Function and Dysfunction of the Presenilins

Sisodia, Sangram S.; Kim, Seong H.; Thinakaran, Gopal

doi:10.1086/302475

Cited by 76Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Function and Dysfunction of the Presenilins

Open access

Sisodia, Sangram S., Kim, Seong H., Thinakaran, Gopal·1999·The American Journal of Human Genetics

DOI 10.1086/302475PMC PMC1378068

Open this paper in CoChat — free account

Integrity signals

Registry

Crossref · 10.1086/302475

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Mutations in APP and presenilins PS1 and PS2 increase production of Aβ42 and cause familial Alzheimer's disease.
“Mutations in the genes for amyloid precursor protein (APP) and presenilins (PS1, PS2) increase production of 𝛃 -amyloid 42 (A 𝛃 42 ) and cause familial Alzheimer's disease (FAD).”
From Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation (2006) · cites this paper as Sisodia et al., 1999
A strong genetic association exists between early-onset familial Alzheimer's disease and the 42 amino acid species of Aβ peptide (Aβ42).
“A strong genetic association exists between earlyonset familial forms of AD (FAD) and the 42 amino acid species of the A 𝛃 peptide (A 𝛃 42 ) (for review, see Hutton et al., 1998; Younkin, 1998; Sisodia et al., 1999).”
From Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation (2006) · cites this paper as Sisodia et al., 1999
Aβ is cleaved from APP by the sequential action of β- and γ-secretases.
“A 𝛃 is cleaved from APP by the sequential action of two proteases, the 𝛃 - and 𝛄 -secretases (for review, see Sisodia et al., 1999; Selkoe, 2001).”
From Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation (2006) · cites this paper as Sisodia et al., 1999

