Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity

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

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

Peptidomimetic Probes and Molecular Modeling Suggest That Alzheimer's γ-Secretase Is an Intramembrane-Cleaving Aspartyl Protease

Wolfe, M. S., Xia, W., Moore, C. L., Leatherwood, D. D., Ostaszewski, B., Rahmati, T., Donkor, I. O., & Selkoe, D. J. (1999) · Biochemistry · doi:10.1021/bi982562p · Cited by 289

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864

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

Alzheimer's Disease: Genes, Proteins, and Therapy

Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063

Current concepts in mild cognitive impairment

Petersen, R. C., Doody, R., Kurz, A., Mohs, R. C., Morris, J. C., Rabins, P. V., Ritchie, K., Rossor, M., Thal, L., & Winblad, B. (2001) · Archives of Neurology · doi:10.1001/archneur.58.12.1985 · Cited by 4,781

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744

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

The molecular pathology of Alzheimer's disease

Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708

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

Amyloid Precursor Protein Processing and Alzheimer's Disease

O'Brien, R. J., & Wong, P. C. (2011) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-061010-113613 · Cited by 2,061

Intracellular amyloid-β in Alzheimer's disease

LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942

Aβ Oligomers – a decade of discovery

Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938

Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective

Tanzi, R. E., & Bertram, L. (2005) · Cell · doi:10.1016/j.cell.2005.02.008 · Cited by 1,849

Alzheimer's Disease and the Amyloid-β Peptide

Murphy, M. P., & LeVine, H. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-1221 · Cited by 1,750

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

Alzheimer’s Disease: The Challenge of the Second Century

Holtzman, D. M., Morris, J. C., & Goate, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002369 · Cited by 1,424

Alzheimer's Disease and Parkinson's Disease

Nussbaum, R. L., & Ellis, C. E. (2003) · New England Journal of Medicine · doi:10.1056/nejm2003ra020003 · Cited by 1,351

Regulated Intramembrane Proteolysis

Brown, M. S., Ye, J., Rawson, R. B., & Goldstein, J. L. (2000) · Cell · doi:10.1016/s0092-8674(00)80675-3 · Cited by 1,329

Toxic Proteins in Neurodegenerative Disease

Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251

Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease

Walsh, D. M., & Selkoe, D. J. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.010 · Cited by 1,207

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

Cao, X., & Südhof, T. C. (2001) · Science · doi:10.1126/science.1058783 · Cited by 1,202

Translating cell biology into therapeutic advances in Alzheimer's disease

Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,166

Trafficking and Proteolytic Processing of APP

Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075

Identification of a Novel Aspartic Protease (Asp 2) as β-Secretase

Hussain, I., Powell, D., Howlett, D. R., Tew, D. G., Meek, T. D., Chapman, C., Gloger, I. S., Murphy, K. E., Southan, C. D., Ryan, D. M., et al. (1999) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0811 · Cited by 1,080

Review Article: Genetics of Alzheimer Disease

Bekris, L. M., Yu, C.-E., Bird, T. D., & Tsuang, D. W. (2010) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988710383571 · Cited by 1,029

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

Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1

Li, Y.-M., Xu, M., Lai, M.-T., Huang, Q., Castro, J. L., DiMuzio-Mower, J., Harrison, T., Lellis, C., Nadin, A., Neduvelil, J. G., et al. (2000) · Nature · doi:10.1038/35015085 · Cited by 866

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

Selkoe, D. J. (2004) · Nature Cell Biology · doi:10.1038/ncb1104-1054 · Cited by 863

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

Hardy, J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06181.x · Cited by 814

The secretases: enzymes with therapeutic potential in Alzheimer disease

De Strooper, B., Vassar, R., & Golde, T. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2009.218 · Cited by 799

The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives

Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.010 · Cited by 786

The genetics of Alzheimer disease

Tanzi, R. E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006296 · Cited by 727

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

Alzheimer's Disease: From Pathology to Therapeutic Approaches

Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802808 · Cited by 626

NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ42 in vivo

Eriksen, J. L., Sagi, S. A., Smith, T. E., Weggen, S., Das, P., McLendon, D. C., Ozols, V. V., Jessing, K. W., Zavitz, K. H., Koo, E. H., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18162 · Cited by 634

Effects of secreted oligomers of amyloid β‐protein on hippocampal synaptic plasticity: a potent role for trimers

Townsend, M., Shankar, G. M., Mehta, T., Walsh, D. M., & Selkoe, D. J. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2005.103754 · Cited by 619

