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Welsch, T., Endlich, N., Gökce, G., Doroshenko, E., Simpson, J. C., Kriz, W., Shaw, A. S., & Endlich, K. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00178.2005 · Cited by 54 · see citing works

Synapsin Regulates Activity-Dependent Outgrowth of Synaptic Boutons at the Drosophila Neuromuscular Junction

Васин, А. И., Zueva, L. V., Torrez, C., Volfson, D., Littleton, J. T., & Bykhovskaia, M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.5074-13.2014 · Cited by 54 · see citing works

Effects of CD2-associated protein deficiency on amyloid-β in neuroblastoma cells and in an APP transgenic mouse model

Liao, F., Jiang, H., Srivatsan, S., Xiao, Q., Lefton, K. B., Yamada, K., Mahan, T. E., Lee, J.-M., Shaw, A. S., & Holtzman, D. M. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0006-y · Cited by 53 · see citing works

Dimerization Is Essential for 14-3-3ζ Stability and Function in Vivo

Messaritou, G., Grammenoudi, S., & Skoulakis, E. M. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.045989 · Cited by 52 · see citing works

Drosophila twinfilin is required for cell migration and synaptic endocytosis

Wang, D., Zhang, L., Zhao, G., Wahlström, G., Heino, T. I., Chen, J., & Zhang, Y. (2010) · Journal of Cell Science · doi:10.1242/jcs.060251 · Cited by 51 · see citing works

The Alzheimer's disease risk factor CD2AP maintains blood–brain barrier integrity

Cochran, J. N., Rush, T., Buckingham, S. C., & Roberson, E. D. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv371 · Cited by 50 · see citing works

CD2AP/SHIP1 Complex Positively Regulates Plasmacytoid Dendritic Cell Receptor Signaling by Inhibiting the E3 Ubiquitin Ligase Cbl

Bao, M., Hanabuchi, S., Facchinetti, V., Du, Q., Bover, L., Plumas, J., Chaperot, L., Cao, W., Qin, J., Sun, S.-C., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200887 · Cited by 49 · see citing works

Mechanisms of tau and Aβ-induced excitotoxicity

Pallo, S. P., DiMaio, J., Cook, A., Nilsson, B., & Johnson, G. V. W. (2016) · Brain Research · doi:10.1016/j.brainres.2015.12.048 · Cited by 46 · see citing works

Overexpression of 14-3-3ζ Promotes Tau Phosphorylation at Ser262 and Accelerates Proteosomal Degradation of Synaptophysin in Rat Primary Hippocampal Neurons

Qureshi, H. Y., Han, D. C., MacDonald, R., & Paudel, H. K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0084615 · Cited by 44 · see citing works

The Ubiquitin–Proteasome System Is Necessary for Long-Term Synaptic Depression inAplysia

Fioravante, D., Liu, R.-Y., & Byrne, J. H. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2139-08.2008 · Cited by 43 · see citing works

A Drosophila model system to assess the function of human monogenic podocyte mutations that cause nephrotic syndrome

Fu, Y., Zhu, J., Richman, A., Zhao, Z., Zhang, F., Ray, P. E., & Han, Z. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddw428 · Cited by 43 · see citing works

Calmodulin antagonizes amyloid-β peptides-mediated inhibition of brain plasma membrane Ca2+-ATPase

Berrocal, M., Sepúlveda, M. R., Vázquez-Hernández, M., & Mata, A. M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.02.013 · Cited by 41 · see citing works

The Adaptor Protein CD2AP Is a Coordinator of Neurotrophin Signaling-Mediated Axon Arbor Plasticity

Harrison, B. J., Venkat, G., Lamb, J. L., Hutson, T. H., Drury, C., Rau, K. K., Bunge, M. B., Mendell, L. M., Gage, F. H., Johnson, R. D., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2423-15.2016 · Cited by 40 · see citing works

The Krebs Cycle Enzyme Isocitrate Dehydrogenase 3A Couples Mitochondrial Metabolism to Synaptic Transmission

Uğur, B., Bao, H., Stawarski, M., Duraine, L., Zuo, Z., Qi, L. Y., Neely, G. G., Macleod, G. T., Chapman, E. R., & Bellen, H. J. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.12.005 · Cited by 40 · see citing works

New Approaches for Studying Synaptic Development, Function, and Plasticity UsingDrosophilaas a Model System

Frank, C. A., Wang, X., Collins, C. A., Rodal, A. A., Yuan, Q., Verstreken, P., & Dickman, D. K. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3261-13.2013 · Cited by 36 · see citing works

