Not just amyloid: physiological functions of the amyloid precursor protein family

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

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

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The Cellular Phase of Alzheimer’s Disease

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Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus

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Characterization and Chromosomal Localization of a cDNA Encoding Brain Amyloid of Alzheimer's Disease

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A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60

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Glia-Derived d-Serine Controls NMDA Receptor Activity and Synaptic Memory

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Release of Alzheimer Amyloid Precursor Derivatives Stimulated by Activation of Muscarinic Acetylcholine Receptors

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Novel CNS drug discovery and development approach: model-based integration to predict neuro-pharmacokinetics and pharmacodynamics

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Targeting Amyloid-β Precursor Protein, APP, Splicing with Antisense Oligonucleotides Reduces Toxic Amyloid-β Production

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Neuronal and Glial Differentiation of Human Neural Stem Cells Is Regulated by Amyloid Precursor Protein (APP) Levels

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Loss of all three APP family members during development impairs synaptic function and plasticity, disrupts learning, and causes an autism‐like phenotype

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Acrolein, an endogenous aldehyde induces Alzheimer's disease-like pathologies in mice: A new sporadic AD animal model

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Distinct types of amyloid‐β oligomers displaying diverse neurotoxicity mechanisms in Alzheimer's disease

Madhu, P., & Mukhopadhyay, S. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30141 · Cited by 53

The Nerve Growth Factor Receptor (NGFR/p75NTR): A Major Player in Alzheimer’s Disease

Bruno, F., Abondio, P., Montesanto, A., Luiselli, D., Bruni, A. C., & Maletta, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043200 · Cited by 49

The Role of Salivary Biomarkers in the Early Diagnosis of Alzheimer’s Disease and Parkinson’s Disease

Pawlik, P., & Błochowiak, K. J. (2021) · Diagnostics · doi:10.3390/diagnostics11020371 · Cited by 48

Amyloid β 42 fibril structure based on small-angle scattering

Lattanzi, V., André, I., Gasser, U., Dubackic, M., Olsson, U., & Linse, S. S. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2112783118 · Cited by 48

Systemic Actions of SGLT2 Inhibition on Chronic mTOR Activation as a Shared Pathogenic Mechanism between Alzheimer’s Disease and Diabetes

Stanciu, G. D., Rusu, R. N., Bild, V., Filipiuc, L. E., Tamba, B.-I., & Ababei, D. C. (2021) · Biomedicines · doi:10.3390/biomedicines9050576 · Cited by 47

Death-associated protein kinase 1 as a therapeutic target for Alzheimer's disease

Zhang, T., Kim, B. M., & Lee, T. H. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-023-00395-5 · Cited by 49

The Interaction Between Contactin and Amyloid Precursor Protein and Its Role in Alzheimer’s Disease

Bamford, R. A., Widagdo, J., Takamura, N., Eve, M., Anggono, V., & Oguro‐Ando, A. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.10.006 · Cited by 47

Morphological and Molecular Profiling of Amyloid-β Species in Alzheimer’s Pathogenesis

Almeida, Z. L., Vaz, D. C., & Brito, R. M. M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04543-4 · Cited by 49

Processing of Mutant β-Amyloid Precursor Protein and the Clinicopathological Features of Familial Alzheimer’s Disease

Bi, C., Bi, S., & Li, B. (2018) · Aging and Disease · doi:10.14336/ad.2018.0425 · Cited by 46

Alzheimer’s Disease, a Lipid Story: Involvement of Peroxisome Proliferator-Activated Receptor α

Sáez-Orellana, F., Octave, J., & Pierrot, N. (2020) · Cells · doi:10.3390/cells9051215 · Cited by 47

Knockdown of Amyloid Precursor Protein: Biological Consequences and Clinical Opportunities

Gabriele, R. M. C., Abel, E., Fox, N. C., Wray, S., & Arber, C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.835645 · Cited by 44

Post Translational Modulation of β-Amyloid Precursor Protein Trafficking to the Cell Surface Alters Neuronal Iron Homeostasis

Tsatsanis, A., Dickens, S., Kwok, J. C. F., Wong, B. X. W., & Duce, J. A. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02747-y · Cited by 45

Salivary Biomarkers: Future Approaches for Early Diagnosis of Neurodegenerative Diseases