Presenilins Form ER Ca2+ Leak Channels, a Function Disrupted by Familial Alzheimer's Disease-Linked Mutations

Tu, H., Nelson, O., Bezprozvanny, A., Wang, Z., Lee, S.-F., Hao, Y.-H., Serneels, L., De Strooper, B., Yu, G., & Bezprozvanny, I. (2006) · Cell · doi:10.1016/j.cell.2006.06.059 · Cited by 616

Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease

Barage, S. H., & Sonawane, K. D. (2015) · Neuropeptides · doi:10.1016/j.npep.2015.06.008 · Cited by 579

β-Secretase Protein and Activity Are Increased in the Neocortex in Alzheimer Disease

Fukumoto, H. (2002) · Archives of Neurology · doi:10.1001/archneur.59.9.1381 · Cited by 575

The Alzheimer’s Disease Mitochondrial Cascade Hypothesis

Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100339 · Cited by 562

The Alzheimer's disease Beta-secretase enzyme, BACE1

Cole, S. L., & Vassar, R. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-22 · Cited by 550

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

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

Geling, A., Steiner, H., Willem, M., Bally‐Cuif, L., & Haass, C. (2002) · The EMBO Reports · doi:10.1093/embo-reports/kvf124 · Cited by 497

Reduced IGF-1 signaling delays age-associated proteotoxicity in mice

Cohen, E., Paulsson, J. F., Blinder, P., Burstyn-Cohen, T., Du, D., Estepa, G., Adame, A., Pham, H. M., Holzenberger, M., Kelly, J. W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.11.014 · Cited by 488

A Portrait of Alzheimer Secretases--New Features and Familiar Faces

Esler, W. P., & Wolfe, M. S. (2001) · Science · doi:10.1126/science.1064638 · Cited by 493

A Hundred Years of Alzheimer's Disease Research

Hardy, J. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.016 · Cited by 467

The Many Substrates of Presenilin/γ-Secretase

Haapasalo, A., & Kovacs, D. M. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-101065 · Cited by 458

Proteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process

De Strooper, B. (2010) · Physiological Reviews · doi:10.1152/physrev.00023.2009 · Cited by 455

REVIEW: Curcumin and Alzheimer’s disease

Hamaguchi, T., Ono, K., & Yamada, M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00147.x · Cited by 450

Maturation and Endosomal Targeting of β-Site Amyloid Precursor Protein-cleaving Enzyme

Huse, J. T., Pijak, D. S., Leslie, G. J., Lee, V. M.-Y., & Doms, R. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004175200 · Cited by 402

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

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

Haass, C., & Strooper, B. D. (1999) · Science · doi:10.1126/science.286.5441.916 · Cited by 388

Longer Forms of Amyloid β Protein: Implications for the Mechanism of Intramembrane Cleavage by γ-Secretase

Qi-Takahara, Y., Morishima-Kawashima, M., Tanimura, Y., Dolios, G., Hirotani, N., Horikoshi, Y., Kametani, F., Maeda, M., Saido, T. C., Wang, R., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1575-04.2005 · Cited by 391

Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer’s disease

D'Andrea, M. R., Nagele, R. G., Wang, H., Peterson, P. A., & Lee, D. H. S. (2001) · Histopathology · doi:10.1046/j.1365-2559.2001.01082.x · Cited by 390

Analysis of 138 pathogenic mutations in presenilin-1 on the in vitro production of Aβ42 and Aβ40 peptides by γ-secretase

Sun, L., Zhou, R., Yang, G., & Shi, Y. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1618657114 · Cited by 382

The familial Alzheimer's disease APPV717I mutation alters APP processing and Tau expression in iPSC-derived neurons

Muratore, C. R., Rice, H. C., Srikanth, P., Callahan, D. G., Shin, T., Benjamin, L. N. P., Walsh, D. M., Selkoe, D. J., & Young-Pearse, T. L. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu064 · Cited by 379

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

Song, W., Nadeau, P., Yuan, M., Yang, X., Shen, J., & Yankner, B. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6959 · Cited by 362

Soluble protein oligomers as emerging toxins in Alzheimer’s and other amyloid diseases

Ferreira, S. T., Vieira, M. N. N., & De Felice, F. G. (2007) · IUBMB Life · doi:10.1080/15216540701283882 · Cited by 335

Proteolytic ectodomain shedding of membrane proteins in mammals-hardware, concepts, and recent developments

Lichtenthaler, S. F., Lemberg, M. K., & Fluhrer, R. (2018) · The EMBO Journal · doi:10.15252/embj.201899456 · Cited by 323