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051 · see citing works
Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599 · see citing works
Candidate gene for the chromosome 1 familial Alzheimer’s disease locus
Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577 · see citing works
A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
De Strooper, B., Annaert, W., Cupers, P., Saftig, P., Craessaerts, K., Mumm, J. S., Schroeter, E. H., Schrijvers, V., Wolfe, M. S., Ray, W. J., et al. (1999) · Nature · doi:10.1038/19083 · Cited by 2,100 · see citing works
Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
Rogaev, E. I., Sherrington, R., Rogaeva, E. A., Levesque, G., Ikeda, M., Liang, Y., Chi, H., Lin, C., Holman, K., Tsuda, T., et al. (1995) · Nature · doi:10.1038/376775a0 · Cited by 2,052 · see citing works
Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
Wolfe, M. S., Xia, W., Ostaszewski, B. L., Diehl, T. S., Kimberly, W. T., & Selkoe, D. J. (1999) · Nature · doi:10.1038/19077 · Cited by 1,913 · 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
Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
Holcomb, L., Gordon, M. N., McGowan, E., Yu, X., Benkovic, S., Jantzen, P., Wright, K., Saad, I., Mueller, R., Morgan, D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-097 · Cited by 1,386 · see citing works
Accelerated Amyloid Deposition in the Brains of Transgenic Mice Coexpressing Mutant Presenilin 1 and Amyloid Precursor Proteins
Borchelt, D. R., Ratovitski, T., van Lare, J., Lee, M. K., Gonzales, V., Jenkins, N. A., Copeland, N. G., Price, D. L., & Sisodia, S. S. (1997) · Neuron · doi:10.1016/s0896-6273(00)80974-5 · Cited by 1,023 · see citing works
Self-citation
Endoproteolysis of Presenilin 1 and Accumulation of Processed Derivatives In Vivo
Thinakaran, G., Borchelt, D., Lee, M. K., Slunt, H. H., Spitzer, L., Kim, G. J., Ratovitski, T., Davenport, F., Nordstedt, C., Seeger, M., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80291-3 · Cited by 1,009 · see citing works
Self-citation
Genetic Linkage Evidence for a Familial Alzheimer's Disease Locus on Chromosome 14
Schellenberg, G. D., Bird, T. D., Wijsman, E. M., Orr, H. T., Anderson, L., Nemens, E. J., White, J. A., Bonnycastle, L. L., Weber, J. L., Alonso, M. E., et al. (1992) · Science · doi:10.1126/science.1411576 · Cited by 945 · see citing works
The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
Selkoe, D. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01363-4 · Cited by 862 · see citing works
A Familial Alzheimer's Disease Locus on Chromosome 1
Levy‐Lahad, E., Wijsman, E. M., Nemens, E. J., Anderson, L., Goddard, K. A. B., Weber, J. L., Bird, T. D., & Schellenberg, G. D. (1995) · Science · doi:10.1126/science.7638621 · Cited by 811 · 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
Presenilin is required for activity and nuclear access of Notch in Drosophila
Struhl, G., & Greenwald, I. (1999) · Nature · doi:10.1038/19091 · Cited by 804 · see citing works
Presenilin 1 is required for Notch 1 and Dll1 expression in the paraxial mesoderm
Wong, P. C., Zheng, H., Chen, H., Bêcher, M. W., SIRINATHSINGHJI, D. J. S., Trumbauer, M. E., Chen, H. Y., Price, D. L., der Ploeg, L. H. T. V., & Sisodia, S. S. (1997) · Nature · doi:10.1038/387288a0 · Cited by 712 · see citing works
Self-citation
Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
Levitan, D. J., & Greenwald, I. (1995) · Nature · doi:10.1038/377351a0 · Cited by 709 · see citing works
MUTANT GENES IN FAMILIAL ALZHEIMER'S DISEASE AND TRANSGENIC MODELS
Price, D. L., & Sisodia, S. S. (1998) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.21.1.479 · Cited by 568 · see citing works
Self-citation
Destabilization of β-catenin by mutations in presenilin-1 potentiates neuronal apoptosis
Zhang, Z., Hartmann, H., Do, V. M., Abramowski, D., Sturchler, C., Staufenbiel, M., Sommer, B., van de Wetering, M., Clevers, H. C., Säftig, P., et al. (1998) · Nature · doi:10.1038/27208 · Cited by 511 · see citing works
Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants
Ye, Y., Lukinova, N. I., & Fortini, M. (1999) · Nature · doi:10.1038/19096 · Cited by 492 · see citing works
The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology
Lemere, C. A., Lopera, F., Kosik, K. S., Lendon, C. L., Ossa, J., Saido, T. C., Yamaguchi, H., Ruiz, A., Martinez, A., Madrigal, L., et al. (1996) · Nature Medicine · doi:10.1038/nm1096-1146 · Cited by 487 · see citing works
Protein Topology of Presenilin 1
Doan, A., Thinakaran, G., Borchelt, D., Slunt, H. H., Ratovitski, T., Podlisny, M. B., Selkoe, D. J., Seeger, M., Gandy, S., Price, D. L., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80232-9 · Cited by 371 · see citing works
Self-citation
The Presenilin 1 Protein Is a Component of a High Molecular Weight Intracellular Complex That Contains β-Catenin
Yu, G., Chen, F., Lévesque, G., Nishimura, M., Zhang, D., Lévesque, L., Rogaeva, E., Xu, D., Liang, Y., Duthie, M., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16470 · Cited by 367 · see citing works
Effects of PS1 Deficiency on Membrane Protein Trafficking in Neurons
Naruse, S., Thinakaran, G., Luo, J.-J., Kusiak, J. W., Tomita, T., Iwatsubo, T., Qian, X., Ginty, D. D., Price, D. L., Borchelt, D. R., et al. (1998) · Neuron · doi:10.1016/s0896-6273(00)80637-6 · Cited by 355 · see citing works
Self-citation
