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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Amyloid Beta Peptide-Mediated Alterations in Mitochondrial Dynamics and its Implications for Alzheimer’s Disease

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Hypothesis on ontogenesis and pathophysiology of Alzheimer’s disease

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Lack of β-amyloid cleaving enzyme-1 (BACE1) impairs long-term synaptic plasticity but enhances granule cell excitability and oscillatory activity in the dentate gyrus in vivo

Vnencak, M., Schölvinck, M. L., Schwarzacher, S. W., Deller, T., Willem, M., & Jedlička, P. (2019) · Brain Structure and Function · doi:10.1007/s00429-019-01836-6 · Cited by 13

Common Pathological Mechanisms and Risk Factors for Alzheimer’s Disease and Type-2 Diabetes: Focus on Inflammation

Moyse, E., Haddad, M., Benlabiod, C., Ramassamy, C., & Krantic, S. M. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191106094356 · Cited by 14

The Amyloid Precursor Protein Regulates Synaptic Transmission at Medial Perforant Path Synapses

Lenz, M., Eichler, A., Kruse, P., Galanis, C., Kleidonas, D., Andrieux, G., Boerries, M., Jedlička, P., Müller, U., Deller, T., et al. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1824-22.2023 · Cited by 14

The Therapeutic Potential of Glymphatic System Activity to Reduce the Pathogenic Accumulation of Cytotoxic Proteins in Alzheimer’s Disease

Kopeć, K., Koziorowski, D., & Szlufik, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157552 · Cited by 15

Shifting the balance: soluble ADAM10 as a potential treatment for Alzheimer's disease

Hershkovits, A. S., Gelley, S., Hanna, R., Kleifeld, O., Shulman, A., & Fishman, A. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1171123 · Cited by 12

APP‐C31: An Intracellular Promoter of Both Metal‐Free and Metal‐Bound Amyloid‐β40 Aggregation and Toxicity in Alzheimer's Disease

Nam, E., Lin, Y., Park, J., Do, H., Han, J., Jeong, B., Park, S., Lee, D. Y., Kim, M., Han, J., et al. (2023) · Advanced Science · doi:10.1002/advs.202307182 · Cited by 12

Multiple Transcriptomic Analyses Explore Potential Synaptic Biomarker Rabphilin-3A for Alzheimer's Disease

Nguyen, D. P. Q., Pham, S., Jallow, A. W., Ho, N.-T., Le, B., Quang, H. T., Lin, Y.-F., & Lin, Y.-F. (2024) · Scientific Reports · doi:10.1038/s41598-024-66693-8 · Cited by 14

Unraveling the Roles of UBE3A in Neurodevelopment and Neurodegeneration

Yang, X., & Huang, Y. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26052304 · Cited by 12

The Strategies for Treating “Alzheimer’s Disease”: Insulin Signaling May Be a Feasible Target

You, G., Yao, J., Liu, Q., & Li, N. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44120421 · Cited by 12

Amyloid precursor protein 𝛽CTF accumulates in synapses in sporadic and genetic forms of Alzheimer's disease

Ferrer‐Raventós, P., Puertollano‐Martín, D., Querol‐Vilaseca, M., Sánchez‐Aced, É., Valle‐Tamayo, N., González, A. C., Núñez‐Llaves, R., Pegueroles, J., Dols‐Icardo, O., Iulita, M. F., et al. (2023) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12879 · Cited by 13

Is brain iron trafficking part of the physiology of the amyloid precursor protein?

Bailey, D. K., & Kosman, D. J. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01684-z · Cited by 12

Paradoxical effects of mutant ubiquitin on Aβ plaque formation in an Alzheimer mouse model

Verheijen, B. M., Stevens, J., Gentier, R. J. G., Hekke, C. D. V. ‘., van den Hove, D., Hermes, D. J. H. P., Steinbusch, H. W. M., Ruijter, J. M., Grimm, M. O. W., Haupenthal, V. J., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.08.011 · Cited by 12

Differential neuropsychiatric associations of plasma biomarkers in older adults with major depression and subjective cognitive decline

Wei, Y., Kung, Y., Lin, C., Yeh, C., Chen, P., Huang, W., Shyu, Y., Lin, C., & Chen, C. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-03049-w · Cited by 11

The pathogenic APP N-terminal Val225Ala mutation alters tau protein liquid-liquid phase separation and exacerbates synaptic damage

Chen, J., Li, S., Zhang, F., Chen, J., Cai, C., Guo, Y., Lei, Z., Zeng, L., Zi, D., Shen, Y., et al. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02837-6 · Cited by 12

A Proteomics Profiling Reveals the Neuroprotective Effects of Melatonin on Exogenous β‐amyloid‐42 Induced Mitochondrial Impairment, Intracellular β‐amyloid Accumulation and Tau Hyperphosphorylation in Human SH‐SY5Y Cells

Panmanee, J., Phanchana, M., Pearngam, P., Petchyam, N., Promthep, K., Wisomka, P., Kutpruek, S., Pannengpetch, S., Prasertporn, T., Mukda, S., et al. (2025) · Cell Biology International · doi:10.1002/cbin.70013 · Cited by 11

Motor Skills: Recruitment of Kinesins, Myosins and Dynein during Assembly and Egress of Alphaherpesviruses

Wilson, D. W. (2021) · Viruses · doi:10.3390/v13081622 · Cited by 12

Recent progress on synthetic and protein-based genetically encoded sensors for fluorimetric Cu( i ) recognition: binding and reaction-based approaches

Kumar, S., Kaushal, J., Goswami, T., Kumar, P., & Kumar, P. (2022) · Sensors & Diagnostics · doi:10.1039/d1sd00065a · Cited by 11

Alzheimer’s Disease and Its Possible Evolutionary Origin: Hypothesis

Whitfield, J. F., Rennie, K., & Chakravarthy, B. (2023) · Cells · doi:10.3390/cells12121618 · Cited by 11

Persistent diazinon induced neurotoxicity: The effect on inhibitory avoidance memory performance, amyloid precursor proteins, and TNF-α levels in the prefrontal cortex of rats

Afshari, S., Sarailoo, M., Asghariazar, V., Safarzadeh, E., & Dadkhah, M. (2024) · Human & Experimental Toxicology · doi:10.1177/09603271241235408 · Cited by 11

Prostaglandin J2 promotes O-GlcNAcylation raising APP processing by α- and β-secretases: relevance to Alzheimer's disease

Jean-Louis, T. L., Rockwell, P., & Figueiredo‐Pereira, M. E. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.10.009 · Cited by 11

Recent Endeavors on Molecular Imaging for Mapping Metals in Biology

Gao, J., Chen, Y., Guo, Z., & He, W. (2020) · Biophysics Reports · doi:10.1007/s41048-020-00118-7 · Cited by 11

Platelet APP Processing: Is It a Tool to Explore the Pathophysiology of Alzheimer’s Disease? A Systematic Review

Carbone, M. G., Pagni, G., Tagliarini, C., Marazziti, D., & Pomara, N. (2021) · Life · doi:10.3390/life11080750 · Cited by 11

C/EBPβ as a master regulator of inflammasome signaling in neurodegenerative diseases: mechanisms and therapeutic implications

Wang, J., Li, Y., & Xia, Y. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1656165 · Cited by 10

Review of anti-amyloid-beta (Aβ) monoclonal antibodies for the treatment of Alzheimer’s disease

Francis, E., Paylor, S., Van, C., Mathews, B., Sobhanian, M. J., Mansour, D. Z., Hennawi, G., & Brandt, N. (2025) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2025.2556122 · Cited by 10

Impact of chronic doxycycline treatment in the APP/PS1 mouse model of Alzheimer's disease

Gómez‐Murcia, V., Carvalho, K., Thiroux, B., Caillierez, R., Besegher, M., Sergeant, N., Buée, L., Faivre, E., & Blum, D. L. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.108999 · Cited by 11

Platelet-Derived Drug Targets and Biomarkers of Ischemic Stroke—The First Dynamic Human LC-MS Proteomic Study

Gawryś, K., Turek-Jakubowska, A., Gawryś, J., Jakubowski, M., Dȩbski, J., Szahidewicz-Krupska, E., Trocha, M., Derkacz, A., & Doroszko, A. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11051198 · Cited by 10

Apolipoprotein E Isoform-Dependent Effects on Human Amyloid Precursor Protein/Aβ-Induced Behavioral Alterations and Cognitive Impairments and Insoluble Cortical Aβ42 Levels

Holden, S. J., Kundu, P., Torres, E. R. S., Sudhakar, R., Krenik, D., Grygoryev, D., Turker, M. S., & Raber, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.767558 · Cited by 10

Detection and verification of neurodegeneration after traumatic brain injury in the mouse: Immunohistochemical staining for amyloid precursor protein

Xiong, G., Metheny, H. E., Hood, K., Jean, I., Farrugia, A. M., Johnson, B. N., Tummala, S. R., Cohen, N. A., & Cohen, A. S. (2023) · Brain Pathology · doi:10.1111/bpa.13163 · Cited by 10

The amyloid-β peptide: Guilty as charged?

Murphy, M. P., Buzinova, V. A., & Johnson, C. E. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166945 · Cited by 12

Amyloid precursor protein induces reactive astrogliosis

Jáuregui, G. V., Vukić, D., Onyango, I. G., Arias, C., Novotný, J., Texlova, K., Wang, S., Kovačovicova, K. L., Polakova, N., Zelinková, J., et al. (2024) · Acta Physiologica · doi:10.1111/apha.14142 · Cited by 10

Role of APLP2 in the prognosis and clinicopathology of renal cell carcinoma

Gao, L., Zhao, H., Zhang, D., Zhou, C., Wang, H., Ren, C., Liu, Y., Xia, Y., & Shi, B. (2018) · Oncology Letters · doi:10.3892/ol.2018.9577 · Cited by 10

Decrease in 130 kDa- amyloid protein precursor protein (APP) and APP protein ratio in schizophrenia platelets

Терешкина, Е. Б., Бокша, И. С., Prokhorova, T. A., Savushkina, O. K., Burbaeva, G. S., Ma, M., & Mukaetova-Ladinska, E. B. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.134914 · Cited by 10

Amyloid Beta Peptide (Aβ1-42) Reverses the Cholinergic Control of Monocytic IL-1β Release

Richter, K., Ogiemwonyi‐Schaefer, R., Wilker, S., Chaveiro, A. I., Agné, A. M., Hecker, M., Reichert, M., Amati, A., Schlüter, K., Manzini, I., et al. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9092887 · Cited by 10

Amyloid beta induces Fmr1‐dependent translational suppression and hyposynchrony of neural activity via phosphorylation of eIF2α and eEF2

Lizarazo, S., Yook, Y., & Tsai, N. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30754 · Cited by 10

Neurogenesis Is Increased in Human Neural Stem Cells by Aβ40 Peptide

Bernabeu-Zornoza, A., Coronel, R., Palmer, C., Martín, A., López-Alonso, V., & Liste, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105820 · Cited by 11

Amyloid Precursor Protein Dimerisation Reduces Neurite Outgrowth

Luu, L., Ciccotosto, G. D., Vella, L. J., Cheng, L., Roisman, L. C., Multhaup, G., Hill, A. F., Munter, L. M., & Cappai, R. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1070-4 · Cited by 10

Dynamic changes in the brain protein interaction network correlates with progression of Aβ42 pathology in Drosophila

Scholes, H. M., Cryar, A., Kerr, F., Sutherland, D., Gethings, L. A., Vissers, J. P. C., Lees, J., Orengo, C. A., Partridge, L., & Thalassinos, K. (2020) · Scientific Reports · doi:10.1038/s41598-020-74748-9 · Cited by 13

Reduced expression of APLP2 in spinal GABAergic inhibitory neurons contributed to nerve injury-induced microglial activation and pain sensitization

Li, Y.-Z., Zhu, Y.-B., Ge, A.-N., Gao, M., Wang, K., Zeng, X.-R., Li, J., Li, Y., Xu, J.-Y., Bai, H.-H., et al. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.109334 · Cited by 9

Electrochemical biosensor-based detection assays for early diagnosis of neurodegenerative disorders

da Silva, I. S., Cardoso, A. R. A., & Sales, M. G. F. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95539-3.00010-7 · Cited by 9

Consequences of Amyloid‐β Deficiency for the Liver

Buniatian, G. H., Schwinghammer, U., Tremmel, R., Cynis, H., Weiß, T. S., Weiskirchen, R., Lauschke, V. M., Youhanna, S. C., Ramos, I., Valcárcel, M., et al. (2024) · Advanced Science · doi:10.1002/advs.202307734 · Cited by 9

Eta-secretase-like processing of the amyloid precursor protein (APP) by the rhomboid protease RHBDL4

Penalva, Y. C. M., Paschkowsky, S., Recinto, S. J., Duchesne, A., Hammond, T., Spiegler, P., Jansen, G., Levet, C., Charron, F. M., Freeman, M., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107541 · Cited by 9

The aggregation propensity of Tau and amyloid-β in Alzheimer’s disease

Chinnathambi, S., Kumarappan, M., Chandrshekar, M., & Malik, S. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.10.004 · Cited by 9

The novel sphingolipids cP1P and P1P attenuate neuroinflammation and enhance S1PR1/Akt/mTOR signaling to mitigate cognitive decline in an Alzheimer’s disease mouse model

Choe, K., Ahmad, R., Kang, M. H., Lee, H. J., Ahmad, S., Park, T. J., & Kim, M. O. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02485-5 · Cited by 9

The Deficits of Insulin Signal in Alzheimer’s Disease and the Mechanisms of Vanadium Compounds in Curing AD

Yao, J., He, Z., You, G., Liu, Q., & Li, N. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45080402 · Cited by 9

The Icelandic Mutation (APP-A673T) Is Protective against Amyloid Pathology In Vivo

Shimohama, S., Fujioka, R., Mihira, N., Sekiguchi, M., Sartori, L., Joho, D., Saito, T., Saido, T. C., Nakahara, J., Hino, T., et al. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.0223-24.2024 · Cited by 9

When nature’s robots go rogue: exploring protein homeostasis dysfunction and the implications for understanding human aging disease pathologies

Reisz, J. A., Barrett, A. S., Nemkov, T. G., Hansen, K. C., & D’Alessandro, A. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2018.1453362 · Cited by 11

A novel role of HuR in ‐Epigallocatechin‐3‐gallate ( EGCG ) induces tumour cells apoptosis

Jian, W., Fang, S., Chen, T., Fang, J., Mo, Y., Li, D., Xiong, S., Liu, W., Song, L., Shen, J., et al. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14249 · Cited by 9

Cereblon-mediated degradation of the amyloid precursor protein via the ubiquitin-proteasome pathway

Kurihara, T., Asahi, T., & Sawamura, N. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.01.078 · Cited by 9

Astrocytic N-Methyl-D-Aspartate Receptors Protect the Hippocampal Neurons Against Amyloid-β142-Induced Synaptotoxicity by Regulating Nerve Growth Factor

Song, Y., Du, Z., Chen, X., Zhang, W., Zhang, G., Li, H., Chang, L., & Wu, Y. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210730 · Cited by 9

Unraveling the Molecular Dance: Insights into TREM2/DAP12 Complex Formation in Alzheimer’s Disease through Molecular Dynamics Simulations

Zhong, Z., Ulmschneider, M. B., & Lorenz, C. D. (2024) · ACS Omega · doi:10.1021/acsomega.4c03060 · Cited by 8

Iron-Mediated Overexpression of Amyloid Precursor Protein via Iron Responsive mRNA in Alzheimer’s Disease

Khan, M. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115283 · Cited by 8

Neuroactive venom compounds obtained from Phlogiellus bundokalbo as potential leads for neurodegenerative diseases: insights on their acetylcholinesterase and beta-secretase inhibitory activities in vitro

Lopez, S. M. M., Aguilar, J. S., Fernandez, J. B. B., Lao, A. G. J., Estrella, M. R. R., Devanadera, M. K., Ramones, C. M. V., Villaraza, A. J. L., Guevarra, L. A., Santiago-Bautista, M. R., et al. (2021) · The Journal of venomous animals and toxins including tropical diseases · doi:10.1590/1678-9199-jvatitd-2021-0009 · Cited by 9

The AICD fragment of APP initiates a FoxO3a mediated response via FANCD2

Greenwood, E. K., Angelova, D. M., Büchner, H. M. I., & Brown, D. R. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103760 · Cited by 8

Potential drugs for the treatment of Alzheimer’s disease

Montero-Cosme, T. G., Pascual-Mathey, L. I., Hernández‐Aguilar, M. E., Herrera‐Covarrubias, D., Rojas-Durán, F., & Aranda-Abreu, G. E. (2023) · Pharmacological Reports · doi:10.1007/s43440-023-00481-5 · Cited by 8

Hydrodynamic Control of Alzheimer Aβ Fibrillation with Glucosaminic Acid Containing Click-Cyclized β-Bodies

Zhang, Y., Borch, L. A., Fischer, N. H., & Meldal, M. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c12118 · Cited by 8

Astragalin actives autophagy and inhibits apoptosis of astrocytes in AD mice via down-regulating Fas/Fasl-VDAC1 pathway

Wang, S., Yang, Y., Lin, J., Zhang, W., Yang, C., Zhang, R., Zhou, C., Zhang, L., Wang, X., Liu, J., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.02.047 · Cited by 8

The lipid raft-dwelling protein US9 can be manipulated to target APP compartmentalization, APP processing, and neurodegenerative disease pathogenesis

Brandimarti, R., Hill, G. S., Geiger, J. D., & Meucci, O. (2017) · Scientific Reports · doi:10.1038/s41598-017-15128-8 · Cited by 8

Determining the Protein Stability of Alzheimer’s Disease Protein, Amyloid Precursor Protein

Delport, A., & Hewer, R. (2019) · The Protein Journal · doi:10.1007/s10930-019-09829-4 · Cited by 8

Regulation of Neurodegeneration-associated Protein Fragments by the N-degron Pathways

Eldeeb, M. A., Ragheb, M. A., Soliman, M. H., & Fahlman, R. P. (2022) · Neurotoxicity Research · doi:10.1007/s12640-021-00396-0 · Cited by 9

Identification of the probable structure of the sAPPα-GABA B R1a complex and theoretical solutions for such cases

Yang, H., Mei, J., Xu, W. W., Ma, X., Sun, B., & Ai, H. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp00569g · Cited by 8

Proteomic Analysis Identifies Circulating Proteins Associated With Plasma Amyloid-β and Incident Dementia

Tin, A., Sullivan, K., Walker, K. A., Bressler, J., Talluri, R., Yu, B., Simino, J. M., Guðmundsdóttir, V., Emilsson, V., Jennings, L. L., et al. (2022) · Biological Psychiatry Global Open Science · doi:10.1016/j.bpsgos.2022.04.005 · Cited by 8

Human neurons lacking amyloid precursor protein exhibit cholesterol‐associated developmental and presynaptic deficits

Mesa, H., Zhang, E. Y., Wang, Y., & Zhang, Q. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.30999 · Cited by 9

Role of Neurexins in Alzheimer's Disease

Medina-Samamé, A., Paller, É., Bril, M. R., Archvadze, A., Simões-Abade, M. B. C., Cayuela, P. E., & LeMaoult, C. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.0169-23.2023 · Cited by 8

Probing the Mint2 Protein–Protein Interaction Network Relevant to the Pathophysiology of Alzheimer's Disease

Jensen, T. M. T., Albertsen, L., Bartling, C. R. O., Haugaard‐Kedström, L. M., & Strømgaard, K. (2018) · ChemBioChem · doi:10.1002/cbic.201800004 · Cited by 8

Adenosine Receptors in Alzheimer’s Disease

Canas, P. M., Cunha, R. A., & Agostinho, P. M. (2018) · Springer eBooks · doi:10.1007/978-3-319-90808-3_11 · Cited by 8

Rapid evolution of mammalian APLP1 as a synaptic adhesion molecule

Onodera, W., Asahi, T., & Sawamura, N. (2021) · Scientific Reports · doi:10.1038/s41598-021-90737-y · Cited by 9

Increased P2×2 receptors induced by amyloid-β peptide participates in the neurotoxicity in alzheimer’s disease

Godoy, P. A., Mennickent, D., Cuchillo‐Ibáñez, I., Ramírez-Molina, O., Silva-Grecchi, T., Panes-Fernández, J., Castro, P. A., Sáez‐Valero, J., & Fuentealba, J. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111968 · Cited by 8

Amyloid-precursor Like Proteins APLP1 and APLP2 Are Dispensable for Normal Development of the Neonatal Respiratory Network

Han, K., Müller, U., & Hülsmann, S. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00189 · Cited by 8

An alternative processing pathway of APP reveals two distinct cleavage modes for rhomboid protease RHBDL4

Recinto, S. J., Paschkowsky, S., & Munter, L. M. (2018) · Biological Chemistry · doi:10.1515/hsz-2018-0259 · Cited by 8

Amyloid β interferes with wound healing of brain microvascular endothelial cells by disorganizing the actin cytoskeleton

Maeda, T., Shimamori, K., Kurita, H., Tokuraku, K., & Kuragano, M. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.113958 · Cited by 7

Iron responsive elements mRNA regulate Alzheimer’s amyloid precursor protein translation through iron sensing

Khan, M. A. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1483913 · Cited by 7

The amyloid precursor family of proteins in excitatory neurons are essential for regulating cortico-hippocampal circuit dynamics in vivo

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Advanced intranasal peptide delivery systems for improved management of Alzheimer's disease

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