Lessons from a failed γ-secretase Alzheimer trial

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

Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · see citing works

The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics

Karran, E., Mercken, M., & Strooper, B. D. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3505 · Cited by 2,188 · see citing works

Amyloid β-peptide is produced by cultured cells during normal metabolism

Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921 · see citing works

Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein

De Strooper, B., Saftig, P., Craessaerts, K., Vanderstichele, H., Guhde, G., Annaert, W., Von Figura, K., & Van Leuven, F. (1998) · Nature · doi:10.1038/34910 · Cited by 1,818 · see citing works

A Phase 3 Trial of Semagacestat for Treatment of Alzheimer's Disease

Doody, R. S., Raman, R., Farlow, M., Iwatsubo, T., Vellas, B., Joffe, S., Kieburtz, K., He, F., Sun, X., Thomas, R. G., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1210951 · Cited by 1,224 · see citing works

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

De Strooper, B. (2003) · Neuron · doi:10.1016/s0896-6273(03)00205-8 · Cited by 965 · see citing works

Skeletal and CNS Defects in Presenilin-1-Deficient Mice

Shen, J., Bronson, R. T., Chen, D. F., Xia, W., Selkoe, D. J., & Tonegawa, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80244-5 · Cited by 808 · see citing works

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

Saura, C. A., Choi, S.-Y., Beglopoulos, V., Malkani, S., Zhang, D., Rao, B. S. S., Chattarji, S., Kelleher, R. J., Kandel, E. R., Duff, K., et al. (2004) · Neuron · doi:10.1016/s0896-6273(04)00182-5 · Cited by 757 · see citing works

Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice

McGowan, E., Pickford, F., Kim, J., Onstead, L., Eriksen, J., Yu, C., Skipper, L., Murphy, M. P., Beard, J., Das, P., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.030 · Cited by 565 · see citing works

Neurotoxicity of Alzheimer’s disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio

Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., Vandersteen, A., Segers‐Nolten, I., Van Der Werf, K., Subramaniam, V., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.211 · Cited by 532 · see citing works

Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease

Weihofen, A., Binns, K. L., Lemberg, M. K., Ashman, K., & Martoglio, B. (2002) · Science · doi:10.1126/science.1070925 · Cited by 532 · see citing works

The mechanism of γ‐Secretase dysfunction in familial Alzheimer disease

Chávez‐Gutiérrez, L., Bammens, L., Benilova, I., Vandersteen, A., Benurwar, M., Borgers, M., Lismont, S., Zhou, L., Van Cleynenbreugel, S., Esselmann, H., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.79 · Cited by 495 · see citing works

Not(ch) just development: Notch signalling in the adult brain

Ables, J. L., Breunig, J. J., Eisch, A. J., & RAKIC, P. T. (2011) · Nature reviews. Neuroscience · doi:10.1038/nrn3024 · Cited by 460 · see citing works

Notch Inhibition Induces Cochlear Hair Cell Regeneration and Recovery of Hearing after Acoustic Trauma

Mizutari, K., Fujioka, M., Hosoya, M., Bramhall, N. F., Okano, H. J., Okano, H., & Edge, A. S. B. (2013) · Neuron · doi:10.1016/j.neuron.2012.10.032 · Cited by 398 · see citing works

Three-dimensional structure of human γ-secretase

Lu, P., Bai, X., Ma, D., Xie, T., Yan, C., Sun, L., Yang, G., Zhao, Y., Zhou, R., Scheres, S. H. W., et al. (2014) · Nature · doi:10.1038/nature13567 · Cited by 345 · see citing works

A γ‐secretase inhibitor decreases amyloid‐β production in the central nervous system

Bateman, R. J., Siemers, E. R., Mawuenyega, K. G., Wen, G., Browning, K. R., Sigurdson, W. C., Yarasheski, K. E., Friedrich, S. W., DeMattos, R. B., May, P. C., et al. (2009) · Annals of Neurology · doi:10.1002/ana.21623 · Cited by 322 · see citing works

Presenilins are essential for regulating neurotransmitter release

Zhang, C., Wu, B., Beglopoulos, V., Wines-Samuelson, M., Zhang, D., Dragatsis, I., Südhof, T. C., & Shen, J. (2009) · Nature · doi:10.1038/nature08177 · Cited by 280 · see citing works

A critique of the drug discovery and phase 3 clinical programs targeting the amyloid hypothesis for Alzheimer disease

Karran, E. H., & Hardy, J. (2014) · Annals of Neurology · doi:10.1002/ana.24188 · Cited by 275 · see citing works

γ-Secretase Heterogeneity in the Aph1 Subunit: Relevance for Alzheimer’s Disease

Serneels, L., Biervliet, J. V., Craessaerts, K., Dejaegere, T., Horré, K., Houtvin, T. V., Esselmann, H., Paul, S., Schäfer, M., Berezovska, O., et al. (2009) · Science · doi:10.1126/science.1171176 · Cited by 259 · see citing works

Differential Effects between γ-Secretase Inhibitors and Modulators on Cognitive Function in Amyloid Precursor Protein-Transgenic and Nontransgenic Mice