Differential interaction and aggregation of 3-repeat and 4-repeat tau isoforms with 14-3-3ζ protein

Sadik, G., Tanaka, T., Kato, K., Yanagi, K., Kudo, T., & Takeda, M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.107 · Cited by 33 · see citing works

Cortactin Is a Regulator of Activity-Dependent Synaptic Plasticity Controlled by Wingless

Alicea, D. A., Perez, M., Maldonado‐Díaz, C., Dominicci-Cotto, C., & Marie, B. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1375-16.2017 · Cited by 33 · see citing works

Genetic meta-analysis identifies 9 novel loci and functional pathways for Alzheimer’s disease riskPreprint

Jansen, I. E., Savage, J. E., Watanabe, K., Bryois, J., Williams, D. M., Steinberg, S., Sealock, J., Karlsson, I., Hägg, S., Athanasiu, L., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/258533 · Cited by 33 · see citing works

Plasma Membrane Calcium ATPase Activity Is Regulated by Actin Oligomers through Direct Interaction

Dalghi, M. G., Fernández, M. M., Ferreira-Gomes, M., Mangialavori, I. C., Malchiodi, E. L., Strehler, E. E., & Rossi, J. P. F. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470542 · Cited by 32 · see citing works

Role for a Cindr–Arf6 axis in patterning emerging epithelia

Johnson, R. I., Sedgwick, A., D’Souza‐Schorey, C., & Cagan, R. L. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-04-0305 · Cited by 32 · see citing works

CD2AP and Cbl-3/Cbl-c Constitute a Critical Checkpoint in the Regulation of Ret Signal Transduction

Tsui, C. C., & Pierchala, B. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2738-08.2008 · Cited by 28 · see citing works

The role of Plasma Membrane Calcium ATPases (PMCAs) in neurodegenerative disorders

Hajieva, P., Baeken, M. W., & Moosmann, B. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2017.09.033 · Cited by 27 · see citing works

Impairment of the activity of the plasma membrane Ca2+-ATPase in Alzheimer's disease

Mata, A. M., Berrocal, M., & Sepúlveda, M. R. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390819 · Cited by 23 · see citing works

14-3-3ζ binds the proteasome, limits proteolytic function and enhances sensitivity to proteasome inhibitors

Gu, Y., Xu, K., Torre, C., Samur, M., Barwick, B. G., Rupji, M., Arora, J., Neri, P. E., Kaufman, J. L., Nooka, A. K., et al. (2017) · Leukemia · doi:10.1038/leu.2017.288 · Cited by 18 · see citing works

Interactions between Drosophila IgCAM adhesion receptors and cindr, the Cd2ap/Cin85 ortholog

Johnson, R. I., Bao, S., & Cagan, R. L. (2012) · Developmental Dynamics · doi:10.1002/dvdy.23879 · Cited by 17 · see citing works

CD2-associated Protein (CD2AP) Enhances Casitas B Lineage Lymphoma-3/c (Cbl-3/c)-mediated Ret Isoform-specific Ubiquitination and Degradation via Its Amino-terminal Src Homology 3 Domains

Calco, G. N., Stephens, O. R., Donahue, L. M., Tsui, C. C., & Pierchala, B. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.537878 · Cited by 12 · see citing works

Adaptor protein complex of FRS 2β and CIN 85/ CD 2 AP provides a novel mechanism for ErbB2/ HER 2 protein downregulation

Minegishi, Y., Shibagaki, Y., Mizutani, A., Fujita, K., Tezuka, T., Kinoshita, M., Kuroda, M., Hattori, S., & Gotoh, N. (2012) · Cancer Science · doi:10.1111/cas.12086 · Cited by 7 · see citing works

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 · see citing works

Synaptic tau: A pathological or physiological phenomenon?

Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01246-y · Cited by 117 · see citing works

Promiscuous Roles of Autophagy and Proteasome in Neurodegenerative Proteinopathies

Limanaqi, F., Biagioni, F., Gambardella, S., Familiari, P., Frati, A., & Fornai, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21083028 · Cited by 93 · see citing works

Apolipoprotein E4 and meningeal lymphatics in Alzheimer disease: a conceptual framework

Mentis, A. A., Dardiotis, E., & Chrousos, G. P. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-0731-7 · Cited by 82 · see citing works

Intracellular Trafficking Mechanisms of Synaptic Dysfunction in Alzheimer’s Disease

Perdigão, C., Barata, M. A., Araújo, M. N. C. D. F., Mirfakhar, F. S., Castanheira, J., & Almeida, C. G. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00072 · Cited by 63 · see citing works