Schepici, G., Silvestro, S., Trubiani, O., Bramanti, P., & Mazzon, E. (2020) · Brain Sciences · doi:10.3390/brainsci10040245 · Cited by 44

The actin-modulating protein synaptopodin mediates long-term survival of dendritic spines

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Leukotrienes vs. Montelukast—Activity, Metabolism, and Toxicity Hints for Repurposing

Marques, C. F., Marques, M. M., & Justino, G. C. (2022) · Pharmaceuticals · doi:10.3390/ph15091039 · Cited by 47

Molecular mechanisms and therapeutic potential of lithium in Alzheimer’s disease: repurposing an old class of drugs

Shen, Y., Zhao, M., Zhao, P., Meng, L., Zhang, Y., Zhang, G., Taishi, Y., & Sun, L. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1408462 · Cited by 45

Physiological effects of amyloid precursor protein and its derivatives on neural stem cell biology and signaling pathways involved

Liste, I., Coronel, R., Palmer, C., Bernabeu-Zornoza, A., Monteagudo, M., Rosca, A., & Zambrano, A. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.257511 · Cited by 48

Proteomic Investigations of Autism Brain Identify Known and Novel Pathogenetic Processes

Abraham, J. R., Szoko, N., Barnard, J., Rubin, R. A., Schlatzer, D., Lundberg, K. C., Li, X., & Natowicz, M. R. (2019) · Scientific Reports · doi:10.1038/s41598-019-49533-y · Cited by 43

Molecular mechanisms linking type 2 diabetes mellitus and late-onset Alzheimer's disease: A systematic review and qualitative meta-analysis

Lemche, E., Killick, R., Mitchell, J., Caton, P., Choudhary, P., & Howard, J. K. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106485 · Cited by 45

Electrochemical aptamer-based nanobiosensors for diagnosing Alzheimer's disease: A review

Negahdary, M., & Angnes, L. (2022) · Biomaterials Advances · doi:10.1016/j.msec.2022.112689 · Cited by 42

Knockdown of astrocytic Grin2a aggravates β‐amyloid‐induced memory and cognitive deficits through regulating nerve growth factor

Du, Z., Song, Y., Chen, X., Zhang, W., Zhang, G., Li, H., Chang, L., & Wu, Y. (2021) · Aging Cell · doi:10.1111/acel.13437 · Cited by 41

Cholesterol and Lipid Rafts in the Biogenesis of Amyloid-β Protein and Alzheimer's Disease

Pantelopulos, G. A., Abraham, C. B., & Straub, J. E. (2024) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-062823-023436 · Cited by 43

The multiple roles of chronic stress and glucocorticoids in Alzheimer's disease pathogenesis

Burke, M. R., Sotiropoulos, I., & Waites, C. L. (2024) · Trends in Neurosciences · doi:10.1016/j.tins.2024.08.015 · Cited by 43

Therapeutic Potential of Targeting Mitochondria for Alzheimer’s Disease Treatment

Atlante, A., Amadoro, G., Latina, V., & Valenti, D. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11226742 · Cited by 40

Abnormal clotting of the intrinsic/contact pathway in Alzheimer disease patients is related to cognitive ability

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Hebbian and Homeostatic Synaptic Plasticity—Do Alterations of One Reflect Enhancement of the Other?

Galanis, C., & Vlachos, A. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00050 · Cited by 43

Measurement of α-synuclein as protein cargo in plasma extracellular vesicles

Gilboa, T., Ter‐Ovanesyan, D., Wang, S., Whiteman, S. T., Kannarkat, G. T., Church, G. M., Chen‐Plotkin, A. S., & Walt, D. R. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2408949121 · Cited by 38

(−)-Phenserine inhibits neuronal apoptosis following ischemia/reperfusion injury

Chang, C.-F., Lai, J.-H., Wu, J. C.-C., Greig, N. H., Becker, R. E., Luo, Y., Chen, Y., Kang, S.-J., Chiang, Y. H., & Chen, K. (2017) · Brain Research · doi:10.1016/j.brainres.2017.09.015 · Cited by 38

Targeting neurodegeneration to prevent post-traumatic epilepsy.

Ali, I., Silva, J. C., Liu, S., Shultz, S. R., Kwan, P., Jones, N. C., & O'Brien, T. J. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.08.006 · Cited by 38

New Insights Into Blood-Brain Barrier Maintenance: The Homeostatic Role of β-Amyloid Precursor Protein in Cerebral Vasculature

Ristori, E., Donnini, S., & Ziche, M. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.01056 · Cited by 38

O-GlcNAcylation and neuronal energy status: Implications for Alzheimer’s disease

Pinho, T. S., Verde, D. V., Correia, S. C., Cardoso, S., & Moreira, P. I. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.05.003 · Cited by 41

C/EBPβ/AEP Signaling Drives Alzheimer’s Disease Pathogenesis

Xiong, J., Zhang, Z., & Ye, K. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01025-w · Cited by 37

APP dyshomeostasis in the pathogenesis of Alzheimer’s disease: implications for current drug targets

Sirisi, S., Sánchez‐Aced, É., Belbin, O., & Lleó, A. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-024-01504-w · Cited by 41

Click Chemistry-mediated Biotinylation Reveals a Function for the Protease BACE1 in Modulating the Neuronal Surface Glycoproteome

Herber, J., Njavro, J. R., Feederle, R., Schepers, U., Müller, U., Bräse, S., Müller, S. A., & Lichtenthaler, S. F. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000608 · Cited by 40

Proamyloidogenic effects of membrane type 1 matrix metalloproteinase involve MMP-2 and BACE-1 activities, and the modulation of APP trafficking.

Paumier, J.-M., Py, N. A., García-González, L., Bernard, A., Stephan, D., Louis, L., Checler, F., Khrestchatisky, M., Baranger, K., & Rivera, S. (2019) · The FASEB Journal · doi:10.1096/fj.201801076r · Cited by 40

Mind the Gap: Mitochondria and the Endoplasmic Reticulum in Neurodegenerative Diseases

Leal, N. S., & Martins, L. M. (2021) · Biomedicines · doi:10.3390/biomedicines9020227 · Cited by 40

Stress-responsive regulation of extracellular proteostasis

Mesgarzadeh, J. S., Buxbaum, J. N., & Wiseman, R. L. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202112104 · Cited by 38

An agnostic reevaluation of the amyloid cascade hypothesis of Alzheimer's disease pathogenesis: The role of APP homeostasis

Caselli, R. J., Knopman, D. S., & Bu, G. (2020) · Alzheimer s & Dementia · doi:10.1002/alz.12124 · Cited by 36

Iron and Targeted Iron Therapy in Alzheimer’s Disease

Wang, J., Fu, J., Zhao, Y., Liu, Q., Yan, X., & Su, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216353 · Cited by 35

Molecular mechanisms underlying actions of certain long noncoding RNAs in Alzheimer’s disease

Ahmadi, S., Zobeiri, M., & Bradburn, S. (2020) · Metabolic Brain Disease · doi:10.1007/s11011-020-00564-9 · Cited by 35

Presynaptic APP levels and synaptic homeostasis are regulated by Akt phosphorylation of huntingtin

Bruyère, J., Abada, Y.-S. K., Vitet, H., Fontaine, G., Deloulme, J., Cès, A., Denarier, É., Pernet‐Gallay, K., Andrieux, A., Humbert, S., et al. (2020) · eLife · doi:10.7554/elife.56371 · Cited by 38

Inflammasome activation in neurodegenerative diseases

Ravichandran, K. A., & Heneka, M. T. (2021) · Essays in Biochemistry · doi:10.1042/ebc20210021 · Cited by 37

Aducanumab and Its Effects on Tau Pathology: Is This the Turning Point of Amyloid Hypothesis?

Silvestro, S., Valeri, A., & Mazzon, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042011 · Cited by 37

Amyloid Precursor Protein (APP) Controls the Expression of the Transcriptional Activator Neuronal PAS Domain Protein 4 (NPAS4) and Synaptic GABA Release

Opsomer, R., Contino, S., Perrin, F., Gualdani, R., Tasiaux, B., Doyen, P. J., Vergouts, M., Vrancx, C., Doshina, A., Pierrot, N., et al. (2020) · eNeuro · doi:10.1523/eneuro.0322-19.2020 · Cited by 38

MicroRNAs and MAPKs: Evidence of These Molecular Interactions in Alzheimer’s Disease

Raffaele, I., Silvestro, S., & Mazzon, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054736 · Cited by 33

Amyloid precursor protein is required for in vitro platelet adhesion to amyloid peptides and potentiation of thrombus formation

