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

A secreted form of human ADAM9 has an α-secretase activity for APP

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Generation of Anti-apoptotic Presenilin-2 Polypeptides by Alternative Transcription, Proteolysis, and Caspase-3 Cleavage

Vito, P., Ghayur, T., & D'adamio, L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28315 · Cited by 107

α1-antichymotrypsin

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Relative Increase in Alzheimer's Disease of Soluble Forms of Cerebral Aβ Amyloid Protein Precursor Containing the Kunitz Protease Inhibitory Domain

Moir, R. D., Lynch, T., Bush, A. I., Whyte, S., Henry, A., Portbury, S. D., Multhaup, G., Small, D. H., Tanzi, R. E., Beyreuther, K. T., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.5013 · Cited by 103

Insulin-degrading enzyme in the Alzheimer's disease brain: prominent localization in neurons and senile plaques

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α2-macroglobulin expression in neuritic-type plaques in patients with Alzheimer's disease

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α2-Macroglobulin in late-onset Alzheimer's disease

Kovacs, D. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00113-3 · Cited by 98

Degradation of Amyloid β-Protein by a Serine Protease-α2-Macroglobulin Complex

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A Genome Survey for Novel Alzheimer Disease Risk Loci: Results at 10-cM Resolution

Zubenko, G. S., Hughes, H. B., Stiffler, J. S., Hurtt, M. R., & Kaplan, B. B. (1998) · Genomics · doi:10.1006/geno.1998.5306 · Cited by 97

Glu11 Site Cleavage and N-Terminally Truncated Aβ Production upon BACE Overexpression

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Characterization of the Glycosylation Profiles of Alzheimer's β-Secretase Protein Asp-2 Expressed in a Variety of Cell Lines

Charlwood, J., Dingwall, C., Matico, R., Hussain, I., Johanson, K., Moore, S. E., Powell, D. J., Skehel, M. J., Ratcliffe, S., Clarke, B. P., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009361200 · Cited by 96

Presenilin 1 Regulates Pharmacologically Distinct γ-Secretase Activities

Murphy, M. P., Uljon, S., Fraser, P. E., Fauq, A. H., Lookingbill, H. A., Findlay, K. A., Smith, T. E., Lewis, P. A., McLendon, D. C., Wang, R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002812200 · Cited by 96

A non‐amyloidogenic function of BACE‐2 in the secretory pathway

Fluhrer, R., Capell, A., Westmeyer, G., Willem, M., Hartung, B., Condron, M. M., Teplow, D. B., Haass, C., & Walter, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00908.x · Cited by 95

Substantial linkage disequilibrium across the insulin-degrading enzyme locus but no association with late-onset Alzheimer's disease

Abraham, R., Myers, A., Wavrant-DeVrièze, F., Hamshere, M. L., Thomas, H. V., Marshall, H. N., Compton, D., Spurlock, G., Turic, D., Hoogendoorn, B., et al. (2001) · Human Genetics · doi:10.1007/s00439-001-0614-1 · Cited by 95

Genetic variability in the regulatory region of presenilin 1 associated with risk for Alzheimer's disease and variable expression

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An α-2-macroglobulin insertion-deletion polymorphism in Alzheimer disease (reply)

Blacker, D., Crystal, A. S., Wilcox, M., Laird, N. M., & Tanzi, R. E. (1999) · Nature Genetics · doi:10.1038/8732 · Cited by 93

Aph-2/Nicastrin

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The protease inhibitory properties of the Alzheimer's beta-amyloid precursor protein.

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A new aspartyl protease on 21q22.3, BACE2, is highly similar to Alzheimer’s amyloid precursor protein β-secretase

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No Genetic Effect of α1-Antichymotrypsin in Alzheimer Disease

Haines, J. L., Pritchard, M. L., Saunders, A. M., Schildkraut, J. M., Growdon, J. H., Gaskell, P. C., Farrer, L. A., Auerbach, S. H., Gusella, J. F., Locke, P. A., et al. (1996) · Genomics · doi:10.1006/geno.1996.0158 · Cited by 87

Separation of presenilin function in amyloid β-peptide generation and endoproteolysis of Notch

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Endogenous Presenilin-1 Targets to Endocytic Rather Than Biosynthetic Compartments

Lah, J. J., & Levey, A. I. (2000) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2000.0861 · Cited by 84

Molecular evolution of serpins: homologous structure of the human .alpha.1-antichymotrypsin and .alpha.1-antitrypsin genes

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Targeted Inactivation of the Mouse α2-Macroglobulin Gene

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Genetic association of alpha2-macroglobulin with Alzheimer's disease in a Finnish elderly population.

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Amyloidogenic determinant as a substrate recognition motif of insulin‐degrading enzyme

Kurochkin, I. V. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00422-0 · Cited by 79

An α-2-macroglobulin insertion-deletion polymorphism in Alzheimer disease

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α-2 macroglobulin polymorphism and Alzheimer disease risk in the UK

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α‐Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

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Mapping of the gene encoding the beta-amyloid precursor protein and its relationship to the Down syndrome region of chromosome 21.

