BACE1 is the major β-secretase for generation of Aβ peptides by neurons

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

Expression Analysis of BACE2 in Brain and Peripheral Tissues

Bennett, B. D., Babu-Khan, S., Loeloff, R., Louis, J.-C., Curran, E., Citron, M., & Vassar, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002688200 · Cited by 317

Sialylation enhances the secretion of neurotoxic amyloid‐β peptides

Nakagawa, K., Kitazume, S., Oka, R., Maruyama, K., Saido, T. C., Sato, Y., Endo, T., & Hashimoto, Y. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03595.x · Cited by 83

Risk factor SORL1: from genetic association to functional validation in Alzheimer’s disease

Andersen, O. M., Rudolph, I.-M., & Willnow, T. E. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1615-4 · Cited by 83

BACE1 Regulates Hippocampal Astrogenesis via the Jagged1-Notch Pathway

Hu, X., He, W., Luo, X., Tsubota, K. E., & Yan, R. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.005 · Cited by 81

In Vivo Cleavage of α2,6-Sialyltransferase by Alzheimer β-Secretase

Kitazume, S., Nakagawa, K., Oka, R., Tachida, Y., Ogawa, K., Luo, Y., Citron, M., Shitara, H., Taya, C., Yonekawa, H., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409417200 · Cited by 79

Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site

Schönherr, C., Bien, J., Isbert, S., Wichert, R., Prox, J., Altmeppen, H., Kumar, S., Walter, J., Lichtenthaler, S. F., Weggen, S., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0084-5 · Cited by 76

Behavioral and neural network abnormalities in human APP transgenic mice resemble those of App knock-in mice and are modulated by familial Alzheimer's disease mutations but not by inhibition of BACE1

Johnson, E. C. B., Ho, K., Yu, G.-Q., Das, M., Sanchez, P. E., Djukic, B., Lopez, I., Yu, X., Gill, M., Zhang, W., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00393-5 · Cited by 73

β-Secretase Cleavage at Amino Acid Residue 34 in the Amyloid β Peptide Is Dependent upon γ-Secretase Activity

Shi, X.-P., Tugusheva, K., Bruce, J. E., Lucka, A., Wu, G.-X., Chen-Dodson, E., Price, E., Li, Y., Xu, M., Huang, Q., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209859200 · Cited by 70

Autophagy-mediated Regulation of BACE1 Protein Trafficking and Degradation

Feng, T., Tammineni, P., Agrawal, C., Jeong, Y. Y., & Cai, Q. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.766584 · Cited by 69

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

Toll-like receptor 4 and CD11b expressed on microglia coordinate eradication of Candida albicans cerebral mycosis

Wu, Y., Du, S., Bimler, L. H., Mauk, K. E., Lortal, L., Kichik, N., Griffiths, J. S., Osicka, R., Song, L., Polsky, K., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113240 · Cited by 67

Murine Aβ over-production produces diffuse and compact Alzheimer-type amyloid deposits

Xu, G., Ran, Y., Fromholt, S. E., Fu, C., Yachnis, A. T., Golde, T. E., & Borchelt, D. R. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0252-9 · Cited by 65

Identification of a β-Secretase Activity, Which Truncates Amyloid β-Peptide after Its Presenilin-dependent Generation

Fluhrer, R., Multhaup, G., Schlicksupp, A., Okochi, M., Takeda, M., Lammich, S., Willem, M., Westmeyer, G., Bode, W., Walter, J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211485200 · Cited by 64

Snapin-Mediated BACE1 Retrograde Transport Is Essential for Its Degradation in Lysosomes and Regulation of APP Processing in Neurons

Ye, X., & Cai, Q. (2014) · Cell Reports · doi:10.1016/j.celrep.2013.12.008 · Cited by 63

ER stress is not elevated in the 5XFAD mouse model of Alzheimer's disease

Sadleir, K. R., Popovic, J., & Vassar, R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005769 · Cited by 60

BACE1 Protein Endocytosis and Trafficking Are Differentially Regulated by Ubiquitination at Lysine 501 and the Di-leucine Motif in the Carboxyl Terminus

Kang, E. L., Biscaro, B., Piazza, F., & Tesco, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407072 · Cited by 55

BACE1 inhibitory effects of lavandulyl flavanones from Sophora flavescens

Hwang, E. M., Ryu, Y. B., Kim, H. Y., Kim, D.-G., Hong, S.-G., Lee, J. H., Curtis-Long, M. J., Jeong, S. H., Park, J.-Y., & Park, K. H. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.05.080 · Cited by 53

BACE1 SUMOylation increases its stability and escalates the protease activity in Alzheimer’s disease

Bao, J., Qin, M., Mahaman, Y. A. R., Zhang, B., Huang, F., Zeng, K., Xia, Y., Ke, D., Wang, Q., Liu, R., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800498115 · Cited by 50