Visconte, C., Canino, J., Guidetti, G. F., Zarà, M., Seppi, C., Abubaker, A. A., Pula, G., Torti, M., & Canobbio, I. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.08.017 · Cited by 33

Real-time nanoscale organization of amyloid precursor protein

Kedia, S., Ramakrishna, P., Netrakanti, P. R., Jose, M., Sibarita, J., Nadkarni, S., & Nair, D. K. (2020) · Nanoscale · doi:10.1039/d0nr00052c · Cited by 33

The plasminogen activating system in the pathogenesis of Alzheimer’s disease

Yepes, M. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.308076 · Cited by 33

Amyloid Precursor Protein (APP) and GABAergic Neurotransmission

Tang, B. L. (2019) · Cells · doi:10.3390/cells8060550 · Cited by 34

The Role of Extracellular Matrix Components in the Spreading of Pathological Protein Aggregates

Moretto, E., Stuart, S., Surana, S., Vargas, J. N. S., & Schiavo, G. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.844211 · Cited by 32

Ferroptosis participates in neuron damage in experimental cerebral malaria and is partially induced by activated CD8+ T cells

Liang, J., Shen, Y., Wang, Y., Huang, Y., Wang, J., Zhu, Q., Tong, G., Yu, K., Cao, W. W., Wang, Q., et al. (2022) · Molecular Brain · doi:10.1186/s13041-022-00942-7 · Cited by 32

Olfactory Dysfunction and Alzheimer’s Disease: A Review

McLaren, A., & Kawaja, M. D. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231377 · Cited by 35

Deficits in the Proline-Rich Synapse-Associated Shank3 Protein in Multiple Neuropsychiatric Disorders

Alexandrov, P. N., Zhao, Y., Jaber, V. R., Cong, L., & Lukiw, W. J. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00670 · Cited by 31

A magnetic nanofiber-based zwitterionic hydrophilic material for the selective capture and identification of glycopeptides

Huan, W., Zhang, J., Qin, H., Huan, F., Wang, B., Wu, M., & Li, J. (2019) · Nanoscale · doi:10.1039/c9nr01441a · Cited by 31

A Near‐Infrared‐Controllable Artificial Metalloprotease Used for Degrading Amyloid‐β Monomers and Aggregates

Ma, M., Wang, Y., Gao, N., Liu, X., Sun, Y., Ren, J., & Qu, X. (2019) · Chemistry - A European Journal · doi:10.1002/chem.201902828 · Cited by 31

α-Lipoic Acid Has the Potential to Normalize Copper Metabolism, Which Is Dysregulated in Alzheimer’s Disease

Metsla, K., Kirss, S., Laks, K., Sildnik, G., Palgi, M., Palumaa, T., Tõugu, V., & Palumaa, P. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215026 · Cited by 34

The Amyloid Precursor Protein Modulates the Position and Length of the Axon Initial Segment

Ma, F., Akolkar, H., Xu, J., Liu, Y., Popova, D., Xie, J., Youssef, M. M., Benosman, R. B., Hart, R. P., & Herrup, K. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.0172-22.2023 · Cited by 33

Increased soluble amyloid-beta causes early aberrant brain network hypersynchronisation in a mature-onset mouse model of amyloidosis

Ben-Nejma, I. R. H., Keliris, A., Daans, J., Ponsaerts, P., Verhoye, M., der Linden, A. V., & Keliris, G. A. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0810-7 · Cited by 35

Protein-Protein Interactions and Aggregation Inhibitors in Alzheimer’s Disease

Ganeshpurkar, A., Swetha, R., Kumar, D., Gangaram, G. P., Singh, R., Gutti, G., Jana, S., Kumar, D., Kumar, A., & Singh, S. K. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190304153353 · Cited by 30

Early impairment of cortical circuit plasticity and connectivity in the 5XFAD Alzheimer’s disease mouse model

Chen, C., Ma, X., Wei, J., Shakir, N., Zhang, J. K., Zhang, L., Nehme, A., Cui, Y., Ferguson, D., Bai, F., et al. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-02132-4 · Cited by 32

Discovery of potent and selective dual cholinesterases and β-secretase inhibitors in pomegranate as a treatment for Alzheimer’s disease