Assessment of normal and mutant human presenilin function in Caenorhabditis elegans
Levitan, D. J., Doyle, T. G., Brousseau, D., Lee, M. K., Thinakaran, G., Slunt, H. H., Sisodia, S. S., & Greenwald, I. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14940 · Cited by 354 · see citing works
Self-citation
Presenilin 1 interaction in the brain with a novel member of the Armadillo family
Zhou, J., Liyanage, U. K., Medina, M., Ho, C., Simmons, A. D., Lovett, M., & Kosik, K. S. (1997) · Neuroreport · doi:10.1097/00001756-199705260-00054 · Cited by 297 · see citing works
Presenilin Proteins Undergo Heterogeneous Endoproteolysis between Thr291and Ala299and Occur as Stable N- and C-Terminal Fragments in Normal and Alzheimer Brain Tissue
Podlisny, M. B., Citron, M., Amarante, P., Sherrington, R., Xia, W., Zhang, J., Diehl, T. S., Levesque, G., Fraser, P., Haass, C., et al. (1997) · Neurobiology of Disease · doi:10.1006/nbdi.1997.0129 · Cited by 291 · see citing works
Expression of Presenilin 1 and 2 (PS1 and PS2) in Human and Murine Tissues
Lee, M. K., Slunt, H. H., Martin, L. J., Thinakaran, G., Kim, G. J., Gandy, S., Seeger, M., Koo, E. H., Price, D. L., & Sisodia, S. S. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-23-07513.1996 · Cited by 286 · see citing works
Self-citation
REVIEWThe Gene Defects Responsible for Familial Alzheimer's Disease
Tanzi, R. E., Kovacs, D. M., Kim, T.-W., Moir, R. D., Guenette, S. Y., & Wasco, W. (1996) · Neurobiology of Disease · doi:10.1006/nbdi.1996.0016 · Cited by 265 · see citing works
Interaction between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer disease
Xia, W., Zhang, J., Perez, R. G., Koo, E. H., & Selkoe, D. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.15.8208 · Cited by 236 · see citing works
Presenilin mutations associated with Alzheimer disease cause defective intracellular trafficking of β-catenin,a component of the presenilin protein complex
Nishimura, M., Yu, G., Lévesque, G., Zhang, D. M., Ruel, L., Chen, F., Milman, P., Holmes, E., Liang, Y., Kawarai, T., et al. (1999) · Nature Medicine · doi:10.1038/5526 · Cited by 218 · see citing works
Formation of stable complexes between two Alzheimer's disease gene products: Presenilin-2 and β-amyloid precursor protein
Weidemann, A., Paliga, K., Dürrwang, U., Czech, C., Evin, G. M., Masters, C. L., & Beyreuther, K. T. (1997) · Nature Medicine · doi:10.1038/nm0397-328 · Cited by 211 · see citing works
Endoproteolytic Cleavage and Proteasomal Degradation of Presenilin 2 in Transfected Cells
Kim, T., Pettingell, W. H., Hallmark, O. G., Moir, R. D., Wasco, W., & Tanzi, R. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11006 · Cited by 208 · see citing works
Human presenilin‐1, but not familial Alzheimer’s disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing
Baumeister, R., Leimer, U., Zweckbronner, I., Jakubek, C., Grünberg, J., & Haass, C. (1997) · Genes and Function · doi:10.1046/j.1365-4624.1997.00012.x · Cited by 203 · see citing works
Membrane Topology of the C. elegans SEL-12 Presenilin
Li, X., & Greenwald, I. (1996) · Neuron · doi:10.1016/s0896-6273(00)80231-7 · Cited by 199 · see citing works
Stable Association of Presenilin Derivatives and Absence of Presenilin Interactions with APP
Thinakaran, G., Regard, J. B., Bouton, C. M. L. S., Harris, C. L., Price, D. L., Borchelt, D., & Sisodia, S. S. (1998) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0171 · Cited by 173 · see citing works
Self-citation
Light and Electron Microscopic Localization of Presenilin-1 in Primate Brain
Lah, J. J., Heilman, C. J., Nash, N. R., Rees, H. D., Yi, H., Counts, S. E., & Levey, A. I. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-06-01971.1997 · Cited by 168 · see citing works
Evidence for a physical interaction between presenilin and Notch
Ray, W. J., Yao, M., Nowotny, P., Mumm, J. S., Zhang, W., Wu, J. Y., Kopan, R., & Goate, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3263 · Cited by 167 · see citing works
HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signaling
Li, X., & Greenwald, I. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.22.12204 · Cited by 160 · see citing works
Microglia and the Immune Pathology of Alzheimer Disease
Giulian, D. (1999) · The American Journal of Human Genetics · doi:10.1086/302477 · Cited by 141 · see citing works
Effects of SEL-12 presenilin on LIN-12 localization and function in Caenorhabditis elegans
Levitan, D. J., & Greenwald, I. (1998) · Development · doi:10.1242/dev.125.18.3599 · Cited by 92 · see citing works
Reverse genetic analysis of Caenorhabditis elegans presenilins reveals redundant but unequal roles for sel- 12 and hop- 1 in Notch-pathway signaling
Westlund, B., Parry, D., Clover, R., Basson, M., & Johnson, C. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2497 · Cited by 82 · see citing works
Evidence That Intramolecular Associations between Presenilin Domains Are Obligatory for Endoproteolytic Processing
Saura, C. A., Tomita, T., Davenport, F., Harris, C. L., Iwatsubo, T., & Thinakaran, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.13818 · Cited by 74 · see citing works
Self-citation
Direct Interaction of Alzheimer's Disease-related Presenilin 1 with Armadillo Protein p0071
Stahl, B., Diehlmann, A., & Südhof, T. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9141 · Cited by 64 · see citing works