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

Recognition of the amyloid precursor protein by human γ-secretase

Zhou, R., Yang, G., Guo, X., Zhou, Q., Lei, J., & Shi, Y. (2019) · Science · doi:10.1126/science.aaw0930 · Cited by 304

Sequential Proteolytic Processing of the Triggering Receptor Expressed on Myeloid Cells-2 (TREM2) Protein by Ectodomain Shedding and γ-Secretase-dependent Intramembranous Cleavage

Wunderlich, P., Glebov, K., Kemmerling, N., Tien, N. T., Neumann, H., & Walter, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.517540 · Cited by 296

Transport-Dependent Proteolysis of SREBP

DeBose-Boyd, R. A., Brown, M. S., Li, W.-P., Nohturfft, A., Goldstein, J. L., & Espenshade, P. J. (1999) · Cell · doi:10.1016/s0092-8674(00)81668-2 · Cited by 288

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

Szaruga, M., Munteanu, B., Lismont, S., Veugelen, S., Horré, K., Mercken, M., Saido, T. C., Ryan, N. S., De Vos, T., Savvides, S. N., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.004 · Cited by 248

Membrane rafts in Alzheimer's disease beta-amyloid production

Vetrivel, K. S., & Thinakaran, G. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.03.007 · Cited by 247

The Lipoprotein Receptor LR11 Regulates Amyloid β Production and Amyloid Precursor Protein Traffic in Endosomal Compartments

Offe, K., Dodson, S. E., Shoemaker, J. T., Fritz, J. J., Gearing, M., Levey, A. I., & Lah, J. J. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4946-05.2006 · Cited by 245

Genetically engineered pigs as models for human disease

Perleberg, C., Kind, A., & Schnieke, A. (2018) · Disease Models & Mechanisms · doi:10.1242/dmm.030783 · Cited by 222

Alzheimer's β-secretase, β-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase

Kitazume, S., Tachida, Y., Oka, R., Shirotani, K., Saido, T. C., & Hashimoto, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241509198 · Cited by 232

Reversal of long-term dendritic spine alterations in Alzheimer disease models

Smith, D. L., Pozueta, J., Gong, B., Arancio, O., & Shelanski, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908706106 · Cited by 229

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

Pathogenic APP mutations near the gamma-secretase cleavage site differentially affect Abeta secretion and APP C-terminal fragment stability

De Jonghe, C. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.16.1665 · Cited by 223

Alzheimer Disease: Mechanistic Understanding Predicts Novel Therapies

Selkoe, D. J. (2004) · Annals of Internal Medicine · doi:10.7326/0003-4819-140-8-200404200-00047 · Cited by 208

Regulated intramembrane proteolysis - lessons from amyloid precursor protein processing: Regulated intramembrane proteolysis and APP processing

Lichtenthaler, S. F., Haass, C., & Steiner, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07248.x · Cited by 205

Maturation and Pro-peptide Cleavage of β-Secretase

Capell, A., Steiner, H., Willem, M., Kaiser, H., Meyer, C., Walter, J., Lammich, S., Multhaup, G., & Haass, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003202200 · Cited by 205

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

Amyloid Angiopathy and Variability in Amyloid β Deposition Is Determined by Mutation Position in Presenilin-1-Linked Alzheimer’s Disease

Mann, D. M. A., Pickering-Brown, S. M., Takeuchi, A., & Iwatsubo, T. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64688-3 · Cited by 182

A Cell Biological Perspective on Alzheimer's Disease

Annaert, W., & De Strooper, B. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.020402.142302 · Cited by 182

GSK‐3 in Neurodegenerative Diseases

Lei, P., Ayton, S., Bush, A. I., & Adlard, P. A. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/189246 · Cited by 177

Role of mitochondrial homeostasis and dynamics in Alzheimer's disease

Selfridge, J. E., E, L., Lu, J., & Swerdlow, R. H. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.057 · Cited by 175

Insights on the pathophysiology of Alzheimer's disease: The crosstalk between amyloid pathology, neuroinflammation and the peripheral immune system

Dá Mesquita, S., Ferreira, A. C., Sousa, J. C., Correia-Neves, M., Sousa, N., & Marques, F. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.06.014 · Cited by 166

Intramembrane proteolysis by presenilins

Steiner, H., & Haass, C. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043065 · Cited by 161

The physiology of the β‐amyloid precursor protein intracellular domain AICD

Pardossi‐Piquard, R., & Checler, F. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07475.x · Cited by 159