Multi-tissue neocortical transcriptome-wide association study implicates 8 genes across 6 genomic loci in Alzheimer’s disease

Gockley, J., Montgomery, K. S., Poehlman, W. L., Wiley, J. C., Liu, Y., Gerasimov, E. S., Greenwood, A. K., Sieberts, S. K., Wingo, A. P., Wingo, T. S., et al. (2021) · Genome Medicine · doi:10.1186/s13073-021-00890-2 · Cited by 60 · see citing works

Retromer subunit, VPS29, regulates synaptic transmission and is required for endolysosomal function in the aging brain

Ye, H., Ojelade, S. A., Li‐Kroeger, D., Zuo, Z., Wang, L., Li, Y., Gu, J. Y. J., Tepaß, U., Rodal, A. A., Bellen, H. J., et al. (2020) · eLife · doi:10.7554/elife.51977 · Cited by 52 · see citing works

The role of genetic risk factors of Alzheimer’s disease in synaptic dysfunction

Fu, W.-Y., & Ip, N. Y. (2023) · Seminars in Cell &amp; Developmental Biology · doi:10.1016/j.semcdb.2022.07.011 · Cited by 48 · see citing works

Mechanisms of neuronal survival safeguarded by endocytosis and autophagy

Overhoff, M., Bruyckere, E. D., & Kononenko, N. L. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15194 · Cited by 38 · see citing works

γ-secretase promotes Drosophila postsynaptic development through the cleavage of a Wnt receptor

Restrepo, L. J., DePew, A. T., Moese, E. R., Tymanskyj, S. R., Parisi, M. J., Aimino, M. A., Duhart, J. C., Fei, H., & Mosca, T. J. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.05.006 · Cited by 26 · see citing works

Functional variants identify sex-specific genes and pathways in Alzheimer’s Disease

Bourquard, T., Lee, K. D., Al‐Ramahi, I., Pham, M., Shapiro, D., Lagisetty, Y., Soleimani, S., Mota, S., Wilhelm, K. O., Samieinasab, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38374-z · Cited by 27 · see citing works

Proteostasis-associated aging: lessons from a Drosophila model

Yu, G., & Hyun, S. (2020) · Genes & Genomics · doi:10.1007/s13258-020-01012-9 · Cited by 29 · see citing works

Pyk2 overexpression in postsynaptic neurons blocks amyloid β1–42-induced synaptotoxicity in microfluidic co-cultures

Kilinc, D., Vreulx, A.-C., Mendes, T., Flaig, A., Coelho, D. M., Verschoore, M., Demiautte, F., Amouyel, P., Bank, N.-C. B., Eysert, F., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa139 · Cited by 27 · see citing works

Distinct systemic impacts of Aβ42 and Tau revealed by whole-organism snRNA-seq

Park, Y.-J., Lu, T., Jackson, T., Goodman, L. D., Ran, L., Chen, J., Liang, C., Harrison, E. M., Ko, C., Chen, X. X., et al. (2024) · Neuron · doi:10.1016/j.neuron.2025.04.017 · Cited by 25 · see citing works

Association of CD2AP neuronal deposits with Braak neurofibrillary stage in Alzheimer’s disease

Camacho, J., Rábano, A., Marazuela, P., Bonaterra‐Pastra, A., Serna, G., Moliné, T., y Cajal, S. R., Martínez-Sáez, E. A., & Hernández‐Guillamón, M. (2021) · Brain Pathology · doi:10.1111/bpa.13016 · Cited by 23 · see citing works

Cell type-specific functions of Alzheimer's disease endocytic risk genes

Maninger, J., Nowak, K., Goberdhan, S., O’Donoghue, R., & Connor‐Robson, N. (2024) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2022.0378 · Cited by 21 · see citing works

CD2AP deficiency aggravates Alzheimer’s disease phenotypes and pathology through p38 MAPK activation

Xue, Y., Zhang, Z.-S., Lin, R.-R., Huang, H.-F., Zhu, K., Chen, D.-F., Wu, Z., & Tao, Q. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00454-5 · Cited by 20 · see citing works

Simple model systems reveal conserved mechanisms of Alzheimer’s disease and related tauopathies

Jiang, Y., & MacNeil, L. T. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00664-x · Cited by 20 · see citing works

Biomarker identification for Alzheimer’s disease through integration of comprehensive Mendelian randomization and proteomics data

Zhan, H., Cammann, D., Cummings, J. L., Dong, X., & Chen, J. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06317-5 · Cited by 17 · see citing works

Microglial CD2AP deficiency exerts protection in an Alzheimer’s disease model of amyloidosis