Flagged first, then by citations

Sorted by citations

Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · see citing works
“A strong genetic association exists between earlyonset familial forms of AD (FAD) and the 42 amino acid species of the A peptide (A 42) (for review, see Hutton et al., 1998; Younkin, 1998; Sisodia et al., 1999).”
Background
Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation
Luo, Y., Bolon, B., Kahn, S., Bennett, B. D., Babu-Khan, S., Denis, P., Fan, W., Kha, H., Zhang, J., Gong, Y., et al. (2001) · Nature Neuroscience · doi:10.1038/85059 · Cited by 1,001 · see citing works
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 · see citing works
Inflammatory process in Alzheimer's Disease
Meraz-Ríos, M. A., Toral-Rios, D., Franco-Bocanegra, D., Villeda-Hernández, J., & Campos-Peña, V. (2013) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2013.00059 · Cited by 427 · see citing works
BACE1: The β-Secretase Enzyme in Alzheimer's Disease
Vassar, R. J. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:23:1-2:105 · Cited by 369 · see citing works
Drugs in Clinical Trials for Alzheimer's Disease: The Major Trends
Бачурин, С. О., Bovina, E. V., & Ustyugov, A. A. (2017) · Medicinal Research Reviews · doi:10.1002/med.21434 · Cited by 305 · see citing works
Aβ-Generating Enzymes
Vassar, R. J., & Citron, M. (2000) · Neuron · doi:10.1016/s0896-6273(00)00051-9 · Cited by 299 · see citing works
Energy Inhibition Elevates β-Secretase Levels and Activity and Is Potentially Amyloidogenic in APP Transgenic Mice: Possible Early Events in Alzheimer's Disease Pathogenesis
Velliquette, R. A., O'Connor, T., & Vassar, R. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2350-05.2005 · Cited by 254 · see citing works
Amyloidogenic processing of β-amyloid precursor protein in intracellular compartments
Vetrivel, K. S., & Thinakaran, G. (2006) · Neurology · doi:10.1212/01.wnl.0000192107.17175.39 · Cited by 217 · see citing works
Self-citation
β-Secretase (BACE) as a drug target for alzheimer’s disease
Vassar, R. J. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00157-6 · Cited by 209 · see citing works
The β-Secretase, BACE: A Prime Drug Target for Alzheimer's Disease
Vassar, R. J. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:157 · Cited by 186 · see citing works
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 · see citing works
JNK activation is associated with intracellular β-amyloid accumulation
Shoji, M., Iwakami, N., Takeuchi, S., Waragai, M., Suzuki, M., Kanazawa, I., Lippa, C. F., Ono, S., & Okazawa, H. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00245-x · Cited by 166 · see citing works
The γ-secretase complex: from structure to function
Zhang, X., Li, Y., Xu, H., & Zhang, Y. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00427 · Cited by 164 · see citing works
NDRG2: a novel Alzheimer's disease associated protein
Mitchelmore, C., Büchmann-Møller, S., Rask, L., West, M. J., Troncoso, J. C., & Jensen, N. A. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.01.003 · Cited by 143 · see citing works
Microglia and the Immune Pathology of Alzheimer Disease
Giulian, D. (1999) · The American Journal of Human Genetics · doi:10.1086/302477 · Cited by 141 · see citing works
Statins Cause Intracellular Accumulation of Amyloid Precursor Protein, β-Secretase-cleaved Fragments, and Amyloid β-Peptide via an Isoprenoid-dependent Mechanism
Cole, S. L., Grudzien, A., Manhart, I. O., Kelly, B. L., Oakley, H. D., & Vassar, R. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413895200 · Cited by 132 · see citing works
Presenilin-1 Regulates Intracellular Trafficking and Cell Surface Delivery of β-Amyloid Precursor Protein
Cai, D., Leem, J. Y., Greenfield, J. P., Wang, P., Kim, B. S., Wang, R., Radomski, K. L., Kim, S.-H., Zheng, H., Greengard, P., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209065200 · Cited by 132 · see citing works
Self-citation
Transcriptional regulation of APH‐1A and increased γ‐secretase cleavage of APP and Notch by HIF‐1 and hypoxia
Wang, R., Zhang, Y., Zhang, X., Liu, R., Zhang, X., Hong, S., Xia, K., Xia, J., Zhang, Z., & Xu, H. (2006) · The FASEB Journal · doi:10.1096/fj.06-5839fje · Cited by 108 · see citing works
Synaptic transmission block by presynaptic injection of oligomeric amyloid beta
Moreno, H., Yu, E., Pigino, G. F., Hernandez, A. I., Kim, N., Moreira, J. E., Sugimori, M., & Llinás, R. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900944106 · Cited by 107 · see citing works
Icariin improves memory impairment in Alzheimer's disease model mice (5xFAD) and attenuates amyloid β‐induced neurite atrophy
Urano, T., & Tohda, C. (2010) · Phytotherapy Research · doi:10.1002/ptr.3183 · Cited by 101 · see citing works
The Basic Biology of BACE1: A Key Therapeutic Target for Alzheimer’s Disease
Cole, S. L., & Vassar, R. (2007) · Current Genomics · doi:10.2174/138920207783769512 · Cited by 97 · see citing works
BACE1 Structure and Function in Health and Alzheimers Disease
Cole, S., & Vassar, R. (2008) · Current Alzheimer Research · doi:10.2174/156720508783954758 · Cited by 96 · see citing works
Plasminogen activator activity is inhibited while neuroserpin is up‐regulated in the Alzheimer disease brain
Fabbro, S., & Seeds, N. W. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05894.x · Cited by 89 · see citing works
Expression of Notch Pathway Components in Spermatogonia and Sertoli Cells of Neonatal Mice
Dirami, G., Ravindranath, N., Achi, M. V., & Dym, M. (2001) · Journal of Andrology · doi:10.1002/j.1939-4640.2001.tb03434.x · Cited by 83 · see citing works
A Role for Presenilin 1 in Regulating the Delivery of Amyloid Precursor Protein to the Cell Surface
Leem, J. Y., Saura, C. A., Pietrzik, C. U., Christianson, J. C., Wanamaker, C., King, L. T., Veselits, M., Tomita, T., Gasparini, L., Iwatsubo, T., et al. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0546 · Cited by 72 · see citing works