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α-2 macroglobulin gene and Alzheimer disease

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Erratum: Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1

Huppert, S. S., Le, A., Schroeter, E. H., Mumm, J. S., Saxena, M. T., Milner, L. A., & Kopan, R. (2000) · Nature · doi:10.1038/35046136 · Cited by 74

A Novel Metalloproteinase Associated with Brain Myelin Membranes

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Insulin-Degrading Enzyme: Stable Expression of the Human Complementary DNA, Characterization of its Protein Product, and Chromosomal Mapping of the Human and Mouse Genes

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Genomic Structure and Expression of STM2, the Chromosome 1 Familial Alzheimer Disease Gene

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Familial Alzheimer's disease: Site of mutation influences clinical phenotype

Lippa, C. F., Swearer, J. M., Kane, K., Nochlin, D., Bird, T. D., Ghetti, B. F., Nee, L. E., George‐Hyslop, P. S., Pollen, D. A., & Drachman, D. A. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200009)48:3 · Cited by 67

The Alternatively Spliced Kunitz Protease Inhibitor Domain Alters Amyloid β Protein Precursor Processing and Amyloid β Protein Production in Cultured Cells

Ho, L., Fukuchi, K.-I., & Younkin, S. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30929 · Cited by 66

Complex N‐glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments

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Alzheimer's Peptide Aβ1–42 Binds to Two β-Sheets of α1-Antichymotrypsin and Transforms It from Inhibitor to Substrate

Janciauskiene, S. M., Rubin, H. N., Lukacs, C., & Wright, H. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.28360 · Cited by 64

Endogenous presenilin 1 redistributes to the surface of lamellipodia upon adhesion of Jurkat cells to a collagen matrix

Schwarzman, A. L., Singh, N., Tsiper, M. V., Gregori, L. L., Dranovsky, A., Vitek, M. P., Glabe, C. G., George‐Hyslop, P. S., & Goldgaber, D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.14.7932 · Cited by 64

Cell surface expression of the Alzheimer disease-related presenilin proteins

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The −48 C/T polymorphism in the presenilin 1 promoter is associated with an increased risk of developing Alzheimer's disease and an increased Aβ load in brain

Lambert, J.-C., Mann, D. M. A., Harris, J. M., Chartier-Harlin, M.-C., Cumming, A., Coates, J., Lemmon, H., StClair, D., Iwatsubo, T., & Lendon, C. (2001) · Journal of Medical Genetics · doi:10.1136/jmg.38.6.353 · Cited by 61

Mechanism of Interleukin-1- and Tumor Necrosis Factor α-Dependent Regulation of the α1-Antichymotrypsin Gene in Human Astrocytes

Kordula, T., Bugno, M., Rydel, R. E., & Travis, J. W. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-20-07510.2000 · Cited by 60

Regulation of Brain G-protein Go by Alzheimer's Disease Gene Presenilin-1

Smine, A., Xu, X., Nishiyama, K., Katada, T., Gambetti, P. L., Yadav, S. P., Wu, X., Shi, Y., Yasuhara, S., Homburger, V., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16281 · Cited by 60

A Splice Variant of β-Secretase Deficient in the Amyloidogenic Processing of the Amyloid Precursor Protein

Bodendorf, U., Fischer, F., Bodian, D., Multhaup, G., & Paganetti, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008861200 · Cited by 58

The Alzheimer amyloid precursor protein maps to human chromosome 21 bands q21.105–q21.05

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Differential Effects of the Swedish Mutant Amyloid Precursor Protein on β-Amyloid Accumulation and Secretion in Neurons and Nonneuronal Cells

Forman, M. S., Cook, D. G., Leight, S., Doms, R. W., & Lee, V. M. ‐. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32247 · Cited by 57

In search of an enzyme: the β-secretase of Alzheimer's disease is an aspartic proteinase

Howlett, D. R., Simmons, D. L., Dingwall, C., & Christie, G. (2000) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01647-7 · Cited by 56

Three novel alternatively spliced isoforms of the human beta-site amyloid precursor protein cleaving enzyme (BACE) and their effect on amyloid beta-peptide production

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A specific structural interaction of Alzheimer's peptide Aβ1–42 with α1-antichymotrypsin

Janciauskiene, S. M., Eriksson, S., & Wright, H. T. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0896-668 · Cited by 51

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

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Closing in on the Amyloid Cascade

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Nicastrin, a presenilin-interacting protein, contains an aminopeptidase/transferrin receptor superfamily domain

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The secretases that cleave angiotensin converting enzyme and the amyloid precursor protein are distinct from tumour necrosis factor‐α convertase

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A detetion polymorphism in the human alpha-2-macroglobulin (A2M) gene

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Effect of the APOE promoter polymorphisms on cerebral amyloid peptide deposition in Alzheimer's disease

Lambert, J., Mann, D. M. A., Goumidi, L., Harris, J., Amouyel, P., Iwatsubo, T., Lendon, C., & Chartier‐Harlin, M. (2001) · The Lancet · doi:10.1016/s0140-6736(00)04063-0 · Cited by 46

The common acute lymphoblastic leukemia antigen gene maps to chromosomal region 3 (q21-q27).