Mitani, Y., Yarimizu, J., Saita, K., Uchino, H., Akashiba, H., Shitaka, Y., Ni, K., & Matsuoka, N. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4264-11.2012 · Cited by 203 · see citing works

Activity-Induced Notch Signaling in Neurons Requires Arc/Arg3.1 and Is Essential for Synaptic Plasticity in Hippocampal Networks

Alberi, L. A., Liu, S., Wang, Y. J., Badie, R., Smith‐Hicks, C. L., Wu, J., Pierfelice, T. J., Abazyan, B. N., Mattson, M. P., Kuhl, D., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.01.004 · Cited by 199 · see citing works

Structure of a presenilin family intramembrane aspartate protease

Li, X., Dang, S., Yan, C., Gong, X., Wang, J., & Shi, Y. (2012) · Nature · doi:10.1038/nature11801 · Cited by 186 · see citing works

Differential contribution of the three Aph1 genes to γ-secretase activity in vivo

Serneels, L., Dejaegere, T., Craessaerts, K., Horré, K., Jorissen, E., Tousseyn, T., Hébert, S. S., Coolen, M. W., Martens, G. J. M., Zwijsen, A., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408901102 · Cited by 179 · see citing works

Nicastrin Is Required for Assembly of Presenilin/γ-Secretase Complexes to Mediate Notch Signaling and for Processing and Trafficking of β-Amyloid Precursor Protein in Mammals

Li, T., Ma, G., Cai, H., Price, D. L., & Wong, P. C. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-08-03272.2003 · Cited by 178 · see citing works

Identification of a novel family of presenilin homologues

Ponting, C. P. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.9.1037 · Cited by 173 · see citing works

Dynamic regulation of Notch signaling in neural progenitor cells

Kageyama, R., Ohtsuka, T., Shimojo, H., & Imayoshi, I. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.08.009 · Cited by 150 · see citing works

A fast growing spectrum of biological functions of γ-secretase in development and disease

Jurisch‐Yaksi, N., Sannerud, R., & Annaert, W. G. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.04.016 · Cited by 140 · see citing works

Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases

Voß, M., Schröder, B., & Fluhrer, R. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.03.033 · Cited by 135 · see citing works

Concentration-Dependent Modulation of Amyloid-β in Vivo and in Vitro Using the γ-Secretase Inhibitor, LY-450139

Lanz, T. A., Karmilowicz, M. J., Wood, K. M., Pozdnyakov, N., Du, P., Piotrowski, M. A., Brown, T. M., Nolan, C. E., Richter, K. E. G., Finley, J. E., et al. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.110700 · Cited by 133 · see citing works

Studies of Aβ Pharmacodynamics in the Brain, Cerebrospinal Fluid, and Plasma in Young (Plaque-Free) Tg2576 Mice Using the γ-Secretase Inhibitor N2-[(2 S)-2-(3,5-Difluorophenyl)-2-hydroxyethanoyl]-N1-[(7 S)-5-methyl-6-oxo-6,7-dihydro-5 H-dibenzo[b,d]azepin-7-yl]-L-alaninamide (LY-411575)

Lanz, T. A., Hosley, J. D., Adams, W. J., & Merchant, K. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.103.060715 · Cited by 130 · see citing works

Therapeutic approaches to modulating Notch signaling: Current challenges and future prospects

Groth, C., & Fortini, M. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.01.016 · Cited by 121 · see citing works

APH-1a Is the Principal Mammalian APH-1 Isoform Present in γ-Secretase Complexes during Embryonic Development

Ma, G., Li, T., Price, D. L., & Wong, P. C. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3814-04.2005 · Cited by 102 · see citing works

Safety profile of semagacestat, a gamma-secretase inhibitor: IDENTITY trial findings

Henley, D. B., Sundell, K. L., Sethuraman, G., Dowsett, S. A., & May, P. C. (2014) · Current Medical Research and Opinion · doi:10.1185/03007995.2014.939167 · Cited by 98 · see citing works

BMS-708,163 Targets Presenilin and Lacks Notch-Sparing Activity

Crump, C. J., Castro, S. V., Wang, F., Pozdnyakov, N., Ballard, T. E., Sisodia, S. S., Bales, K. R., Johnson, D. S., & Li, Y. (2012) · Biochemistry · doi:10.1021/bi301137h · Cited by 95 · see citing works

Spike bursts increase amyloid-β 40/42 ratio by inducing a presenilin-1 conformational change

Dolev, I., Fogel, H., Milshtein-Parush, H., Berdichevsky, Y., Lipstein, N., Brose, N., Gazit, N., & Slutsky, I. (2013) · Nature Neuroscience · doi:10.1038/nn.3376 · Cited by 87 · see citing works

Signal Peptide Peptidase Forms a Homodimer That Is Labeled by an Active Site-directed γ-Secretase Inhibitor

Nyborg, A. C., Kornilova, A. Y., Jansen, K. R., Ladd, T. B., Wolfe, M. S., & Golde, T. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309305200 · Cited by 81 · see citing works

Novel Class of Polytopic Proteins with Domains Associated with Putative Protease Activity