Self-citation
Isoprenoids and Alzheimer's disease: A complex relationship
Cole, S. L., & Vassar, R. J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.11.007 · Cited by 70 · see citing works
The Nonconserved Hydrophilic Loop Domain of Presenilin (PS) Is Not Required for PS Endoproteolysis or Enhanced Aβ42 Production Mediated by Familial Early Onset Alzheimer's Disease-linked PS Variants
Saura, C. A., Tomita, T., Soriano, S., Takahashi, M., Leem, J.-Y., Honda, T., Koo, E. H., Iwatsubo, T., & Thinakaran, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909624199 · Cited by 65 · see citing works
Self-citation
Early Onset Alzheimer’s Disease and Oxidative Stress
Meraz‐Ríos, M. A., Franco-Bocanegra, D., Toral-Ríos, D., & Campos‐Peña, V. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/375968 · Cited by 62 · see citing works
Calpain Dysregulation in Alzheimer’s Disease
Ferreira, A. (2012) · ISRN Biochemistry · doi:10.5402/2012/728571 · Cited by 61 · see citing works
Metabolic syndrome as a risk factor for Alzheimer's disease: Is Aβ a crucial factor in both pathologies?
Campos-Peña, V., Toral-Rios, D., Becerril-Pérez, F., Sánchez-Torres, C., Delgado-Namorado, Y., Torres-Ossorio, E., Franco-Bocanegra, D., & Carvajal, K. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6768 · Cited by 58 · see citing works
Inhibition of BACE, a Promising Approach to Alzheimers Disease Therapy
Roggo, S. P. (2002) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026024607490 · Cited by 58 · see citing works
β-Secretase, APP and Aβ in Alzheimer’s Disease
Vassar, R. J. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_4 · Cited by 52 · see citing works
Presenilins and γ-Secretase Inhibitors Affect Intracellular Trafficking and Cell Surface Localization of the γ-Secretase Complex Components
Wang, H., Luo, W., Zhang, Y., Li, Y., Thinakaran, G., Greengard, P., & Xu, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404345200 · Cited by 47 · see citing works
Self-citation
Presenilins and APP in Neuritic and Synaptic Plasticity: Implications for the Pathogenesis of Alzheimer's Disease
Chan, S. L., Furukawa, K., & Mattson, M. P. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:167 · Cited by 45 · see citing works
Potential Treatment Opportunities for Alzheimer's Disease Through Inhibition of Secretases and Aβ Immunization
Schenk, D., Games, D., & Seubert, P. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:259 · Cited by 44 · see citing works
A pharmacogenomic approach to Alzheimer’s disease
Cacabelos, R., Álvarez, A., Fernández‐Novoa, L., & Lombardi, V. (2000) · Acta Neurologica Scandinavica · doi:10.1034/j.1600-0404.2000.00302.x · Cited by 42 · see citing works
Regional brain metabolism with cytochrome c oxidase histochemistry in a PS1/A246E mouse model of autosomal dominant Alzheimer's disease: Correlations with behavior and oxidative stress
Strazielle, C., Jazi, R., Verdier, Y., Qian, S., & Lalonde, R. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.08.005 · Cited by 41 · see citing works
Genetic counseling and ethical issues for autism
McMahon, W. M., Baty, B. J., & Botkin, J. R. (2006) · American Journal of Medical Genetics Part C Seminars in Medical Genetics · doi:10.1002/ajmg.c.30082 · Cited by 41 · see citing works
Altered splicing in exon 8 of the DNA replication factor CIZ1 affects subnuclear distribution and is associated with Alzheimer's disease
Dahmcke, C. M., Büchmann-Møller, S., Jensen, N. A., & Mitchelmore, C. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.05.007 · Cited by 38 · see citing works
Pterostilbene ameliorates intracerebroventricular streptozotocin induced memory decline in rats
Naik, B. N., Nirwane, A. M., & Majumdar, A. S. (2016) · Cognitive Neurodynamics · doi:10.1007/s11571-016-9413-1 · Cited by 36 · see citing works
Transcriptional Regulation of PEN-2, a Key Component of the γ-Secretase Complex, by CREB
Wang, R., Zhang, Y., Sun, P., Liu, R., Zhang, X., Zhang, X., Xia, K., Xia, J., Xu, H., & Zhang, Z. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1347-1354.2006 · Cited by 36 · see citing works
Novel Role of Presenilins in Maturation and Transport of Integrin β1
Zou, K., Hosono, T., Nakamura, T., Shiraishi, H., Maeda, T., Komano, H., Yanagisawa, K., & Michikawa, M. (2008) · Biochemistry · doi:10.1021/bi7014508 · Cited by 32 · see citing works
Amyloid‐beta levels are significantly reduced and spatial memory defects are rescued in a novel neuroserpin‐deficient Alzheimer’s disease transgenic mouse model
Fabbro, S., Schaller, K., & Seeds, N. W. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07359.x · Cited by 31 · see citing works
Intracellular Retention of Caveolin 1 in Presenilin-deficient Cells
Wood, D. R., Nye, J. S., Lamb, N. J. C., Fernandez, A., & Kitzmann, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410332200 · Cited by 28 · see citing works
Intracerebroventricular Aβ-Induced Neuroinflammation Alters Peripheral Immune Responses in Rats
Gupta, P., Sil, S., Ghosh, R., Ghosh, A., & Ghosh, T. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1189-9 · Cited by 26 · see citing works
Spastic paraplegia, ataxia, mental retardation (SPAR)
Hedera, P., Rainier, S. R., Zhao, X. P., Schalling, M., Lindblad‐Toh, K., Yuan, Q.-P., Ikeuchi, T., Trobe, J. D., Wald, J. J., Eldevik, O. P., et al. (2002) · Neurology · doi:10.1212/wnl.58.3.411 · Cited by 26 · see citing works
Expression of Amyloid precursor protein, tau and presenilin RNAs in rat hippocampus following deafferentation lesions
Ramírez, M. J., Heslop, K. E., Francis, P. T., & Rattray, M. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02580-x · Cited by 25 · see citing works
A partner for presenilin
Schenk, D. (2000) · Nature · doi:10.1038/35024194 · Cited by 25 · see citing works
Identification of the Presenilins in Hematopoietic Cells with Localization of Presenilin 1 to Neutrophil and Platelet Granules
