A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain

Alzheimer's Disease: Genes, Proteins, and Therapy

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β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

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Amyloid Precursor Protein Processing and Alzheimer's Disease

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Mutant presenilins specifically elevate the levels of the 42 residue β-amyloid peptide in vivo: evidence for augmentation of a 42-specific γ secretase

Jankowsky, J. L., Fadale, D. J., Anderson, J., Xu, G. M., Gonzales, V., Jenkins, N. A., Copeland, N. G., Lee, M. K., Younkin, L. H., Wagner, S. L., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh019 · Cited by 1,575 · see citing works

A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity

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

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Review Article: Genetics of Alzheimer Disease

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Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future

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Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases

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Fringe is a glycosyltransferase that modifies Notch

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The amyloid hypothesis for Alzheimer’s disease: A critical reappraisal

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APP mouse models for Alzheimer’s disease preclinical studies.

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Loss of Presenilin Function Causes Impairments of Memory and Synaptic Plasticity Followed by Age-Dependent Neurodegeneration

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Direct inhibition of the NOTCH transcription factor complex

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History and progress of hypotheses and clinical trials for Alzheimer’s disease

Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723 · see citing works

Notch mediates TGFα-induced changes in epithelial differentiation during pancreatic tumorigenesis

Miyamoto, Y., Maitra, A., Ghosh, B., Zechner, U., Argani, P., Iacobuzio-Donahue, C. A., Sriuranpong, V., Iso, T., Meszoely, I. M., Wolfe, M. S., et al. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00140-5 · Cited by 643 · see citing works

Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP

Kamal, A., Almenar-Queralt, A., LeBlanc, J. F., Roberts, E. A., & Goldstein, L. S. B. (2001) · Nature · doi:10.1038/414643a · Cited by 583 · see citing works

The updated biology of hypoxia-inducible factor

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γ-Secretase, notch, Aβ and alzheimer's disease: Where do the presenilins fit in?

Sisodia, S. S., & St George-Hyslop, P. H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn785 · Cited by 512 · see citing works

A γ‐secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafish

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The Presenilins in Alzheimer's Disease--Proteolysis Holds the Key

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Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations

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Impaired neurogenesis is an early event in the etiology of familial Alzheimer’s disease in transgenic mice

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Canonical Notch Signaling Is Dispensable for the Maintenance of Adult Hematopoietic Stem Cells

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Recognition of the amyloid precursor protein by human γ-secretase

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

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MYRF is a membrane-associated transcription factor that autoproteolytically cleaves to directly activate myelin genes

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Alzheimer’s-Causing Mutations Shift Aβ Length by Destabilizing γ-Secretase-Aβn Interactions

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Critical role of endothelial Notch1 signaling in postnatal angiogenesis

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Amyloid precursor protein (APP) and the biology of proteolytic processing: relevance to Alzheimer’s disease

Ling, Y., Morgan, K., & Kalsheker, N. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00133-x · Cited by 224 · see citing works

Structural basis of γ-secretase inhibition and modulation by small molecule drugs

Yang, G., Zhou, R., Guo, X., Yan, C., Lei, J., & Shi, Y. (2021) · Cell · doi:10.1016/j.cell.2020.11.049 · Cited by 189 · see citing works

Notch-Dependent Repression of miR-155 in the Bone Marrow Niche Regulates Hematopoiesis in an NF-κB-Dependent Manner

Wang, L., Zhang, H., Rodriguez, S., Cao, L., Parish, J., Mumaw, C., Zollman, A., Kamoka, M. M., Mu, J., Chen, D. Z., et al. (2014) · Cell Stem Cell · doi:10.1016/j.stem.2014.04.021 · Cited by 186 · see citing works

The presenilin-1 ΔE9 mutation results in reduced γ-secretase activity, but not total loss of PS1 function, in isogenic human stem cells

Woodruff, G., Young, J. E., Martinez, F. J., Buen, F., Gore, A., Kinaga, J., Li, Z., Yuan, S. H., Zhang, K., & Goldstein, L. S. B. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.018 · Cited by 177 · see citing works

Alzheimer’s disease and hippocampal adult neurogenesis; exploring shared mechanisms