Grigorenko, A. P., Moliaka, Y., Коровайцева, Г. И., & Rogaev, E. I. (2002) · Biochemistry (Moscow) · doi:10.1023/a:1016365227942 · Cited by 71 · see citing works

Ultradian Oscillations in Notch Signaling Regulate Dynamic Biological Events

Kageyama, R., Niwa, Y., Shimojo, H., Kobayashi, T., & Ohtsuka, T. (2010) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(10)92010-3 · Cited by 61 · see citing works

A technical KO of amyloid-β peptide

Haass, C., & Selkoe, D. J. (1998) · Nature · doi:10.1038/34800 · Cited by 53 · see citing works

Notch-Inducible Hyperphosphorylated CREB and Its Ultradian Oscillation in Long-Term Memory Formation

Zhang, J., Little, C. J., Tremmel, D. M., Yin, J. C. P., & Wesley, C. S. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.0783-13.2013 · Cited by 46 · see citing works

Alzheimer's Disease: Presenilin 2-Sparing γ-Secretase Inhibition Is a Tolerable Aβ Peptide-Lowering Strategy

Borgegård, T., Gustavsson, S., Nilsson, C. B., Parpal, S., Klintenberg, R., Berg, A., Rosqvist, S., Serneels, L., Svensson, S., Olsson, F., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1451-12.2012 · Cited by 43 · see citing works

Amyloid-β1-15/16 as a Marker for γ-Secretase Inhibition in Alzheimer's Disease

Portelius, E., Zetterberg, H., Dean, R. A., Marcil, A., Bourgeois, P., Nutu, M., Andréasson, U., Siemers, E., Mawuenyega, K. G., Sigurdson, W. C., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120508 · Cited by 42 · see citing works

Discovery of (R)-4-Cyclopropyl-7,8-difluoro-5-(4-(trifluoromethyl)phenylsulfonyl)-4,5-dihydro-1H-pyrazolo[4,3-c]quinoline (ELND006) and (R)-4-Cyclopropyl-8-fluoro-5-(6-(trifluoromethyl)pyridin-3-ylsulfonyl)-4,5-dihydro-2H-pyrazolo[4,3-c]quinoline (ELND007): Metabolically Stable γ-Secretase Inhibitors that Selectively Inhibit the Production of Amyloid-β over Notch

Probst, G. D., Aubele, D. L., Bowers, S., Dressen, D. B., Garofalo, A. W., Hom, R. K., Konradi, A. W., Marugg, J. L., Mattson, M. N., Neitzel, M. L., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301741t · Cited by 36 · see citing works

Three-dimensional Structure of the Signal Peptide Peptidase

Miyashita, H., Maruyama, Y., Isshiki, H., Osawa, S., Ogura, T., Mio, K., Sato, C., Tomita, T., & Iwatsubo, T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.260273 · Cited by 26 · see citing works

Disposition and Metabolism of Semagacestat, a γ-Secretase Inhibitor, in Humans

Yi, P., Hadden, C. E., Kulanthaivel, P., Calvert, N. A., Annes, W. F., Brown, T. J., Barbuch, R. J., Chaudhary, A., Ayan‐Oshodi, M., & Ring, B. J. (2010) · Drug Metabolism and Disposition · doi:10.1124/dmd.109.030841 · Cited by 23 · see citing works

The amyloid hypothesis of Alzheimer's disease at 25 years

Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164 · see citing works

Alzheimer Disease: An Update on Pathobiology and Treatment Strategies

Long, J. M., & Holtzman, D. M. (2019) · Cell · doi:10.1016/j.cell.2019.09.001 · Cited by 3,204 · see citing works

The Cellular Phase of Alzheimer’s Disease

De Strooper, B., & Karran, E. (2016) · Cell · doi:10.1016/j.cell.2015.12.056 · Cited by 1,990 · see citing works

Defeating Alzheimer's disease and other dementias: a priority for European science and society

Winblad, B., Amouyel, P., Andrieu, S., Ballard, C., Brayne, C., Brodaty, H., Cedazo-Minguez, A., Dubois, B., Edvardsson, D., Feldman, H., et al. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)00062-4 · Cited by 1,676 · see citing works

APP mouse models for Alzheimer’s disease preclinical studies.

Sasaguri, H., Nilsson, P., Hashimoto, S., Nagata, K., Saito, T., De Strooper, B., Hardy, J., Vassar, R., Winblad, B., & Saido, T. C. (2017) · The EMBO Journal · doi:10.15252/embj.201797397 · Cited by 793 · see citing works

The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics

Karran, E., & De Strooper, B. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00391-w · Cited by 742 · see citing works

The β-Secretase BACE1 in Alzheimer’s Disease

Hampel, H., Vassar, R., De Strooper, B., Hardy, J., Willem, M., Singh, N., Zhou, J., Yan, R., Vanmechelen, E., De Vos, A., et al. (2021) · Biological Psychiatry · doi:10.1016/j.biopsych.2020.02.001 · Cited by 694 · see citing works

The road to restoring neural circuits for the treatment of Alzheimer's disease

Canter, R. G., Penney, J., & Tsai, L.-H. (2016) · Nature · doi:10.1038/nature20412 · Cited by 565 · see citing works