Korade, Ž., Calafat, J., Udby, L., Lovelock, J., Kjeldsen, L., Rothermund, K. D., Sisodia, S. S., Borregaard, N., & Corey, S. J. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0486 · Cited by 24 · see citing works
Self-citation
Should Alzheimer's disease be equated with human brain ageing?: A maladaptive interaction between brain evolution and senescence
Neill, D. (2011) · Ageing Research Reviews · doi:10.1016/j.arr.2011.06.004 · Cited by 21 · see citing works
Notch Signaling in T-Cell Acute Lymphoblastic Leukemia
Weng, A. P., & Lau, A. N. (2005) · Future Oncology · doi:10.2217/14796694.1.4.511 · Cited by 20 · see citing works
Alzheimer Disease: The Role of Aβ in the Glutamatergic System
Campos‐Peña, V., & Antônio, M. (2014) · InTech eBooks · doi:10.5772/57367 · Cited by 18 · see citing works
The presenilin loop region is essential for glycogen synthase kinase 3 β (GSK3β) mediated functions on motor proteins during axonal transport
Banerjee, R., Rudloff, Z., Naylor, C., Yu, M. C., & Gunawardena, S. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy190 · Cited by 17 · see citing works
A carboxylated Zn‐phthalocyanine inhibits fibril formation of Alzheimer's amyloid β peptide
Tabassum, S., Sheikh, A. M., Yano, S., Ikeue, T., Handa, M., & Nagai, A. (2014) · FEBS Journal · doi:10.1111/febs.13151 · Cited by 15 · see citing works
Chapter 4. Secretase inhibitors as therapeutics for Alzheimer's disease
Olson, R. E., & Thompson, L. A. (2000) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(00)35005-9 · Cited by 14 · see citing works
Presenilins regulate the cellular level of the tumor suppressor PTEN
Zhang, H., Liu, R., Wang, R., Hong, S., Xu, H., & Zhang, Y. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.11.020 · Cited by 12 · see citing works
Human β-secretase and Alzheimer’s disease
Citron, M. (2001) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.5.3.341 · Cited by 11 · see citing works
Current Trends in the Development of Drugs for the Treatment of Alzheimer’s Disease and their Clinical Trials
Бачурин, С. О., Bovina, E. V., & Ustyugov, A. A. (2018) · Biomedical Chemistry Research and Methods · doi:10.18097/bmcrm00015 · Cited by 10 · see citing works
Stature Estimation from Foramen Magnum Region in Chinese Population
Cui, Y., & Zhang, J. (2013) · Journal of Forensic Sciences · doi:10.1111/1556-4029.12192 · Cited by 10 · see citing works
PS1 Affects the Pathology of Alzheimer’s Disease by Regulating BACE1 Distribution in the ER and BACE1 Maturation in the Golgi Apparatus
Li, N., Qiu, Y., Wang, H., Zhao, J., & Qing, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232416151 · Cited by 9 · see citing works
Analysis of the disease risk locus DXS1047 polymorphism in Brazilian Alzheimer patients
Nishimura, A. L., de Oliveira, J. R. M., Matioli, S. R., de Brito-Marques, P. R., Bahia, V. S., Nitríni, R., & Zatz, M. (2000) · Molecular Psychiatry · doi:10.1038/sj.mp.4000767 · Cited by 9 · see citing works
La apoptosis en las enfermedades neurodegenerativas: evidencias y controversias
Jiménez-Del-Río, M., & Velez‐Pardo, C. (2001) · Revista de Neurología · doi:10.33588/rn.3209.2000495 · Cited by 6 · see citing works
No evidence of association between the D10S1423 locus and Alzheimer disease in Brazilian patients
Nishimura, A. L., Oliveira, J. R. M., Otto, P. A., Matioli, S. R., de Brito-Marques, P. R., Bahia, V. S., Nitríni, R., & Zatz, M. (2001) · Journal of Neural Transmission · doi:10.1007/s007020170076 · Cited by 6 · see citing works
Genetics of Alzheimer´S Disease
Campos‐Peña, V., Gmez, R., & Antônio, M. (2014) · InTech eBooks · doi:10.5772/58286 · Cited by 4 · see citing works
APP Biology, Processing and Function
Thinakaran, G., & Koo, E. H. (2007) · Springer eBooks · doi:10.1007/978-0-387-35135-3_2 · Cited by 4 · see citing works
Self-citation
Redox Status and Aging Link in Neurodegenerative Diseases 2015
de la Cruz, V. P., Korrapati, S. V., & Pedraza-Chaverri, J. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/494316 · Cited by 2 · see citing works
Fingolimod normalizes metabolic signatures associated with synaptic plasticity and memory in APP/PS1 model: Sphingosine-1-phosphate receptor a therapeutic target for Alzheimer’s
Kalecký, K., Buitrago, L., Alarcón, J. M., Singh, A., Bottiglieri, T., Kaddurah-Daouk, R. F., & Hernández, A. I. (2026) · Scientific Reports · doi:10.1038/s41598-026-42518-8 · Cited by 3 · see citing works
Rescue of hippocampal synaptic plasticity and memory performance by Fingolimod (FTY720) in APP/PS1 model of Alzheimer’s disease is accompanied by correction in metabolism of sphingolipids, polyamines, and phospholipid saturation compositionPreprint
Kalecký, K., Buitrago, L., Alarcón, J. M., Singh, A., Bottiglieri, T., Kaddurah-Daouk, R. F., & Hernandez, A. I. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.17.633452 · Cited by 1 · see citing works
Untersuchungen über die Auswirkungen von Geschlecht und genetischem Hintergrund auf die Alzheimerpathologie im 5xFAD-Mausmodell
Nordmeyer, P. J. (2015) · doi:10.53846/goediss-5124
Lessons from presenilin domain analysis: endoproteolytic processing and enhanced Aβ42 production mediated by FAD-linked variants
Thinakaran, G., Saura, C. A., Tomita, T., Honda, T., & Iwatsubo, T. (2001) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8225-5_19
Self-citation
Anti-Aging Medicine LiteratureWatch
Pawelec, G. (1998) · Rejuvenation Research · doi:10.1089/rej.1.1998.1.275
The Molecular and Genetic Basis of Neurodegenerative Diseases
Tousseyn, T., Simko, J. P., Gaskin, D. A., & DeArmond, S. J. (2009) · Elsevier eBooks · doi:10.1016/b978-1-4160-3966-2.00052-7
Untersuchung genetischer und geschlechtlicher Einflüsse in der Alzheimerpathologie anhand des Maustiermodells 5XFAD
Kratz, S. R. A. (2010) · doi:10.53846/goediss-871
Presenilins
(2004) · Encyclopedic Dictionary of Genetics, Genomics and Proteomics · doi:10.1002/0471684228.egp09989
Anti-Aging Medicine LiteratureWatch
Pawelec, G. (1999) · Rejuvenation Research · doi:10.1089/rej.1.1999.2.295