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Elevated expression of beta-site amyloid precursor protein cleaving enzyme 2 in brains of patients with Down syndrome

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α1‐Antichymotrypsin as a risk modifier for late‐onset Alzheimer's disease in Japanese apolipoprotein E ε4 allele carriers

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Apolipoprotein E and α-1-antichymotrypsin allele polymorphism in sporadic and familial Alzheimer's disease

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Association of alpha1-antichymotrypsin deficiency with milder lung disease in patients with cystic fibrosis

Mahadeva, R. (2001) · Thorax · doi:10.1136/thorax.56.1.53 · Cited by 42

Genetic variation in α1-antichymotrypsin and its association with Alzheimer’s disease

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Amyloid β vaccination: reduced plaques and improved cognition

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Inhibitory effect of a presenilin 1 mutation on the Wnt signalling pathway by enhancement of β‐catenin phosphorylation

Kawamura, Y., Kikuchi, A., Takada, R., Takada, S., Sudoh, S., Shibamoto, S., Yanagisawa, K., & Komano, H. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02197.x · Cited by 38

Spotlight on BACE: The secretases as targets for treatment in Alzheimer disease

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Analysis of the Subsite Specificity of Rat Insulysin Using Fluorogenic Peptide Substrates

Song, E.-S., Mukherjee, A., Juliano, M. A., Pyrek, J. S., Goodman, J. P., Juliano, L., & Hersh, L. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008702200 · Cited by 38

No association between the alpha 1‐antichymotrypsin A allele and Alzheimer's disease

Murphy, G. M., Sullivan, E. V., Gallagher-Thompson, D. E., Thompson, L. W., van Duijn, C. M., Forno, L. S., Ellis, W. G., Jagust, W. J., Yesavage, J. A., & Tinklenberg, J. R. (1997) · Neurology · doi:10.1212/wnl.48.5.1313 · Cited by 37

Hereditary α2‐Macroglobulin Deficiency

Bergqvist, D., & Nilsson, I. M. (1979) · Scandinavian Journal of Haematology · doi:10.1111/j.1600-0609.1979.tb02745.x · Cited by 36

Effects of recombinant neutral endopeptidase (EC 3.4.24.11) on the growth of lung cancer cell lines in vitro and in vivo.

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Apolipoprotein E and alpha‐1 antichymotrypsin polymorphism genotyping in Alzheimer's disease and in dementia with Lewy bodies Distinctions between diseases

Lamb, H., CHRISTIE, J. E., Singleton, A., Leake, A., Perry, R. H., Ince, P. G., McKeith, I. G., Melton, L., Edwardson, J. A., & Morris, C. M. (1998) · Neurology · doi:10.1212/wnl.50.2.388 · Cited by 35

Posttranslational Modification and Plasma Membrane Localization of the Drosophila melanogaster Presenilin

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BACE1 interacts with nicastrin

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Alpha-1-antichymotrypsin bi-allele polymorphism, apolipoprotein-E tri-allele polymorphism and genetic risk of Alzheimer's syndrome

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The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity

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α1‐Antichymotrypsin/Alzheimer's peptide Aβ1–42 complex perturbs lipid metabolism and activates transcription factors PPARγ and NFκB in human neuroblastoma (Kelly) cells

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The Role of Alzheimer's Disease-Related Presenilin 1 in Intercellular Adhesion

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Dinucleotide repeat polymorphisms in the Neprilysin gene are not associated with sporadic Alzheimer's disease

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Structure of the human alpha-2 macroglobulin gene and its promotor

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Negative Regulation of the Sapk/Jnk Signaling Pathway by Presenilin 1

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The gene for the human putative apoE receptor is on chromosome 12 in the segment q13–14

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Polymorphism in the alpha1-antichymotrypsin (ACT) gene promoter: effect on expression in transfected glial and liver cell lines and plasma ACT concentrations

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A partner for presenilin

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α-Antichymotrypsin gene polymorphism and risk for Alzheimer's disease in the Spanish population

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Potential novel targets for Alzheimer pharmacotherapy: I. Secretases

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Apolipoprotein E is a genetic risk factor for fetal iodine deficiency disorder in China

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Proteolysis in Alzheimer's disease

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Protease inhibitors of human plasma. Alpha 1-antichymotrypsin.

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The common acute lymphoblastic leukemia antigen (Neutral endopeptidase-3.4.24.11) gene is located on human chromosome 3

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