Self-Organizing 3D Human Neural Tissue Derived from Induced Pluripotent Stem Cells Recapitulate Alzheimer’s Disease Phenotypes

Raja, W. K., Mungenast, A. E., Lin, Y.-T., Ko, T., Abdurrob, F., Seo, J., & Tsai, L.-H. (2016) · PLOS ONE · doi:10.1371/journal.pone.0161969 · Cited by 569 · see citing works

Sampling the conformational space of the catalytic subunit of human γ-secretase

Bai, X., Rajendra, E., Yang, G., Shi, Y., & Scheres, S. H. W. (2015) · eLife · doi:10.7554/elife.11182 · Cited by 554 · see citing works

An atomic structure of human γ-secretase

Bai, X., Yan, C., Yang, G., Lu, P., Ma, D., Sun, L., Zhou, R., Scheres, S. H. W., & Shi, Y. (2015) · Nature · doi:10.1038/nature14892 · Cited by 499 · see citing works

Spheroids as a Type of Three-Dimensional Cell Cultures—Examples of Methods of Preparation and the Most Important Application

Białkowska, K., Komorowski, P., Bryszewska, M., & Miłowska, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176225 · Cited by 341 · see citing works

The amyloid cascade hypothesis: are we poised for success or failure?

Karran, E., & De Strooper, B. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13632 · Cited by 402 · see citing works

Comprehensive review of mechanisms of pathogenesis involved in Alzheimer’s disease and potential therapeutic strategies

Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331 · see citing works

In vitro Models of Neurodegenerative Diseases

Slanzi, A., Iannoto, G., Rossi, B., Zenaro, E., & Constantin, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00328 · Cited by 293 · see citing works

The amyloid cascade hypothesis: an updated critical review

Kepp, K. P., Robakis, N. K. R. K., Høilund‐Carlsen, P. F., Sensi, S. L., & Vissel, B. (2023) · Brain · doi:10.1093/brain/awad159 · Cited by 294 · see citing works

Sodium rutin ameliorates Alzheimer’s disease–like pathology by enhancing microglial amyloid-β clearance

Pan, R., Ma, J., Kong, X.-X., Wang, X., Li, S., Qi, X., Yan, Y., Cheng, J., Liu, Q., Jin, W., et al. (2019) · Science Advances · doi:10.1126/sciadv.aau6328 · Cited by 290 · see citing works

iPSC-Based Compound Screening and In Vitro Trials Identify a Synergistic Anti-amyloid β Combination for Alzheimer’s Disease

Kondo, T., Imamura, K., Funayama, M., Tsukita, K., Miyake, M., Ohta, A., Woltjen, K., Nakagawa, M., Asada, T., Arai, T., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.109 · Cited by 221 · see citing works

The role of the immune system in Alzheimer disease: Etiology and treatment

Jevtic, S. D., Sengar, A. S., Salter, M. W., & McLaurin, J. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.08.005 · Cited by 218 · see citing works

A Close Look at BACE1 Inhibitors for Alzheimer’s Disease Treatment

Das, B., & Yan, R. (2019) · CNS Drugs · doi:10.1007/s40263-019-00613-7 · Cited by 169 · 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

The substrate repertoire of γ-secretase/presenilin

Güner, G., & Lichtenthaler, S. F. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.05.019 · Cited by 195 · see citing works

Neurobiology of Alzheimer’s Disease: Integrated Molecular, Physiological, Anatomical, Biomarker, and Cognitive Dimensions

Raskin, J., Cummings, J. L., Hardy, J., Schuh, K. J., & Dean, R. A. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150701103107 · Cited by 190 · see citing works

Secretase inhibitors for the treatment of Alzheimer's disease: Long road ahead

Kumar, D., Ganeshpurkar, A., Kumar, D., Modi, G. P., Gupta, S., & Singh, S. K. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.02.035 · Cited by 170 · see citing works

BACE1 Physiological Functions May Limit Its Use as Therapeutic Target for Alzheimer's Disease.

Barão, S., Moechars, D., Lichtenthaler, S., & de Strooper, B. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.01.003 · Cited by 161 · see citing works

The Regulation of Astrocytic Glutamate Transporters in Health and Neurodegenerative Diseases

Todd, A., & Hardingham, G. E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249607 · Cited by 170 · see citing works

HMGB1, a pathogenic molecule that induces neurite degeneration via TLR4-MARCKS, is a potential therapeutic target for Alzheimer’s disease

Fujita, K., Motoki, K., Tagawa, K., Chen, X., Hama, H., Nakajima, K., Homma, H., Tamura, T., Watanabe, H., Katsuno, M., et al. (2016) · Scientific Reports · doi:10.1038/srep31895 · Cited by 160 · see citing works

The mutational landscape of a prion-like domain

Bolognesi, B., Faure, A. J., Seuma, M., Schmiedel, J. M., Tartaglia, G. G., & Lehner, B. (2019) · Nature Communications · doi:10.1038/s41467-019-12101-z · Cited by 159 · see citing works

Alzheimer’s disease: How metal ions define β-amyloid function

Kepp, K. P. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.05.007 · Cited by 151 · see citing works

Liver Dysfunction as a Novel Player in Alzheimer’s Progression: Looking Outside the Brain