Ali, M. Y., Zaib, S., Jannat, S., & Khan, I. A. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106137 · Cited by 30

Amyloid Precursor Protein: A Regulatory Hub in Alzheimer's Disease

Chen, J., Chen, J.-S., Li, S., Zhang, F., Deng, J., Zeng, L., & Tan, J. (2023) · Aging and Disease · doi:10.14336/ad.2023.0308 · Cited by 34

Regulation of immune and neural function via leukocyte Ig-like receptors

Takeda, K., & Nakamura, A. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx036 · Cited by 30

Direct evidence of amyloid precursor–like protein 1 trans interactions in cell–cell adhesion platforms investigated via fluorescence fluctuation spectroscopy

Dunsing, V., Mayer, M., Liebsch, F., Multhaup, G., & Chiantia, S. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-07-0459 · Cited by 30

The Synaptic Vesicle Protein 2A Interacts With Key Pathogenic Factors in Alzheimer’s Disease: Implications for Treatment

Kong, Y., Huang, L., Li, W., Liu, X., Zhou, Y., Liu, C., Zhang, S., Xie, F., Zhang, Z., Jiang, D., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.609908 · Cited by 29

Dysfunctional proteins in neuropsychiatric disorders: From neurodegeneration to autism spectrum disorders

Jęśko, H. M., Cieślik, M., Gromadzka, G., & Adamczyk, A. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104853 · Cited by 30

Ginger, a Possible Candidate for the Treatment of Dementias?

Schepici, G., Contestabile, V., Valeri, A., & Mazzon, E. (2021) · Molecules · doi:10.3390/molecules26185700 · Cited by 29

Accelerated aging-related transcriptome alterations in neurovascular unit cells in the brain of Alzheimer’s disease

Zhao, Y. G., Xie, Y., & Liu, Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.949074 · Cited by 29

NMNAT2 supports vesicular glycolysis via NAD homeostasis to fuel fast axonal transport

Yang, S., Niou, Z., Enriquez, A., LaMar, J., Huang, J.-Y., Ling, K., Jafar‐Nejad, P., Gilley, J., Coleman, M. P., Tennessen, J. M., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00690-9 · Cited by 30

Amyloid precursor protein and amyloid precursor‐like protein 2 have distinct roles in modulating myelination, demyelination, and remyelination of axons

Truong, P. H., Ciccotosto, G. D., Merson, T. D., Spoerri, L., Chuei, M. J., Ayers, M. M., Xing, Y. L., Emery, B., & Cappai, R. (2018) · Glia · doi:10.1002/glia.23561 · Cited by 29

APP-Mediated Signaling Prevents Memory Decline in Alzheimer’s Disease Mouse Model

Deyts, C., Clutter, M., Pierce, N., Chakrabarty, P., Ladd, T. B., GODDI, A. A., Rosario, A. M., Cruz, P. E., Vetrivel, K. S., Wagner, S. L., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.087 · Cited by 31

Activating autophagy to eliminate toxic protein aggregates with small molecules in neurodegenerative diseases

Fu, Y., Zhang, J., Qin, R., Ren, Y., Zhou, T., Han, B., & Liu, B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100053 · Cited by 29

Low Evolutionary Selection Pressure in Senescence Does Not Explain the Persistence of Aβ in the Vertebrate Genome

Moir, R. D., & Tanzi, R. E. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00070 · Cited by 29

Plasminogen Activators in Neurovascular and Neurodegenerative Disorders

Yepes, M., Woo, Y., & Martín-Jiménez, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094380 · Cited by 28

MDGA1 negatively regulates amyloid precursor protein–mediated synapse inhibition in the hippocampus

Kim, J., Kim, S., Kim, H., Hwang, I.-W., Bae, S., Karki, S., Kim, D., Ogelman, R., Bang, G., Kim, J. Y., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2115326119 · Cited by 29

The role of UNC5C in Alzheimer’s disease

Li, Q., Wang, B.-L., Sun, F.-R., Li, J., Cao, X., & Tan, L. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.04.43 · Cited by 29

The Human Amyloid Precursor Protein Binds Copper Ions Dominated by a Picomolar-Affinity Site in the Helix-Rich E2 Domain

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Electroacupuncture Mitigates Hippocampal Cognitive Impairments by Reducing BACE1 Deposition and Activating PKA in APP/PS1 Double Transgenic Mice

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