicolas, G., Seaman, M. N. J., Pottier, C., Breusegem, S. Y., Mathur, P. P., Jenardhanan, P., Le Guennec, K., et al. (2015) · Molecular Psychiatry · doi:10.1038/mp.2015.100 · Cited by 106

Vacuolar protein sorting 35 (Vps35) rescues locomotor deficits and shortened lifespan in Drosophila expressing a Parkinson’s disease mutant of Leucine-rich repeat kinase 2 (LRRK2)

Linhart, R., Wong, S. A., Cao, J., Tran, M. L., Huynh, A., Ardrey, C., Park, J. M., Hsu, C., Taha, S., Peterson, R., et al. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-23 · Cited by 105

Stabilizing the retromer complex in a human stem cell model of Alzheimer’s disease reduces TAU phosphorylation independently of amyloid precursor protein

Young, J. E., Fong, L. K., Frankowski, H., Petsko, G. A., Small, S. A., & Goldstein, L. S. B. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.01.031 · Cited by 110

The Retromer Complex: From Genesis to Revelations

Seaman, M. N. J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.12.009 · Cited by 104

Can Parkinson's disease pathology be propagated from one neuron to another?

Dunning, C. J. R., Reyes, J. F., Steiner, J. A., & Brundin, P. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.11.003 · Cited by 111

Identification of molecular heterogeneity in SNX27-retromer-mediated endosome-to-plasma membrane recycling

McGough, I. J., Steinberg, F., Gallon, M., Yatsu, A., Ohbayashi, N., Heesom, K. J., Fukuda, M., & Cullen, P. J. (2014) · Journal of Cell Science · doi:10.1242/jcs.156299 · Cited by 87

Retromer disruption promotes amyloidogenic APP processing

Sullivan, C. P., Jay, A. G., Stack, E. C., Pakaluk, M., Wadlinger, E., Fine, R. E., Wells, J. M., & Morin, P. J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.04.002 · Cited by 103

A pharmacological chaperone improves memory by reducing Aβ and tau neuropathology in a mouse model with plaques and tangles

Li, J.-G., Chiu, J., Ramanjulu, M., Blass, B. E., & Praticò, D. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0350-4 · Cited by 74

The retromer supports AMPA receptor trafficking during LTP

Temkin, P., Morishita, W., Goswami, D., Arendt, K., Chen, L., & Malenka, R. (2017) · Neuron · doi:10.1016/j.neuron.2017.03.020 · Cited by 106

Endosomal sorting and trafficking, the retromer complex and neurodegeneration

Vagnozzi, A. N., & Praticò, D. (2019) · Molecular Psychiatry · doi:10.1038/s41380-018-0221-3 · Cited by 95

The VPS35 gene and Parkinson's disease

Deng, H., Gao, K., & Jankovic, J. J. (2013) · Movement Disorders · doi:10.1002/mds.25430 · Cited by 96

Bidirectional traffic between the Golgi and the endosomes – machineries and regulation

Progida, C., & Bakke, O. (2016) · Journal of Cell Science · doi:10.1242/jcs.185702 · Cited by 96

The Retromer Complex and Sorting Nexins in Neurodegenerative Diseases

Zhang, H., Huang, T. Y., Hong, Y., Yang, W., Zhang, X., Luo, H., Xu, H., & Wang, X. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00079 · Cited by 92

The synaptic maintenance problem: membrane recycling, Ca2+ homeostasis and late onset degeneration

Борисович, Б. И., & Hiesinger, P. R. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-23 · Cited by 89

β‐Site APP‐cleaving enzyme 1 trafficking and Alzheimer’s disease pathogenesis

Tan, J., & Evin, G. M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07623.x · Cited by 90

The retromer complex in development and disease

Wang, S., & Bellen, H. J. (2015) · Development · doi:10.1242/dev.123737 · Cited by 88

The retromer complex

Attar, N., & Cullen, P. J. (2009) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2009.10.002 · Cited by 86

Trafficking, a key player in regulated intramembrane proteolysis

Sannerud, R., & Annaert, W. G. (2008) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.11.004 · Cited by 86

VPS35-deficiency results in an impaired AMPA receptor trafficking and decreased dendritic spine maturation

Tian, Y., Tang, F.-L., Sun, X., Wen, L., Mei, L., Tang, B.-S., & Xiong, W.-C. (2015) · Molecular Brain · doi:10.1186/s13041-015-0156-4 · Cited by 76

Increased Microglial Activity, Impaired Adult Hippocampal Neurogenesis, and Depressive-like Behavior in Microglial VPS35-Depleted Mice

Appel, J. R., Ye, S., Tang, F., Sun, D., Zhang, H., Mei, L., & Xiong, W. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.3621-17.2018 · Cited by 86

Endo-lysosomal pathway and ubiquitin-proteasome system dysfunction in Alzheimer's disease pathogenesis

Cao, J., Zhong, M. B., Toro, C. A., Zhang, L., & Cai, D. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.03.016 · Cited by 82

Alzheimer culprits: Cellular crossroads and interplay

Claeysen, S., Cochet, M., Donneger, R., Dumuis, A., Bockaert, J., & Giannoni, P. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.05.008 · Cited by 82

Sorting Nexin 27 Regulates Aβ Production through Modulating γ-Secretase Activity

Wang, X., Huang, T., Zhao, Y., Zheng, Q., Thompson, R. C., Bu, G., Zhang, Y.-W., Hong, W., & Xu, H. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.037 · Cited by 77

The Retromer Complex Is Required for Rhodopsin Recycling and Its Loss Leads to Photoreceptor Degeneration

Wang, S., Tan, K. L., Agosto, M. A., Xiong, B., Yamamoto, S., Sandoval, H., Jaiswal, M., Bayat, V., Zhang, K., Charng, W., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001847 · Cited by 78

Vps10 Family Proteins and the Retromer Complex in Aging-Related Neurodegeneration and Diabetes

Lane, R. F., George‐Hyslop, P. S., Hempstead, B. L., Small, S. A., Strittmatter, S. M., & Gandy, S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3359-12.2012 · Cited by 78

Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane

Goold, R., McKinnon, C., Rabbanian, S., Collinge, J., Schiavo, G., & Tabrizi, S. J. (2013) · Journal of Cell Science · doi:10.1242/jcs.120477 · Cited by 82

The physical approximation of APP and BACE‐1: A key event in alzheimer's disease pathogenesis

Sun, J., & Roy, S. (2017) · Developmental Neurobiology · doi:10.1002/dneu.22556 · Cited by 78

VPS35 regulates developing mouse hippocampal neuronal morphogenesis by promoting retrograde trafficking of BACE1

Wang, C.-L., Tang, F., Peng, Y. W., Shen, C.-Y., Mei, L., & Xiong, W. (2012) · Biology Open · doi:10.1242/bio.20122451 · Cited by 77

Amyloid precursor protein traffics from the Golgi directly to early endosomes in an Arl5b‐ and AP4‐dependent pathway

Toh, W. H., Tan, J. Z. A., Zulkefli, K. L., Houghton, F. J., & Gleeson, P. A. (2017) · Traffic · doi:10.1111/tra.12465 · Cited by 75

Trafficking in Alzheimer’s Disease: Modulation of APP Transport and Processing by the Transmembrane Proteins LRP1, SorLA, SorCS1c, Sortilin, and Calsyntenin

Eggert, S., Thomas, C., Kins, S., & Hermey, G. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0806-x · Cited by 75

From endosomes to the trans-Golgi network

Lü, L., & Hong, W. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.04.024 · Cited by 81

Inhibition of TBC1D5 activates Rab7a and can enhance the function of the retromer cargo-selective complex

Seaman, M. N. J., Mukadam, A. S., & Breusegem, S. Y. (2018) · Journal of Cell Science · doi:10.1242/jcs.217398 · Cited by 79

SNX27 and SORLA Interact to Reduce Amyloidogenic Subcellular Distribution and Processing of Amyloid Precursor Protein

Huang, T. Y., Zhao, Y., Li, X., Wang, X., Tseng, I.-C., Thompson, R., Tu, S., Willnow, T. E., Zhang, Y.-W., & Xu, H. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.0206-16.2016 · Cited by 69

Physiology and Pathology of Endosome‐to‐Golgi Retrograde Sorting

Burd, C. G. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01188.x · Cited by 75

Intracellular Itinerary of Internalised β‐Secretase, BACE1, and Its Potential Impact on β‐Amyloid Peptide Biogenesis

Chia, P. Z. C., Toh, W. H., Sharples, R., Gasnereau, I., Hill, A. F., & Gleeson, P. A. (2013) · Traffic · doi:10.1111/tra.12088 · Cited by 67

Evolution and Diversity of the GolgiPreprint

Klute, M. J., Melançon, P., & Dacks, J. B. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007849 · Cited by 70

Implication of mouse Vps26b–Vps29–Vps35 retromer complex in sortilin trafficking

Kim, E., Lee, Y., Lee, H.-J., Kim, J. S., Song, B., Huh, J., Lee, S., Kim, S., Kim, S., Hong, Y., et al. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.10.121 · Cited by 69

Dysregulation of intracellular trafficking and endosomal sorting in Alzheimer's disease: controversies and unanswered questions

Toh, W. H., & Gleeson, P. A. (2016) · Biochemical Journal · doi:10.1042/bcj20160147 · Cited by 62