Hollands, C., Bartolotti, N., & Lazarov, O. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00178 · Cited by 160 · see citing works

Making the final cut: Pathogenic amyloid-β peptide generation by γ-secretase

Steiner, H., Fukumori, A., Tagami, S., & Okochi, M. (2018) · Cell Stress · doi:10.15698/cst2018.11.162 · Cited by 133 · see citing works

Biochemistry and Molecular Biology of Amyloid β‐Protein and the Mechanism of Alzheimer's Disease

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Presenilin-1 P264L Knock-In Mutation: Differential Effects on Aβ Production, Amyloid Deposition, and Neuronal Vulnerability

Siman, R., Reaume, A. G., Savage, M. J., Trusko, S., Lin, Y.-G., Scott, R. W., & Flood, D. G. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-23-08717.2000 · Cited by 133 · see citing works

Cancer and Alzheimer’s disease inverse relationship: an age-associated diverging derailment of shared pathways

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Tauroursodeoxycholic acid (TUDCA) supplementation prevents cognitive impairment and amyloid deposition in APP/PS1 mice

Lo, A. C., Callaerts-Vegh, Z., Nunes, A. F., Rodrigues, C. M. P., & D'Hooge, R. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.09.003 · Cited by 120 · see citing works

γ-secretase modulators and presenilin 1 mutants act differently on presenilin/γ-secretase function to cleave Aβ42 and Aβ43

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Bapineuzumab and solanezumab for Alzheimer's disease: is the ‘amyloid cascade hypothesis’ still alive?

Tayeb, H. O., Murray, E. D., Price, B. H., & Tarazi, F. I. (2013) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2013.789856 · Cited by 119 · see citing works

Disease modifying therapy for AD?¹

Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117 · see citing works

Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation

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Selective ferroptosis vulnerability due to familial Alzheimer’s disease presenilin mutations

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Expression Profiling of Lymphocyte Plasma Membrane Proteins

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Targeting Aβ and tau in Alzheimer's disease, an early interim report

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Preclinical validation of a potent γ-secretase modulator for Alzheimer’s disease prevention

Rynearson, K. D., Ponnusamy, M., Prikhodko, O., Xie, Y., Zhang, C., Nguyen, P., Hug, B., Sawa, M., Becker, A., Spencer, B., et al. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20202560 · Cited by 76 · see citing works

Function and Dysfunction of the Presenilins

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Modulation of γ-secretase by EVP-0015962 reduces amyloid deposition and behavioral deficits in Tg2576 mice

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Amyloid precursor protein-induced axonopathies are independent of amyloid-β peptides

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Mutations in APP have independent effects on Aβ and CTFγ generation

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Simvastatin increases notch signaling activity and promotes arteriogenesis after stroke

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Study on the relationship between hepatic fibrosis and epithelial-mesenchymal transition in intrahepatic cells

Chen, Y., Fan, Y., Guo, D.-Y., Xu, B., Shi, X.-Y., Li, J.-T., & Duan, L.-F. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110413 · Cited by 63 · see citing works

Notch/HES1-mediated PARP1 activation: a cell type–specific mechanism for tumor suppression

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A presenilin-1 mutation causes Alzheimer disease without affecting Notch signaling

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A novel mechanism for the regulation of amyloid precursor protein metabolism

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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

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

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

Cyclopamine Modulates γ-Secretase-mediated Cleavage of Amyloid Precursor Protein by Altering Its Subcellular Trafficking and Lysosomal Degradation

Vorobyeva, A. G., Lee, R., Miller, S., Longen, C., Sharoni, M., Kandelwal, P. J., Kim, F. J., Marenda, D. R., & Saunders, A. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.591792 · Cited by 16 · see citing works

TM2D genes regulate Notch signaling and neuronal function in Drosophila

Salazar, J. L., Yang, S.-A., Lin, Y. Q., Li-Kroeger, D., Marcogliese, P. C., Deal, S. L., Neely, G. G., & Yamamoto, S. (2021) · PLOS Genetics · doi:10.1371/journal.pgen.1009962 · Cited by 13 · see citing works