Presenilin 2 — APP Interactions
Wasco, W., Tanzi, R. E., Moir, R. D., Crowley, A. C., Merriam, D. E., Romano, D., Jondro, P. D., & Kellerman, B. A. (1998) · Springer eBooks · doi:10.1007/978-3-642-72103-8_7
Presenilins: Genes for Life and Death
Haass, C. (1997) · Neuron · doi:10.1016/s0896-6273(00)80309-8 · Cited by 145 · see citing works
Presenilins and Alzheimer’s disease: biological functions and pathogenic mechanisms
Czech, C., Tremp, G. L., & Pradier, L. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(99)00033-7 · Cited by 155 · see citing works
Presenilins
Vetrivel, K. S., & Thinakaran, G. (2007) · doi:10.1093/oso/9780198566618.003.0008
Self-citation
Presenilin Proteins and the Pathogenesis of Early-Onset Familial Alzheimer’s Disease: β-Amyloid Production and Parallels to Prion Diseases
Westaway, D. A., Carlson, G. A., Bergeron, C., Lévesque, G., Sherrington, R., Yao, H., Strome, R., Perry, B. J., Davies, A., Gandy, S., et al. (1998) · Springer eBooks · doi:10.1007/978-1-4899-1896-3_17 · Cited by 1 · see citing works