RAB10: an Alzheimer’s disease resilience locus and potential drug target

Tavana, J., Rosene, M., Jensen, N., Ridge, P. G., Kauwe, J. S. K., & Karch, C. M. (2018) · Clinical Interventions in Aging · doi:10.2147/cia.s159148 · Cited by 62

GGA1 regulates signal-dependent sorting of BACE1 to recycling endosomes, which moderates Aβ production

Toh, W. H., Chia, P. Z. C., Hossain, M. I., & Gleeson, P. A. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-05-0270 · Cited by 61

Retromer Ensures the Degradation of Autophagic Cargo by Maintaining Lysosome Function in Drosophila

Maruzs, T., Lőrincz, P., Szatmári, Z., Széplaki, S., Sándor, Z., Lakatos, Z., Puska, G., Juhász, G., & Sass, M. (2015) · Traffic · doi:10.1111/tra.12309 · Cited by 64

Pharmacological modulation of autophagy for Alzheimer's disease therapy: Opportunities and obstacles

Deng, Z., Dong, Y., Zhou, X., Lu, J.-H., & Yue, Z. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.12.009 · Cited by 58

The Dopamine Transporter Recycles via a Retromer-Dependent Postendocytic Mechanism: Tracking Studies Using a Novel Fluorophore-Coupling Approach

Wu, S., Fagan, R. R., Uttamapinant, C., Lifshitz, L. M., Fogarty, K. E., Ting, A. Y., & Melikian, H. E. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.3885-16.2017 · Cited by 61

VPS35 binds farnesylated N-Ras in the cytosol to regulate N-Ras trafficking

Zhou, M., Wiener, H. H., Su, W., Zhou, Y., Liot, C., Ahearn, I. M., Hancock, J. F., & Philips, M. R. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201604061 · Cited by 59

Genetic Modifiers of Age at Onset in Carriers of the G206A Mutation in PSEN1 With Familial Alzheimer Disease Among Caribbean Hispanics

Lee, J. H., Cheng, R., Vardarajan, B., Lantigua, R., Reyes-Dumeyer, D., Ortmann, W., Graham, R. R., Bhangale, T., Behrens, T. W., Medrano, M., et al. (2015) · JAMA Neurology · doi:10.1001/jamaneurol.2015.1424 · Cited by 55

Alzheimer's vulnerable brain region relies on a distinct retromer core dedicated to endosomal recycling

Simoes, S., Guo, J., Buitrago, L., Qureshi, Y. H., Feng, X., Kothiya, M., Cortes, E., Patel, V., Kannan, S., Kim, Y.-H., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110182 · Cited by 68

Assembly and fission of tubular carriers mediating protein sorting in endosomes

Gopaldass, N., Chen, K., Collins, B. M., & Mayer, A. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00746-8 · Cited by 59

Sortilins: new players in lipoprotein metabolism

Willnow, T. E., Kjølby, M., & Nykjær, A. (2010) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e3283416f2b · Cited by 54

Retromer: Structure, function, and roles in mammalian disease

Trousdale, C., & Kim, K. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.07.002 · Cited by 62

Mechanisms of AMPA Receptor Endosomal Sorting

Parkinson, G. T., & Hanley, J. G. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00440 · Cited by 57

A genetically modified minipig model for Alzheimer’s disease with SORL1 haploinsufficiency

Andersen, O. M., Bøgh, N., Landau, A. M., Pløen, G. G., Jensen, A. M. G., Monti, G., Ulhøi, B. P., Nyengaard, J. R., Jacobsen, K. R., Jørgensen, M. M., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100740 · Cited by 48

Isolating Pathogenic Mechanisms Embedded within the Hippocampal Circuit through Regional Vulnerability

Small, S. A. (2014) · Neuron · doi:10.1016/j.neuron.2014.08.030 · Cited by 55

O3‐01–03: Retromer deficiency observed in Alzheimer's disease causes hippocampal dysfunction, neurodegeneration, and Abeta accumulation

Small, S. A., Duff, K., Arancio, O., Ganetzky, B., & Honig, L. S. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.407

O2–03–04: Retromer–mutant mice model features of late–onset Alzheimer's disease

Small, S. A., Yu, R., Muhammad, A., Zhang, H., Flores, I., Planel, E., Arancio, O., Duff, K., & Honig, L. S. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.123

Retromers in Alzheimer’s Disease

Siegenthaler, B. M., & Rajendran, L. (2012) · Neurodegenerative Diseases · doi:10.1159/000335910 · Cited by 33

Retromer Sorting

Small, S. A. (2008) · Archives of Neurology · doi:10.1001/archneurol.2007.64 · Cited by 58

The Role of Retromer in Alzheimer’s Disease

Zhang, Q.-Y., Tan, M., Yu, J., & Tan, L. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9366-0 · Cited by 26