Estrada, L. D., Ahumada, P., Cabrera, D., & Arab, J. P. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00174 · Cited by 144 · see citing works

The case for low-level BACE1 inhibition for the prevention of Alzheimer disease

McDade, E., Voytyuk, I., Aisen, P., Bateman, R., Carrillo, M., de Strooper, B., Haass, C., Reiman, E., Sperling, R., Tariot, P., et al. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-021-00545-1 · Cited by 129 · see citing works

The amyloid-beta forming tripeptide cleavage mechanism of γ-secretase

Bolduc, D. M., Montagna, D. R., Seghers, M., Wolfe, M. S., & Selkoe, D. J. (2016) · eLife · doi:10.7554/elife.17578 · Cited by 141 · see citing works

Gamma Secretase Modulators: New Alzheimer’s Drugs on the Horizon?

Bursavich, M. G., Harrison, B. A., & Blain, J. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01960 · Cited by 141 · see citing works

Alzheimer’s disease due to loss of function: A new synthesis of the available data

Kepp, K. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.004 · Cited by 123 · see citing works

3D culture models of Alzheimer’s disease: a road map to a “cure-in-a-dish”

Choi, S. H., Kim, Y. H., Quinti, L., Tanzi, R. E., & Kim, D. Y. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0139-7 · Cited by 132 · see citing works

Alzheimer's Disease Mechanisms and Emerging Roads to Novel Therapeutics

Sala Frigerio, C., & De Strooper, B. (2016) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-070815-014015 · Cited by 116 · see citing works

Associations Between Hepatic Functions and Plasma Amyloid-Beta Levels—Implications for the Capacity of Liver in Peripheral Amyloid-Beta Clearance

Wang, Y., Wang, Q., Zhang, T., Liu, Y.-H., Yao, X., Zeng, F., Li, J., Zhou, F.-Y., Wang, L., Yan, J.-C., et al. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9826-1 · Cited by 119 · see citing works

Precision pharmacology for Alzheimer’s disease

Hampel, H. J., Vergallo, A., Aguilar, L. F., Benda, N., Broich, K., Cuello, A. C., Cummings, J. L., Dubois, B., Federoff, H. J., Fiandaca, M. S., et al. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.02.014 · Cited by 112 · see citing works

Beta-Site Amyloid Precursor Protein Cleaving Enzyme 1 Inhibition Impairs Synaptic Plasticity via Seizure Protein 6

Zhu, K., Xiang, X., Filser, S., Marinković, P., Dorostkar, M. M., Crux, S., Neumann, U., Shimshek, D. R., Rammes, G., Haass, C., et al. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2016.12.023 · Cited by 107 · see citing works

Dysregulation of Intracellular Calcium Signaling in Alzheimer's Disease

Александровна, П. Е., Pchitskaya, E. I., & Борисович, Б. И. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7506 · Cited by 102 · see citing works

Alzheimer’s disease beyond amyloid: Can the repetitive failures of amyloid-targeted therapeutics inform future approaches to dementia drug discovery?

Mullane, K., & Williams, M. J. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113945 · Cited by 106 · see citing works

RAGE mediates Aβ accumulation in a mouse model of Alzheimer’s disease via modulation of β- and γ-secretase activity

Fang, F., Yu, Q., Arancio, O., Chen, D., Gore, S. S., Yan, S. S., & Yan, S. F. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy017 · Cited by 103 · see citing works

Alzheimer's in 3D culture: Challenges and perspectives

D'Avanzo, C., Aronson, J., Kim, Y. H., Choi, S. H., Tanzi, R. E., & Kim, D. Y. (2015) · BioEssays · doi:10.1002/bies.201500063 · Cited by 111 · see citing works

Alzheimer’s disease (AD) therapeutics – 1: Repeated clinical failures continue to question the amyloid hypothesis of AD and the current understanding of AD causality

Mullane, K., & Williams, M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.09.026 · Cited by 98 · see citing works

Trafficking and proteolytic processing of amyloid precursor protein and secretases in Alzheimer's disease development: An up-to-date review

Yuksel, M., & Tacal, Ö. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172415 · Cited by 94 · see citing works

Small-molecule induction of Aβ-42 peptide production in human cerebral organoids to model Alzheimer's disease associated phenotypes

Pavoni, S., Jarray, R., Nassor, F., Guyot, A.-C., Cottin, S., Rontard, J., Mikol, J., Mabondzo, A. M., Deslys, J., & Yates, F. (2018) · PLoS ONE · doi:10.1371/journal.pone.0209150 · Cited by 95 · see citing works

Copper imbalance in Alzheimer’s disease: Convergence of the chemistry and the clinic

Kepp, K. P., & Squitti, R. (2019) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2019.06.018 · Cited by 90 · see citing works

BACE1 inhibition more effectively suppresses initiation than progression of β-amyloid pathology

Peters, F., Salihoglu, H., Rodrigues, E. F., Herzog, É., Blume, T., Filser, S., Dorostkar, M. M., Shimshek, D. R., Brose, N., Neumann, U., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-017-1804-9 · Cited by 86 · see citing works

Loss of GPR3 reduces the amyloid plaque burden and improves memory in Alzheimer’s disease mouse models