Zhang, L., Huang, L., Zhou, Y., Meng, J., Zhang, L., Zhou, Y., Zheng, N., Guo, T., Zhao, S., Wang, Z., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00789-7 · Cited by 13 · see citing works

The relationship of early- and late-onset Alzheimer’s disease genes with COVID-19

Şirin, S., Dolanbay, S. N., & Aslım, B. (2022) · Journal of Neural Transmission · doi:10.1007/s00702-022-02499-0 · Cited by 13 · see citing works

From bugs to bedside: functional annotation of human genetic variation for neurological disorders using invertebrate models

Mew, M., Caldwell, K. A., & Caldwell, G. A. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac203 · Cited by 13 · see citing works

ALS2 regulates endosomal trafficking, postsynaptic development, and neuronal survival

Kim, J., Kim, S. D., Nahm, M., Li, T.-N., Lin, H.-C., Kim, Y. D., Lee, J., Yao, C., & Lee, S. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202007112 · Cited by 12 · see citing works

Alzheimer’s disease risk gene CD2AP is a dose-sensitive determinant of synaptic structure and plasticity

Pavešković, M., De-Paula, R. B., Ojelade, S. A., Tantry, E. K., Kochukov, M. Y., Bao, S., Veeraragavan, S., Garza, A. R., Srivastava, S., Song, S., et al. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae115 · Cited by 11 · see citing works

The Alzheimer's Disease Risk Gene CD2AP Functions in Dendritic Spines by Remodeling F-Actin

Mirfakhar, F. S., Castanheira, J., Domingues, R., Ramalho, J. S., & Almeida, C. G. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.1734-23.2024 · Cited by 10 · see citing works

Alzheimer’s disease susceptibility locus in CD2AP is associated with increased cerebrospinal fluid tau levels in mild cognitive impairment

Xue, Y., Chen, Y.-H., Lin, R.-R., Huang, H.-F., Wu, Z., & Tao, Q. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.136419 · Cited by 9 · see citing works

Evolutionary conservation of intrinsically unstructured regions in slit-diaphragm proteins

Mulukala, S. K. N., Kambhampati, V., Qadri, A. H., & Pasupulati, A. K. (2021) · PLoS ONE · doi:10.1371/journal.pone.0254917 · Cited by 8 · see citing works

CD2AP at the junction of nephropathy and Alzheimer’s disease

Vandal, M., Janmaleki, M., Rea, I. M., Gunn, C., Hirai, S., Biernaskie, J. A., Chun, J., Gordon, G. R., Shaw, A. S., Sanati‐Nezhad, A., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00852-x · Cited by 8 · see citing works

PTPN11/Corkscrew activates local presynaptic MAPK signaling to regulate Synapsin, synaptic vesicle pools, and neurotransmission strength, with a dual requirement in neurons and glia

Leahy, S. N., Vita, D. J., & Broadie, K. S. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.1077-23.2024 · Cited by 6 · see citing works

Non-microglial downregulation of <i>PLCG2</i> impairs synaptic function and elicits Alzheimer disease-related hallmarks

Coulon, A., Rabiller, F., Takalo, M., Roy, A., Pelletier, A., Martiskainen, H., Siedlecki-Wullich, D., Lannette-Weimann, N., Majerníková, N., Grenon, A., et al. (2024) · doi:10.1101/2024.04.29.591575 · Cited by 3 · see citing works

14-3-3 proteins regulate cullin 7-mediated Eag1 degradation

Hsieh, C.-H., Chou, C., Fang, Y.-C., Hsu, P., Chiu, Y.-H., Yang, C.-S., Jow, G., Tang, C., & Jeng, C. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-00969-w · Cited by 2 · see citing works

Endocytic scaffolds at the crossroads of Alzheimer’s disease and neuronal aging

Shergill, J. K., & Tehran, D. A. (2026) · Biological Chemistry · doi:10.1515/hsz-2025-0250 · Cited by 2 · see citing works

CD2AP in Alzheimer's disease: Key mechanisms and therapeutic potential

Wang, Y., & Zhang, Y.-W. (2025) · Brain medicine : · doi:10.61373/bm025i.0026 · Cited by 2 · see citing works

Pyk2 Overexpression in Postsynaptic Neurons Blocks Aβ 1-42 -induced Synaptotoxicity in a Microfluidic Co-Culture ModelPreprint

Kilinc, D., Vreulx, A.-C., Mendes, T., Flaig, A., Coelho, D. M., Verschoore, M., Demiautte, F., Amouyel, P., Bank, N.-C. B., Eysert, F., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2019.12.20.884205 · Cited by 2 · see citing works