Splice variants of the β-site APP-cleaving enzyme BACE1 in human brain and pancreas

Ehehalt, R., Michel, B., De Pietri Tonelli, D., Zacchetti, D., Simons, K., & Keller, P. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00169-9 · Cited by 51

Targeting the Role of the Endosome in the Pathophysiology of Alzheimer's Disease: A Strategy for Treatment

Tate, B. A., & Mathews, P. M. (2006) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2006.10.re2 · Cited by 48

Identification of Phospholipid Scramblase 1 as a Novel Interacting Molecule with β-Secretase (β-Site Amyloid Precursor Protein (APP) Cleaving Enzyme (BACE))

Kametaka, S., Shibata, M., Moroe, K., Kanamori, S., Ohsawa, Y., Waguri, S., Sims, P. J., Emoto, K., Umeda, M., & Uchiyama, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208611200 · Cited by 47

Characterization of the selective in vitro and in vivo binding properties of crenezumab to oligomeric Aβ

Meilandt, W. J., Maloney, J. A., Imperio, J., Lalehzadeh, G., Earr, T., Crowell, S., Bainbridge, T. W., Lu, Y., Ernst, J. A., Fuji, R. N., et al. (2019) · Alzheimer's Research & Therapy · doi:10.1186/s13195-019-0553-5 · Cited by 45

Promotion of BACE1 mRNA Alternative Splicing Reduces Amyloid β-Peptide Production

Mowrer, K. R., & Wolfe, M. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801322200 · Cited by 45

Development of inhibitors targeting glycogen synthase kinase-3β for human diseases: Strategies to improve selectivity

Wei, J., Wang, J., Zhang, J., Yang, J., Wang, G., & Wang, Y. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114301 · Cited by 42

β-Site Amyloid Precursor Protein Cleaving Enzyme 1(BACE1) Regulates Notch Signaling by Controlling the Cleavage of Jagged 1 (Jag1) and Jagged 2 (Jag2) Proteins

He, W., Hu, J., Xia, Y., & Yan, R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.579862 · Cited by 41

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

Mutant ubiquitin decreases amyloid β plaque formation in a transgenic mouse model of Alzheimer’s disease

van Tijn, P., Dennissen, F. J. A., Gentier, R. J. G., Hobo, B., Hermes, D., Steinbusch, H. W. M., Van Leeuwen, F. W., & Fischer, D. F. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.07.007 · Cited by 39

Inhibition of amyloid precursor protein secretases reduces recovery after spinal cord injury

Pajoohesh-Ganji, A., Burns, M. P., Pal-Ghosh, S., Tadvalkar, G., Hokenbury, N. G., Stepp, M. A., & Faden, A. I. (2014) · Brain Research · doi:10.1016/j.brainres.2014.02.049 · Cited by 29

Regulation of the alternative β-secretase meprin β by ADAM-mediated shedding

Scharfenberg, F., Armbrust, F., Marengo, L., Pietrzik, C., & Becker-Pauly, C. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03179-1 · Cited by 29

Mouse brain proteomics establishes MDGA1 and CACHD1 as in vivo substrates of the Alzheimer protease BACE1

Rudan Njavro, J., Klotz, J., Dislich, B., Wanngren, J., Shmueli, M. D., Herber, J., Kuhn, P., Kumar, R., Koeglsperger, T., Conrad, M., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201902347r · Cited by 28

BACE1 regulates the proliferation and cellular functions of Schwann cells

Hu, X., Hou, H., Bastian, C., He, W., Qiu, S., Ge, Y., Yin, X., Kidd, G. J., Brunet, S., Trapp, B. D., et al. (2017) · Glia · doi:10.1002/glia.23122 · Cited by 27

Post-translational regulation of the β-secretase BACE1

Araki, W. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.04.009 · Cited by 26

Genetic and pharmacological evidence of intraneuronal Aβ accumulation in APP transgenic mice

Philipson, O., Lannfelt, L., & Nilsson, L. N. G. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.08.009 · Cited by 21

Spatiotemporal processing of neural cell adhesion molecules 1 and 2 by BACE1 in vivo

Kim, W., Watanabe, H., Lomoio, S., & Tesco, G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100372 · Cited by 21

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

The Alzheimer’s Disease–Associated Protein BACE1 Modulates T Cell Activation and Th17 Function

Hernandez-Mir, G., Raphael, I., Revu, S., Poholek, C. H., Avery, L., Hawse, W. F., Kane, L. P., & McGeachy, M. J. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1800363 · Cited by 14

Reduced Aβ secretion by human neurons under conditions of strongly increased BACE activity

Scholz, D., Chernyshova, Y., Ückert, A., & Leist, M. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14467 · Cited by 11