Lysosome biogenesis in health and disease

Bajaj, L., Lotfi, P., Pal, R., Ronza, A. D., Sharma, J., & Sardiello, M. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14564 · Cited by 153

Nonfibrillar diffuse amyloid deposition due to a gamma42-secretase site mutation points to an essential role for N-truncated Abeta42 in Alzheimer's disease

Kumar-Singh, S. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.18.2589 · Cited by 158

The involvement of lipid rafts in Alzheimer's disease (Review)

Cordy, J. M., Cordy, J. M., Hooper, N. M., & Turner, A. J. (2006) · Molecular Membrane Biology · doi:10.1080/09687860500496417 · Cited by 157

Qualitative changes in human γ-secretase underlie familial Alzheimer’s disease

Szaruga, M., Veugelen, S., Benurwar, M., Lismont, S., Sepulveda-Falla, D., Lleo, A., Ryan, N. S., Lashley, T., Fox, N. C., Murayama, S., et al. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20150892 · Cited by 155

Epigenetics in Alzheimer’s Disease: Perspective of DNA Methylation

Qazi, T. J., Quan, Z., Mir, A., & Qing, H. (2018) · Molecular Neurobiology · doi:10.1007/s12035-016-0357-6 · Cited by 153

CSF biomarkers for mild cognitive impairment

Blennow, K. (2004) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2004.01368.x · Cited by 151

Neurodegeneration in Normal Brain Aging and Disease

Thal, D. R., Del Tredici, K., & Braak, H. (2004) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2004.23.pe26 · Cited by 149

Interaction of the Cytosolic Domains of sorLA/LR11 with the Amyloid Precursor Protein (APP) and β-Secretase β-Site APP-Cleaving Enzyme

Spoelgen, R., von Arnim, C. A. F., Thomas, A. V., Peltan, I. D., Koker, M., Deng, A., Irizarry, M. C., Andersen, O. M., Willnow, T. E., & Hyman, B. T. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.3882-05.2006 · Cited by 148

Processing of β-Secretase by Furin and Other Members of the Proprotein Convertase Family

Creemers, J. W. M., Ines Dominguez, D., Plets, E., Serneels, L., Taylor, N. A., Multhaup, G., Craessaerts, K., Annaert, W., & De Strooper, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006947200 · Cited by 147

If amyloid drives Alzheimer disease, why have anti-amyloid therapies not yet slowed cognitive decline?

Haass, C., & Selkoe, D. (2022) · PLOS Biology · doi:10.1371/journal.pbio.3001694 · Cited by 145

Nicastrin functions to sterically hinder γ-secretase–substrate interactions driven by substrate transmembrane domain

Bolduc, D. M., Montagna, D. R., Gu, Y., Selkoe, D. J., & Wolfe, M. S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512952113 · Cited by 144

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

(2008) · Handbook of Clinical Neurology · doi:10.1016/s0072-9752(07)01223-7 · Cited by 137

Alzheimer Presenilin-1 Mutations Dramatically Reduce Trimming of Long Amyloid β-Peptides (Aβ) by γ-Secretase to Increase 42-to-40-Residue Aβ

Fernandez, M. A., Klutkowski, J. A., Freret, T., & Wolfe, M. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.581165 · Cited by 136

Analysis of the γ-secretase interactome and validation of its association with tetraspanin-enriched microdomains

Wakabayashi, T., Craessaerts, K., Bammens, L., Bentahir, M., Borgions, F., Herdewijn, P., Staes, A., Timmerman, E., Vandekerckhove, J., Rubinstein, E., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1978 · Cited by 135

Familial Alzheimer’s disease–associated presenilin-1 alters cerebellar activity and calcium homeostasis

Sepulveda-Falla, D., Barrera-Ocampo, A., Hagel, C., Korwitz, A., Vinueza-Veloz, M. F., Zhou, K., Schonewille, M., Zhou, H., Velazquez-Perez, L., Rodriguez-Labrada, R., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci66407 · Cited by 135

Acidic pH promotes the formation of toxic fibrils from β-amyloid peptide

Su, Y., & Chang, P.-T. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03322-9 · Cited by 135

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

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

Microglial PD-1 stimulation by astrocytic PD-L1 suppresses neuroinflammation and Alzheimer’s disease pathology

Kummer, M. P., Ising, C., Kummer, C., Sarlus, H., Griep, A., Vieira‐Saecker, A., Schwartz, S., Halle, A., Brückner, M., Händler, K., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108662 · Cited by 127