PLCG2 downregulation impairs synaptic function and increases Alzheimer’s disease hallmarks in neuronal cultures

Coulon, A., Rabiller, F., Takalo, M., Roy, A., Pelletier, A., Martiskainen, H., Siedlecki-Wullich, D., Lannette-Weimann, N., Majerníková, N., Grenon, A., et al. (2026) · Nature Genetics · doi:10.1038/s41588-026-02709-5 · Cited by 1 · see citing works

Adult Neuronal Expression of the Alzheimer Risk Protein CD2AP is Enriched in NGF-Responsive Basal Forebrain Neurons, where it Collocates with Rab-5 EndosomesPreprint

Fitzsimons, L. A., Atif-Sheikh, M., Mueth, M. G., Rice, M., Howell, G. R., & Harrison, B. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.24.604961 · Cited by 1 · see citing works

Molecular Evolution of Podocyte Slit-diaphragm ProteinsPreprint

Mulukala, N., Kambhampati, V., Qadri, S., & Pasupulati, A. K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.03.366161

The Alzheimer’s disease risk gene CD2AP functions in dendritic spines by remodelling F-actinPreprint

Mirfakhar, F. S., Castanheira, J., Domingues, R., Ramalho, J. S., & Almeida, C. G. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.31.555707

Additional file 2 of Multi-tissue neocortical transcriptome-wide association study implicates 8 genes across 6 genomic loci in Alzheimer’s disease

Gockley, J., Montgomery, K. S., Poehlman, W. L., Wiley, J. C., Liu, Y., Gerasimov, E. S., Greenwood, A. K., Sieberts, S. K., Wingo, A. P., Wingo, T. S., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14538759

Identification of a ubiquitin-binding domain protein, CD2AP, in predicting the prognosis and treatment of lung adenocarcinoma

Dai, Q., Li, L., He, M., Huang, J., Bo, Z., Yin, J., & Ye, Y. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1726531

Simple in vivo models of Alzheimer's disease

Caito, S. W., & Newell-Caito, J. L. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-30008-0.00006-5

Additional file 1 of Multi-tissue neocortical transcriptome-wide association study implicates 8 genes across 6 genomic loci in Alzheimer’s disease

Gockley, J., Montgomery, K. S., Poehlman, W. L., Wiley, J. C., Liu, Y., Gerasimov, E. S., Greenwood, A. K., Sieberts, S. K., Wingo, A. P., Wingo, T. S., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14538753

Additional file 1 of Synaptic tau: A pathological or physiological phenomenon?

Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Figshare · doi:10.6084/m9.figshare.16599510

Synaptic transmission and plasticity: molecular mechanisms, biological functions and therapeutic opportunities in neurodegenerative diseases

Sun, J., Gao, G., Wang, S., Li, S., Tang, J., Liu, H., & Tang, T.-S. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02776-4

Cindr, the Drosophila Homolog of the CD2AP Alzheimer's Disease Susceptibility Gene, is Required for Synaptic Transmission and ProteostasisPreprint

Ojelade, S. A., Lee, T. V., Γιαγτζόγλου, Ν., Yu, L., Uğur, B., Duraine, L., Zuo, Z., Petyuk, V., Jager, P. L. D., Bennett, D. A., et al. (2019) · SSRN Electronic Journal · doi:10.2139/ssrn.3312120 · Cited by 1 · see citing works

P2‐136: CINDR, THE DROSOPHILA HOMOLOG OF CD2AP, AFFECTS SYNAPSE FUNCTION AND PROTEIN TURNOVER

Ojelade, S. A., Lee, T. V., Γιαγτζόγλου, Ν., & Shulman, J. M. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.06.822

[O2–18–04]: THE ALZHEIMER's DISEASE SUSCEPTIBILITY GENE CD2AP REGULATES PRESYNAPTIC FUNCTION

Ojelade, S. A., Lee, T. V., Γιαγτζόγλου, Ν., & Shulman, J. M. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.07.250 · Cited by 1 · see citing works

Alzheimer’s disease risk gene CD2AP is a dose-sensitive determinant of synaptic structure and plasticity

Pavešković, M., De-Paula, R. B., Ojelade, S. A., Tantry, E. K., Kochukov, M. Y., Bao, S., Veeraragavan, S., Garza, A. R., Srivastava, S., Song, S., et al. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae115 · Cited by 11 · see citing works

The Alzheimer's disease risk gene CD2AP modulates mammalian synaptic structure and plasticity

Pavešković, M., Ojelade, S. A., Kochukov, M. Y., Pekarek, B. T., Arenkiel, B. R., & Shulman, J. M. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.049854