Huang, Y., Skwarek‐Maruszewska, A., Horré, K., Vandewyer, E., Wolfs, L., Snellinx, A., Saito, T., Radaelli, E., Corthout, N., Colombelli, J., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aab3492 · Cited by 90 · see citing works

Familial Alzheimer’s disease–associated presenilin 1 mutants promote γ-secretase cleavage of STIM1 to impair store-operated Ca 2+ entry

Tong, B. C., Lee, C. S.-K., Cheng, W.-H., Lai, K., Foskett, J. K., & Cheung, K. (2016) · Science Signaling · doi:10.1126/scisignal.aaf1371 · Cited by 87 · see citing works

Ten Challenges of the Amyloid Hypothesis of Alzheimer’s Disease

Kepp, K. P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160550 · Cited by 80 · see citing works

Phase II clinical trials of anti–amyloid β antibodies: When is enough, enough?

Gold, M. (2017) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2017.04.005 · Cited by 75 · see citing works

Semagacestat Is a Pseudo-Inhibitor of γ-Secretase

Tagami, S., Yanagida, K., Kodama, T. S., Takami, M., Mizuta, N., Ōyama, H., Nishitomi, K., Chiu, Y.-W., Okamoto, T., Ikeuchi, T., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.032 · Cited by 73 · see citing works

A randomized, exploratory molecular imaging study targeting amyloid β with a novel 8‐OH quinoline in Alzheimer's disease: The PBT2‐204 IMAGINE study

Villemagne, V. L., Rowe, C. C., Barnham, K. J., Cherny, R. A., Woodward, M., Bozinosvski, S., Salvado, O., Bourgeat, P., Perez, K. A., Fowler, C. J., et al. (2017) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2017.10.001 · Cited by 72 · see citing works

Pharmacotherapy of Alzheimer’s Disease: Seeking Clarity in a Time of Uncertainty

Ibrahim, N. H., Yahaya, M. F., Mohamed, W. M. Y., Teoh, S. L., Hui, C. K., & Kumar, J. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00261 · Cited by 73 · see citing works

Inhibiting BACE1 to reverse synaptic dysfunctions in Alzheimer’s disease

Yan, R., Fan, Q., Zhou, J., & Vassar, R. J. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.03.025 · Cited by 71 · see citing works

BACE2 distribution in major brain cell types and identification of novel substrates

Voytyuk, I., Müller, S. A., Herber, J., Snellinx, A., Moechars, D., Loo, G., Lichtenthaler, S. F., & Strooper, B. D. (2018) · Life Science Alliance · doi:10.26508/lsa.201800026 · Cited by 69 · see citing works

In vivo functions of p75NTR: challenges and opportunities for an emerging therapeutic target

Malik, S. C., Sözmen, E. G., Baeza-Raja, B., Moan, N. L., Akassoglou, K., & Schachtrup, C. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.06.006 · Cited by 69 · see citing works

Modulation of γ- and β-secretases as early prevention against Alzheimer's disease

Voytyuk, I., De Strooper, B., & Chávez-Gutiérrez, L. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.08.001 · Cited by 67 · see citing works

Notch1 hallmarks fibrillary depositions in sporadic Alzheimer’s disease

Brai, E., Raio, N. A., & Alberi, L. A. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0327-2 · Cited by 63 · see citing works

Cognitive-Enhancing Effects of a Polyphenols-Rich Extract from Fruits without Changes in Neuropathology in an Animal Model of Alzheimer’s Disease

Dal‐Pan, A., Dudonné, S., Bourassa, P., Bourdoulous, M., Tremblay, C., Desjardins, Y., & Calon, F. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160281 · Cited by 62 · see citing works

Antagonistic Effects of BACE1 and APH1B-γ-Secretase Control Axonal Guidance by Regulating Growth Cone Collapse

Barão, S., Gärtner, A., Leyva‐Díaz, E., Demyanenko, G. P., Munck, S., Vanhoutvin, T., Zhou, L., Schachner, M., López‐Bendito, G., Maness, P. F., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.059 · Cited by 63 · 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

Dual BACE1 and Cholinesterase Inhibitory Effects of Phlorotannins from Ecklonia cava—An In Vitro and in Silico Study

Lee, J., & Jun, M. (2019) · Marine Drugs · doi:10.3390/md17020091 · Cited by 58 · see citing works

Mechanisms of neurodegeneration — Insights from familial Alzheimer’s disease

Chávez‐Gutiérrez, L., & Szaruga, M. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.03.005 · Cited by 54 · see citing works

A Novel, Multi-Target Natural Drug Candidate, Matrine, Improves Cognitive Deficits in Alzheimer’s Disease Transgenic Mice by Inhibiting Aβ Aggregation and Blocking the RAGE/Aβ Axis

Cui, L., Cai, Y., Cheng, W., Liu, G., Zhao, J., Cao, H., Tao, H., Wang, Y., Yin, M., Liu, T., et al. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9783-8 · Cited by 57 · see citing works

Functions of the Alzheimer’s Disease Protease BACE1 at the Synapse in the Central Nervous System

Munro, K. M., Nash, A., Pigoni, M., Lichtenthaler, S. F., & Gunnersen, J. M. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0800-1 · Cited by 55 · see citing works

Drug delivery strategies with lipid-based nanoparticles for Alzheimer’s disease treatment

Jang, Y.-J., Kang, S.-J., Park, H. S., Lee, D., Kim, J. H., Kim, J.-E., Kim, D., Chung, C., Yoon, J., & Bhang, S. H. (2025) · Journal of Nanobiotechnology · doi:10.1186/s12951-025-03109-3 · Cited by 62 · see citing works

Evaluation of Functional Decline in Alzheimer’s Dementia Using 3D Deep Learning and Group ICA for rs-fMRI Measurements

Qureshi, M. N. I., Ryu, S., Song, J., Lee, K. H., & Lee, B. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00008 · Cited by 53 · see citing works

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

Chang, J. L., Hinrich, A. J., Roman, B., Norrbom, M., Rigo, F., Marr, R. A., Norstrom, E. M., & Hastings, M. L. (2018) · Molecular Therapy · doi:10.1016/j.ymthe.2018.02.029 · Cited by 52 · see citing works

Amyloid-PET predicts inhibition of de novo plaque formation upon chronic γ-secretase modulator treatment

Brendel, M., Jaworska, A. M., Herms, J. W., Trambauer, J., Rötzer, C., Gildehaus, F.-J., Carlsen, J., Cumming, P. D., Bylund, J., Luebbers, T., et al. (2015) · Molecular Psychiatry · doi:10.1038/mp.2015.74 · Cited by 49 · see citing works

Loss of stability and hydrophobicity of presenilin 1 mutations causing Alzheimer's disease

Somavarapu, A. K., & Kepp, K. P. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13535 · Cited by 48 · see citing works

Proteolytic processing of Neuregulin-1

Willem, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.07.003 · Cited by 50 · see citing works

Amyloid beta modulators and neuroprotection in Alzheimer's disease: a critical appraisal

Kuruva, C. S., & Reddy, P. H. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.10.010 · Cited by 49 · see citing works

Inactivation of γ‐secretases leads to accumulation of substrates and non‐Alzheimer neurodegeneration

Acx, H., Serneels, L., Radaelli, E., Muyldermans, S., Vincke, C., Pepermans, E., Müller, U., Chávez‐Gutiérrez, L., & Strooper, B. D. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201707561 · Cited by 48 · see citing works

Membrane Dynamics of γ-Secretase Provides a Molecular Basis for β-Amyloid Binding and Processing

Somavarapu, A. K., & Kepp, K. P. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00208 · Cited by 49 · see citing works

Dendrimeric Poly(Epsilon-Lysine) Delivery Systems for the Enhanced Permeability of Flurbiprofen across the Blood-Brain Barrier in Alzheimer’s Disease

Al-azzawi, S., Masheta, D., Guildford, A. L., Phillips, G., & Santin, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103224 · Cited by 49 · see citing works

The Alzheimer’s disease-linked protease BACE1 modulates neuronal IL-6 signaling through shedding of the receptor gp130

Müller, S. A., Shmueli, M. D., Feng, X. M., Tüshaus, J., Schumacher, N., Clark, R., Smith, B. E., Chi, A., Rose‐John, S., Kennedy, M. E., et al. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00596-6 · Cited by 49 · see citing works

What lessons can be learned from failed Alzheimer’s disease trials?

Toyn, J. H. (2015) · Expert Review of Clinical Pharmacology · doi:10.1586/17512433.2015.1034690 · Cited by 47 · see citing works

Alzheimer’s Disease Model System Using Drosophila

Tsuda, L., & Lim, Y. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-0529-0_3 · Cited by 46 · see citing works

Gene Therapy Strategies for Alzheimer's Disease: An Overview

Alves, S., Fol, R., & Cartier, N. (2016) · Human Gene Therapy · doi:10.1089/hum.2016.017 · Cited by 45 · see citing works

Tailored emulsion-templated porous polymer scaffolds for iPSC-derived human neural precursor cell culture

Murphy, A. R., Ghobrial, I. M., Jamshidi, P., Laslett, A. L., O’Brien, C., & Cameron, N. R. (2017) · Polymer Chemistry · doi:10.1039/c7py01375b · Cited by 45 · see citing works

Physiological functions of SPP/SPPL intramembrane proteases

Mentrup, T., Cabrera-Cabrera, F., Fluhrer, R., & Schröder, B. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03470-6 · Cited by 41 · see citing works

Accumulation of APP C-terminal fragments causes endolysosomal dysfunction through the dysregulation of late endosome to lysosome-ER contact sites

Bretou, M., Sannerud, R., Escamilla‐Ayala, A., Leroy, T., Vrancx, C., Acker, Z. P. V., Perdok, A., Vermeire, W., Vorsters, I., Keymolen, S. V., et al. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.03.030 · Cited by 43 · see citing works

Misframed ubiquitin and impaired protein quality control: an early event in Alzheimer’s disease

Gentier, R. J. G., & van Leeuwen, F. W. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00047 · Cited by 43 · see citing works

Structure-Based Design of an Iminoheterocyclic β-Site Amyloid Precursor Protein Cleaving Enzyme (BACE) Inhibitor that Lowers Central Aβ in Nonhuman Primates.

Mandal, M., Wu, Y.-S., Misiaszek, J., Li, G.-Q., Buevich, A., Caldwell, J., Liu, X.-X., Mazzola, R., Orth, P., Strickland, C., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01995 · Cited by 37 · see citing works

Aβ 42 /Aβ 40 Ratios of Presenilin 1 Mutations Correlate with Clinical Onset of Alzheimer’s Disease

Tang, N., & Kepp, K. P. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180829 · Cited by 43 · see citing works

A Curcumin Analog Exhibits Multiple Biologic Effects on the Pathogenesis of Alzheimer’s Disease and Improves Behavior, Inflammation, and β-Amyloid Accumulation in a Mouse Model

Su, I., Chang, H., Wang, H.-C., & Tsai, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155459 · Cited by 43 · see citing works

Discovery of an Orally Bioavailable Benzofuran Analogue That Serves as a β-Amyloid Aggregation Inhibitor for the Potential Treatment of Alzheimer’s Disease

Ha, H.-J., Kang, D. W., Kim, H.-M., Kang, J.-M., Ann, J., Hyun, H. J., Lee, J. H., Kim, S. H., Kim, H., Choi, K., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00844 · Cited by 42 · see citing works

Alzheimer’s disease: amyloid-based pathogenesis and potential therapies

Zhou, Y., Sun, Y., Ma, Q., & Liu, Y. (2018) · Cell Stress · doi:10.15698/cst2018.07.143 · Cited by 43 · see citing works

Aberrant Neuronal Cell Cycle Re-Entry: The Pathological Confluence of Alzheimer’s Disease and Brain Insulin Resistance, and Its Relation to Cancer

Köseoğlu, M. M., Norambuena, A., Sharlow, E. R., Lazo, J. S., & Bloom, G. S. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180874 · Cited by 41 · see citing works

Reactions at Biomembrane Interfaces

Bondar, A., & Lemieux, M. J. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00596 · Cited by 41 · see citing works

Materials for Neural Differentiation, Trans‐Differentiation, and Modeling of Neurological Disease

Gong, L., Cao, L., Shen, Z., Shao, L., Gao, S., Zhang, C., Lü, J., & Li, W. (2018) · Advanced Materials · doi:10.1002/adma.201705684 · Cited by 40 · see citing works

Illumination with 630 nm Red Light Reduces Oxidative Stress and Restores Memory by Photo-Activating Catalase and Formaldehyde Dehydrogenase in SAMP8 Mice

Zhang, J., Yue, X., Luo, H., Jiang, W., Mei, Y., Ai, L., Gao, G., Wu, Y., Yang, H. M., An, J., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7520 · Cited by 40 · 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

Proteases: Pivot Points in Functional Proteomics

Verhamme, I. M., Leonard, S. E., & Perkins, R. C. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8814-3_20 · Cited by 39 · see citing works

The Maze of APP Processing in Alzheimer’s Disease: Where Did We Go Wrong in Reasoning?

Chen, M. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00186 · Cited by 41 · see citing works

Can insulin signaling pathways be targeted to transport Aβ out of the brain?

Vandal, M., Bourassa, P., & Calon, F. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00114 · Cited by 37 · see citing works

Restoring Calcium Homeostasis to Treat Alzheimer’s Disease: A Future Perspective

Александровна, П. Е., Власова, О. Л., & Борисович, Б. И. (2015) · Neurodegenerative Disease Management · doi:10.2217/nmt.15.36 · Cited by 36 · see citing works

Transgenerational inheritance of chronic adolescent stress: Effects of stress response and the amygdala transcriptome

Manners, M., Yohn, N. L., Lahens, N., Grant, G. R., Bartolomei, M., & Blendy, J. (2018) · Genes, Brain and Behavior · doi:10.1111/gbb.12493 · Cited by 31 · see citing works

Learning by Failing: Ideas and Concepts to Tackle γ-Secretases in Alzheimer's Disease and Beyond

Strooper, B. D., & Gutiérrez, L. C. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124309 · Cited by 122 · see citing works

Unlocking Truths of γ-Secretase In Alzheimer'S Disease: What Is the Translational Potential?

Wolfe, M. S. (2014) · Future Neurology · doi:10.2217/fnl.14.35 · Cited by 16 · see citing works

Are γ-secretase inhibitors detrimental for Alzheimer's disease patients?

Ross, J., & Imbimbo, B. P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101548 · Cited by 8 · see citing works

Therapeutic intervention for Alzheimer's disease with γ-secretase inhibitors: still a viable option?

Imbimbo, B. P., Panza, F., Frisardi, V., Solfrizzi, V., D’Onofrio, G., Logroscino, G., Seripa, D., & Pilotto, A. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2011.550572 · Cited by 96 · see citing works

γ-Secretase Inhibitors and Modulators for the Treatment of Alzheimer's Disease: Disappointments and Hopes

Imbimbo, B. P., & Giardina, G. A. M. (2011) · Current Topics in Medicinal Chemistry · doi:10.2174/156802611795860942 · Cited by 195 · see citing works