Authors: Sisodia, S. S., Kim, S. H., & Thinakaran, G.
Affiliations: University of Chicago (US)
Corresponding author: Sisodia, Sangram S.
ORCID: Sisodia, Sangram S.
Kim, Seong H.
Thinakaran, Gopal
Venue: The American Journal of Human Genetics
Publisher: Elsevier BV
Published: 1999-07
Volume: 65
Issue: 1
Pages: 7-12
ISSN: 0002-9297 (ISSN-L)
DOI: 10.1086/302475
PMC: PMC1378068
OpenAlex: W2090703486
Cited by: 76
References: 44
Citations by year: 2026: 1 · 2025: 1 · 2022: 1 · 2018: 3 · 2017: 1 · 2016: 2 · 2015: 2 · 2014: 5 · 2013: 2 · 2012: 1
FWCI: 1.13
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5132 d)
Locations: The American Journal of Human Genetics (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
U.S. Public Health Service
National Institute on Aging (P01AG010491, AG10491, P50AG005146, AG 05146)
National Institute of Neurological Disorders and Stroke (NS-20471)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: presenilin, presenilin 1, presenilin 2, Alzheimer's disease, familial Alzheimer's disease, amyloid precursor protein, amyloid-beta, tau hyperphosphorylation, neurofibrillary tangles, amyloid plaques, autosomal dominant inheritance, APP mutations
MeSH terms: Adult, Alzheimer Disease, Animals, Humans, Membrane Proteins, Mice, Transgenic, Middle Aged, Models, Biological, Helminth Proteins, Amyloid beta-Protein Precursor, Caenorhabditis elegans, Age of Onset, Caenorhabditis elegans Proteins, Mice, Receptors, Notch, Presenilin-1, Presenilin-2

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Function and Dysfunction of the Presenilins

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks