Aph-1, Pen-2, and Nicastrin with Presenilin Generate an Active γ-Secretase Complex

The Amyloid-β Pathway in Alzheimer’s Disease

Hampel, H., Hardy, J., Blennow, K., Chen, C., Perry, G., Kim, S. H., Villemagne, V. L., Aisen, P., Vendruscolo, M., Iwatsubo, T., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01249-0 · Cited by 1,952 · see citing works

Degradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies

Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898 · see citing works

Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs

Forman, M. S., Trojanowski, J. Q., & Lee, V. M.-Y. (2004) · Nature Medicine · doi:10.1038/nm1113 · Cited by 715 · see citing works

The Aging Brain

Yankner, B. A., Lu, T., & Loerch, P. (2008) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.2.010506.092044 · Cited by 677 · see citing works

Alzheimer’s Disease Genetics: From the Bench to the Clinic

Karch, C. M., Cruchaga, C., & Goate, A. M. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.041 · Cited by 473 · see citing works

The innate immunity protein IFITM3 modulates γ-secretase in Alzheimer’s disease

Hur, J.-Y., Frost, G. R., Wu, X., Crump, C., Pan, S. J., Wong, E., Barros, M., Li, T., Nie, P., Zhai, Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2681-2 · Cited by 382 · see citing works

Interferon-γ and Tumor Necrosis Factor-α Regulate Amyloid-β Plaque Deposition and β-Secretase Expression in Swedish Mutant APP Transgenic Mice

Yamamoto, M., Kiyota, T., Horiba, M., Buescher, J. L., Walsh, S. M., Gendelman, H. E., & Ikezu, T. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.060378 · Cited by 367 · see citing works

Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein

Cordy, J. M., Hussain, I., Dingwall, C., Hooper, N. M., & Turner, A. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1635130100 · Cited by 356 · see citing works

Mass spectrometric characterization of brain amyloid beta isoform signatures in familial and sporadic Alzheimer’s disease

Portelius, E., Bogdanovic, N., Gustavsson, M. K., Volkmann, I., Brinkmalm, G., Zetterberg, H., Winblad, B., & Blennow, K. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0690-1 · Cited by 348 · see citing works

Obesity‐related leptin regulates Alzheimer's Aβ

Fewlass, D. C., Noboa, K., Pi‐Sunyer, F. X., Johnston, J. M., Yan, S. D., & Tezapsidis, N. (2004) · The FASEB Journal · doi:10.1096/fj.04-2572com · Cited by 308 · see citing works

Rumi Is a CAP10 Domain Glycosyltransferase that Modifies Notch and Is Required for Notch Signaling

Acar, M., Jafar-Nejad, H., Takeuchi, H., Rajan, A., Ibrani, D., Rana, N. A., Pan, H., Haltiwanger, R. S., & Bellen, H. J. (2008) · Cell · doi:10.1016/j.cell.2007.12.016 · Cited by 306 · see citing works

The role of G protein-coupled receptors in the pathology of Alzheimer's disease

Thathiah, A., & De Strooper, B. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn2977 · Cited by 288 · see citing works

Lessons from a failed γ-secretase Alzheimer trial

De Strooper, B. (2014) · Cell · doi:10.1016/j.cell.2014.10.016 · Cited by 277 · see citing works

The role of metallobiology and amyloid-β peptides in Alzheimer's disease

Roberts, B. R., Ryan, T. M., Bush, A. I., Masters, C. L., & Duce, J. A. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07500.x · Cited by 266 · see citing works

Neurotherapeutic applications of nanoparticles in Alzheimer’s disease

Sahni, J. K., Doggui, S., Ali, J., Baboota, S., Dao, L., & Ramassamy, C. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2010.11.033 · Cited by 219 · see citing works

Prophylactic treatment with paroxetine ameliorates behavioral deficits and retards the development of amyloid and tau pathologies in 3xTgAD mice

NELSON, R., GUO, Z., HALAGAPPA, V, PEARSON, M., GRAY, A., MATSUOKA, Y., BROWN, M., MARTIN, B., IYUN, T., & MAUDSLEY, S. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.01.037 · Cited by 173 · see citing works

Presenilin-Dependent  -Secretase-Mediated Control of p53-Associated Cell Death in Alzheimer's Disease

Alves da Costa, C., Sunyach, C., Pardossi-Piquard, R., Sevalle, J., Vincent, B., Boyer, N., Kawarai, T., Girardot, N., St. George-Hyslop, P., & Checler, F. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0651-06.2006 · Cited by 168 · see citing works

A Role for Presenilins in Autophagy Revisited: Normal Acidification of Lysosomes in Cells Lacking PSEN1 and PSEN2

Zhang, X., Garbett, K., Veeraraghavalu, K., Wilburn, B., Gilmore, R., Mirnics, K., & Sisodia, S. S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0556-12.2012 · Cited by 122 · see citing works

The intracellular domain of CD44 promotes the fusion of macrophages

Cui, W. (2006) · Blood · doi:10.1182/blood-2005-05-1902 · Cited by 110 · see citing works

Alzheimer’s Disease and Inflammaging

Kosyreva, A., Sentyabreva, A., Tsvetkov, I., & Makarova, O. (2022) · Brain Sciences · doi:10.3390/brainsci12091237 · Cited by 98 · see citing works

Interleukins, Inflammation, and Mechanisms of Alzheimer's Disease

Weisman, D., Hakimian, E., & Ho, G. J. (2006) · Vitamins & Hormones · doi:10.1016/s0083-6729(06)74020-1 · Cited by 95 · see citing works

Axonal transport of APP and the spatial regulation of APP cleavage and function in neuronal cells

Brunholz, S., Sisodia, S., Lorenzo, A., Deyts, C., Kins, S., & Morfini, G. (2012) · Experimental Brain Research · doi:10.1007/s00221-011-2870-1 · Cited by 92 · see citing works

The PERK-Dependent Molecular Mechanisms as a Novel Therapeutic Target for Neurodegenerative Diseases

Rozpędek-Kamińska, W., Siwecka, N., Wawrzynkiewicz, A., Wojtczak, R., Pytel, D., Diehl, J. A., & Majsterek, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062108 · Cited by 84 · see citing works

Amyloid precursor protein (APP) May act as a substrate and a recognition unit for CRL4CRBN and Stub1 E3 ligases facilitating ubiquitination of proteins involved in presynaptic functions and neurodegeneration

Del Prete, D., Rice, R. C., Rajadhyaksha, A. M., & D'Adamio, L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.733626 · Cited by 86 · see citing works

Targeting autophagy in Alzheimer’s disease: Animal models and mechanisms

Zhang, X.-W., 澳门大学中华医药研究院中药质量研究国家重点实验室, 澳. 凼. 9., State Key Laboratory of Quality Research in Chinese Medicine, I. O. C. M. S., Zhu, X.-X., Tang, D.-S., Lu, J.-H., 佛山大学广东省动物分子设计与精准育种重点实验室, 广., & Guangdong Provincial Key Laboratory of Animal Molecular Design and Precise Breeding, G. E. T. C. O. G. P. (2023) · Zoological Research · doi:10.24272/j.issn.2095-8137.2023.294 · Cited by 77 · see citing works

Mutations in APP have independent effects on Aβ and CTFγ generation

Hecimovic, S., Wang, J., Dolios, G., Martinez, M., Wang, R., & Goate, A. M. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.04.018 · Cited by 70 · see citing works

Ubiquilin regulates presenilin endoproteolysis and modulates γ-secretase components, Pen-2 and nicastrin

Massey, L. K., Mah, A. L., & Monteiro, M. J. (2005) · Biochemical Journal · doi:10.1042/bj20050491 · Cited by 66 · see citing works

The effects of caloric restriction and its mimetics in Alzheimer's disease through autophagy pathways

Yang, Y., & Zhang, L. (2020) · Food & Function · doi:10.1039/c9fo02611h · Cited by 57 · see citing works

Turning the tide on Alzheimer’s disease: modulation of γ-secretase

Luo, J. E., & Li, Y.-M. (2022) · Cell & Bioscience · doi:10.1186/s13578-021-00738-7 · Cited by 59 · see citing works

Targeted Delivery of Notch Inhibitor Attenuates Obesity-Induced Glucose Intolerance and Liver Fibrosis

Richter, L. R., Wan, Q., Wen, D., Zhang, Y., Yu, J., Kang, J. K., Zhu, C., McKinnon, E. L., Gu, Z., Qiang, L., et al. (2020) · ACS Nano · doi:10.1021/acsnano.0c01007 · Cited by 59 · see citing works

γ-Secretase and its modulators: Twenty years and beyond

Xia, W. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.02.011 · Cited by 54 · see citing works

LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking

Ranganathan, S., Noyes, N. C., Migliorini, M., Winkles, J. A., Battey, F. D., Hyman, B. T., Smith, E., Yepes, M., Mikhailenko, I., & Strickland, D. K. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5065-10.2011 · Cited by 49 · see citing works

β-amyloid: The known unknowns

Ayton, S., & Bush, A. I. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101212 · Cited by 45 · see citing works

Enhanced Accumulation of Phosphorylated α-Synuclein and Elevated β-Amyloid 42/40 Ratio Caused by Expression of the Presenilin-1 ΔT440 Mutant Associated with Familial Lewy Body Disease and Variant Alzheimer's Disease

Kaneko, H., Kakita, A., Kasuga, K., Nozaki, H., Ishikawa, A., Miyashita, A., Kuwano, R., Ito, G., Iwatsubo, T., Takahashi, H., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4244-07.2007 · Cited by 44 · see citing works

New precision medicine avenues to the prevention of Alzheimer’s disease from insights into the structure and function of γ-secretases

De Strooper, B., & Karran, E. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00057-w · Cited by 36 · see citing works

MicroRNAs targeting Nicastrin regulate Aβ production and are affected by target site polymorphisms

Delay, C., Dorval, V., Fok, A., Grenier-Boley, B., Lambert, J.-C., Hsiung, G.-Y., & Hébert, S. S. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00067 · Cited by 28 · see citing works

Molecular signatures of neurodegeneration in the cortex of PS1/PS2 double knockout mice

Mirnics, K., Norstrom, E. M., Garbett, K., Choi, S., Zhang, X., Ebert, P., & Sisodia, S. S. (2008) · Molecular Neurodegeneration · doi:10.1186/1750-1326-3-14 · Cited by 23 · see citing works

Microbial infection promotes amyloid pathology in a mouse model of Alzheimer’s disease via modulating γ-secretase

Zhao, M., Ma, G., Yan, X., Li, X., Wang, E., Xu, X.-X., Zhao, J.-B., Ma, X., & Zeng, J. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02428-5 · Cited by 21 · see citing works

Widespread γ-secretase activity in the cell, but do we need it at the mitochondria?

Teng, F. Y. H., & Tang, B. L. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.131 · Cited by 21 · see citing works

Amyloid precursor protein processing in human neurons with an allelic series of the PSEN1 intron 4 deletion mutation and total presenilin-1 knockout.

Arber, C., Villegas-Llerena, C., Toombs, J., Pocock, J. M., Ryan, N. S., Fox, N. C., Zetterberg, H., Hardy, J., & Wray, S. (2019) · Brain Communications · doi:10.1093/braincomms/fcz024 · Cited by 19 · see citing works

BACE1 Is Necessary for Experience-Dependent Homeostatic Synaptic Plasticity in Visual Cortex

Petrus, E., & Lee, H.-K. (2014) · Neural Plasticity · doi:10.1155/2014/128631 · Cited by 19 · see citing works

γ-Secretase Inhibitors Selected by Molecular Docking, to Develop a New Drug Against Alzheimer’s Disease

Trasviña-Arenas, C. H., Ayala Medina, L. A., & Vique-Sanchez, J. L. (2023) · Reports of Biochemistry and Molecular Biology · doi:10.61186/rbmb.12.2.340 · Cited by 5 · see citing works

Covalent fragment inhibits intramembrane proteolysis

Eden, A., Zhao, J., Xiao, Y., Gibson, J., & Wang, C. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.958399 · Cited by 3 · see citing works