Proteolytic Degradation of Amyloid -Protein

Decreased Clearance of CNS β-Amyloid in Alzheimer’s Disease

Mawuenyega, K. G., Sigurdson, W., Ovod, V., Munsell, L., Kasten, T., Morris, J. C., Yarasheski, K. E., & Bateman, R. J. (2010) · Science · doi:10.1126/science.1197623 · Cited by 2,078 · see citing works

Gene regulation and DNA damage in the ageing human brain

Lu, T., Pan, Y., Kao, S.-Y., Li, C., Kohane, I., Chan, J., & Yankner, B. A. (2004) · Nature · doi:10.1038/nature02661 · Cited by 1,874 · see citing works

Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database

Bertram, L., McQueen, M. B., Mullin, K., Blacker, D., & Tanzi, R. E. (2007) · Nature Genetics · doi:10.1038/ng1934 · Cited by 1,857 · see citing works

The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.

Van Wart, H. E., & Birkedal-Hansen, H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.14.5578 · Cited by 1,475 · see citing works

Insulin-degrading enzyme regulates the levels of insulin, amyloid β-protein, and the β-amyloid precursor protein intracellular domain in vivo

Farris, W., Mansourian, S., Chang, Y., Lindsley, L., Eckman, E., Frosch, M., Eckman, C., Tanzi, R., Selkoe, D., & Guénette, S. (2003) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0230450100 · Cited by 1,361 · see citing works

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 · see citing works

A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors

Ponte, P. A., Gonzalez‐DeWhitt, P. A., Schilling, J., Miller, J., Hsu, D. K., Greenberg, B., Davis, K. L., Wallace, W., Lieberburg, I. M., Fuller, F. H., et al. (1988) · Nature · doi:10.1038/331525a0 · Cited by 1,050 · see citing works

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 · see citing works

Adult mouse astrocytes degrade amyloid-β in vitro and in situ

Wyss-Coray, T., Loike, J. D., Brionne, T. C., Lu, E., Anankov, R., Yan, F., Silverstein, S. C., & Husemann, J. (2003) · Nature Medicine · doi:10.1038/nm838 · Cited by 909 · see citing works

Metabolic Regulation of Brain Aβ by Neprilysin

Iwata, N., Tsubuki, S., Takaki, Y., Shirotani, K., Lu, B., Gerard, N., Gerard, C., Hama, E., Lee, H., & Saido, T. (2001) · Science · doi:10.1126/science.1059946 · Cited by 894 · see citing works

Immunochemical identification of the serine protease inhibitor α1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease

Abraham, C. R., Selkoe, D. J., & Potter, H. (1988) · Cell · doi:10.1016/0092-8674(88)90462-x · Cited by 893 · see citing works

Identification of the major Aβ1–42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition

Iwata, N., Tsubuki, S., Takaki, Y., Watanabe, K., Sekiguchi, M., Hosoki, E., Kawashima-Morishima, M., Lee, H.-J., Hama, E., Sekine-Aizawa, Y., et al. (2000) · Nature Medicine · doi:10.1038/72237 · Cited by 867 · see citing works

Insulin-degrading Enzyme Regulates Extracellular Levels of Amyloid β-Protein by Degradation

Qiu, W. Q., Walsh, D. M., Ye, Z., Vekrellis, K., Zhang, J., Podlisny, M. B., Rosner, M. R., Safavi, A., Hersh, L. B., & Selkoe, D. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32730 · Cited by 812 · see citing works

Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology.

Roques, B. P., Noble, F., Daugé, V., Fournié‐Zaluski, M., & Beaumont, A. (1993) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)00449-1 · Cited by 754 · see citing works

Enhanced Proteolysis of β-Amyloid in APP Transgenic Mice Prevents Plaque Formation, Secondary Pathology, and Premature Death

Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00787-6 · Cited by 708 · see citing works

Human amyloid-β synthesis and clearance rates as measured in cerebrospinal fluid in vivo

Bateman, R. J., Munsell, L. Y., Morris, J. C., Swarm, R., Yarasheski, K. E., & Holtzman, D. M. (2006) · Nature Medicine · doi:10.1038/nm1438 · Cited by 599 · see citing works

Clearing the brain's amyloid cobwebs

Selkoe, D. J. (2001) · Neuron · doi:10.1016/s0896-6273(01)00475-5 · Cited by 541 · see citing works

Neurons Regulate Extracellular Levels of Amyloid β-Protein via Proteolysis by Insulin-Degrading Enzyme

Vekrellis, K., Ye, Z., Qiu, W. Q., Walsh, D. M., Hartley, D. M., Chesneau, V., Rosner, M. R., & Selkoe, D. J. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-05-01657.2000 · Cited by 495 · see citing works

Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease.

Mueller-Steiner, S., Zhou, Y.-G., Arai, H., Roberson, E., Sun, B.-G., Chen, J., Wang, X., Yu, G.-Q., Esposito, L., Mucke, L., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.027 · Cited by 466 · see citing works

The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function

Turner, A. J., Isaac, R. E., & Coates, D. (2001) · BioEssays · doi:10.1002/1521-1878(200103)23:3 · Cited by 450 · see citing works

Protease nexin-II, a potent anti-chymotrypsin, shows identity to amyloid β-protein precursor

Nostrand, W. E. V., Wagner, S. L., Suzuki, M., Choi, B. H., Farrow, J. S., Geddes, J. W., Cotman, C. W., & Cunningham, D. D. (1989) · Nature · doi:10.1038/341546a0 · Cited by 438 · see citing works

Clearance of Alzheimer's Aβ Peptide

Tanzi, R. E., Moir, R. D., & Wagner, S. L. (2004) · Neuron · doi:10.1016/j.neuron.2004.08.024 · Cited by 431 · see citing works

Neprilysin Gene Transfer Reduces Human Amyloid Pathology in Transgenic Mice

Marr, R. A., Rockenstein, E. M., Mukherjee, A., Kindy, M. S., Hersh, L. B., Gage, F. H., Verma, I. M., & Masliah, E. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-06-01992.2003 · Cited by 391 · see citing works

Matrix Metalloproteinases Expressed by Astrocytes Mediate Extracellular Amyloid-β Peptide Catabolism

Yin, K.-J., Cirrito, J. R., Yan, P., Hu, X., Xiao, Q., Pan, X., Bateman, R., Song, H., Hsu, F.-F., Turk, J., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2085-06.2006 · Cited by 381 · see citing works

Matrix Metalloproteinase-9 Degrades Amyloid-β Fibrils in Vitro and Compact Plaques in Situ

Yan, P., Hu, X., Song, H., Yin, K., Bateman, R. J., Cirrito, J. R., Xiao, Q., Hsu, F. F., Turk, J. W., Xu, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602440200 · Cited by 380 · see citing works

Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism

Shen, Y., Joachimiak, A., Rosner, M. R., & Tang, W. (2006) · Nature · doi:10.1038/nature05143 · Cited by 375 · see citing works

Somatostatin regulates brain amyloid β peptide Aβ42 through modulation of proteolytic degradation

Saito, T., Iwata, N., Tsubuki, S., Takaki, Y., Takano, J., Huang, S.-M., Suemoto, T., Higuchi, M., & Saido, T. C. (2005) · Nature Medicine · doi:10.1038/nm1206 · Cited by 361 · see citing works

Phenotypic and Biochemical Analyses of BACE1- and BACE2-deficient Mice

Dominguez, D. I., Tournoy, J., Hartmann, D., Huth, T., Cryns, K., Deforce, S., Serneels, L., Espuny-Camacho, I., Marjaux, E., Craessaerts, K., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505249200 · Cited by 359 · see citing works

Degradation of the Alzheimer's Amyloid β Peptide by Endothelin-converting Enzyme*

Eckman, E., Reed, D. K., & Eckman, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007579200 · Cited by 345 · see citing works

Cathepsin B

Mort, J. S., & Buttle, D. J. (1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(96)00152-5 · Cited by 333 · see citing works

Neprilysin Degrades Both Amyloid β Peptides 1–40 and 1–42 Most Rapidly and Efficiently among Thiorphan- and Phosphoramidon-sensitive Endopeptidases

Shirotani, K., Tsubuki, S., Iwata, N., Takaki, Y., Yamao‐Harigaya, W., Maruyama, K., Kiryu‐Seo, S., Kiyama, H., Iwata, H., Tomita, T., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008511200 · Cited by 312 · see citing works

Angiotensin-converting Enzyme Degrades Alzheimer Amyloid β-Peptide (Aβ); Retards Aβ Aggregation, Deposition, Fibril Formation; and Inhibits Cytotoxicity*

Hu, J.-G., Igarashi, A., Kamata, M., & Nakagawa, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104068200 · Cited by 307 · see citing works

Age- and region-dependent alterations in Aβ-degrading enzymes: implications for Aβ-induced disorders

Caccamo, A., Oddo, S., Sugarman, M. C., Akbari, Y., & LaFerla, F. M. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.06.013 · Cited by 299 · see citing works

Alzheimer disease, the two-hit hypothesis: An update

Zhu, X., Lee, H., Perry, G. L., & Smith, M. A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.10.014 · Cited by 292 · see citing works

Alzheimer's Disease β-Amyloid Peptide Is Increased in Mice Deficient in Endothelin-converting Enzyme

Eckman, E. A., Watson, M., Marlow, L. A., Sambamurti, K., & Eckman, C. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200642200 · Cited by 263 · see citing works

Presynaptic Localization of Neprilysin Contributes to Efficient Clearance of Amyloid-β Peptide in Mouse Brain

Iwata, N., Mizukami, H., Shirotani, K., Takaki, Y., Muramatsu, S., Lu, B., Gerard, N. P., Gerard, C. J., Ozawa, K., & Saido, T. C. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4792-03.2004 · Cited by 258 · see citing works

Cystatin C-Cathepsin B Axis Regulates Amyloid Beta Levels and Associated Neuronal Deficits in an Animal Model of Alzheimer's Disease

Sun, B., Zhou, Y., Halabisky, B., Lo, I., Cho, S.-H., Mueller-Steiner, S., Devidze, N., Wang, X., Grubb, A., & Gan, L. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.001 · Cited by 231 · see citing works

Human neprilysin is capable of degrading amyloid β peptide not only in the monomeric form but also the pathological oligomeric form

Kanemitsu, H., Tomiyama, T., & Mori, H. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00898-x · Cited by 228 · see citing works

Intracellular Mechanisms of Amyloid Accumulation and Pathogenesis in Alzheimer's Disease

Glabe, C. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:137 · Cited by 222 · see citing works

Statins Promote the Degradation of Extracellular Amyloid β-Peptide by Microglia via Stimulation of Exosome-associated Insulin-degrading Enzyme (IDE) Secretion

Tamboli, I. Y., Barth, E., Christian, L., Siepmann, M., Kumar, S., Singh, S., Tolksdorf, K., Heneka, M. T., Lütjohann, D., Wunderlich, P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149468 · Cited by 219 · see citing works

Neutral endopeptidase can hydrolyze β-amyloid(1–40) but shows no effect on β-amyloid precursor protein metabolism

Howell, S. W., Nalbantoglu, J. N., & Crine, P. (1995) · Peptides · doi:10.1016/0196-9781(95)00021-b · Cited by 204 · see citing works

Degradation of the Amyloid β-Protein by the Novel Mitochondrial Peptidasome, PreP

Falkevall, A., Alikhani, N., Bhushan, S., Pavlov, P. F., Busch, K., Johnson, K. A., Eneqvist, T., Tjernberg, L. O., Ankarcrona, M., & Glaser, E. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602532200 · Cited by 202 · see citing works

Aβ-degrading enzymes: modulators of Alzheimer's disease pathogenesis and targets for therapeutic intervention

Eckman, C. B., & Eckman, E. A. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051101 · Cited by 201 · see citing works

Regulation of Steady-state β-Amyloid Levels in the Brain by Neprilysin and Endothelin-converting Enzyme but Not Angiotensin-converting Enzyme

Eckman, E. A., Adams, S. K., Troendle, F. J., Stodola, B. A., Kahn, M. A., Fauq, A. H., Xiao, H. D., Bernstein, K. E., & Eckman, C. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605827200 · Cited by 196 · see citing works

Neprilysin: An Enzyme Candidate to Slow the Progression of Alzheimer's Disease

El‐Amouri, S. S., Zhu, H., Yu, J., Marr, R. A., Verma, I. M., & Kindy, M. S. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070620 · Cited by 188 · see citing works

Neprilysin-sensitive Synapse-associated Amyloid-β Peptide Oligomers Impair Neuronal Plasticity and Cognitive Function

Huang, S.-M., Mouri, A., Kokubo, H., Nakajima, R., Suemoto, T., Higuchi, M., Staufenbiel, M., Noda, Y., Yamaguchi, H., Nabeshima, T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601372200 · Cited by 179 · see citing works

A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor

Miyazaki, K., Hasegawa, M. L., Funahashi, K., & Umeda, M. (1993) · Nature · doi:10.1038/362839a0 · Cited by 172 · see citing works

An unusual active site identified in a family of zinc metalloendopeptidases.

Becker, A. B., & Roth, R. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.9.3835 · Cited by 168 · see citing works

Increased Production of Matrix Metalloproteinases in Enriched Astrocyte and Mixed Hippocampal Cultures Treated with β‐Amyloid Peptides

Deb, S., & Gottschall, P. E. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66041641.x · Cited by 163 · see citing works

Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria

Leissring, M. A., Farris, W., Wu, X., Christodoulou, D. C., Haigis, M. C., Guarente, L., & Selkoe, D. J. (2004) · Biochemical Journal · doi:10.1042/bj20041081 · Cited by 162 · see citing works

Dutch, Flemish, Italian, and Arctic mutations of APP and resistance of Aβ to physiologically relevant proteolytic degradation

Tsubuki, S., Takai, Y., & Saido, T. C. (2003) · The Lancet · doi:10.1016/s0140-6736(03)13555-6 · Cited by 158 · see citing works

Relationship between β-amyloid degradation and the 26S proteasome in neural cells

Salon, M. L., Pasquini, L. A., Moreno, M. B., Pasquini, J. M., & Soto, E. F. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(02)00060-2 · Cited by 157 · see citing works

Aβ-degrading endopeptidase, neprilysin, in mouse brain: synaptic and axonal localization inversely correlating with Aβ pathology

Fukami, S., Watanabe, K., Iwata, N., Haraoka, J., Lu, B., Gerard, N. P., Gerard, C., Fraser, P., Westaway, D., George-Hyslop, P. S., et al. (2002) · Neuroscience Research · doi:10.1016/s0168-0102(02)00015-9 · Cited by 157 · see citing works

Loss of Neprilysin Function Promotes Amyloid Plaque Formation and Causes Cerebral Amyloid Angiopathy

Farris, W., Schütz, S. G., Cirrito, J. R., Shankar, G. M., Sun, X., George, A., Leissring, M. A., Walsh, D. M., Qiu, W. Q., Holtzman, D. M., et al. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070105 · Cited by 155 · see citing works

Insulin-Degrading Enzyme Sorting in Exosomes: A Secretory Pathway for a Key Brain Amyloid-β Degrading Protease

Bulloj, A., Leal, M. C., Xu, H., Castaño, E. M., & Morelli, L. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1206 · Cited by 149 · see citing works

Enhanced clearance of Aβ in brain by sustaining the plasmin proteolysis cascade

Jacobsen, J. S., Comery, T. A., Martone, R. L., Elokdah, H. M., Crandall, D. L., Oganesian, A., Aschmies, S., Kirksey, Y. M., Gonzales, C., Xu, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710823105 · Cited by 146 · see citing works

Quantitation of amyloid beta-protein (A beta) in the cortex during aging and in Alzheimer's disease.

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BACE overexpression alters the subcellular processing of APP and inhibits Aβ deposition in vivo

Lee, E. B., Zhang, B., Liu, K., Greenbaum, E. A., Doms, R. W., Trojanowski, J. Q., & Lee, V. M.-Y. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200407070 · Cited by 140 · see citing works

Neprilysin Overexpression Inhibits Plaque Formation But Fails to Reduce Pathogenic Aβ Oligomers and Associated Cognitive Deficits in Human Amyloid Precursor Protein Transgenic Mice

Meilandt, W. J., Cissé, M., Ho, K., Wu, T. Z., Esposito, L., Scearce-Levie, K. A., Cheng, I. H.-J., Yu, G.-Q., & Mucke, L. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2984-08.2009 · Cited by 137 · see citing works

Regulation and interactions in the activation of cell-associated plasminogen

My�h�nen, H., & Vaheri, A. I. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4230-9 · Cited by 137 · see citing works

Oxidized neprilysin in aging and Alzheimer’s disease brains

Wang, D.-S., Iwata, N., Hama, E., Saido, T. C., & Dickson, D. W. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.09.003 · Cited by 131 · see citing works

Neprilysin and Amyloid Beta Peptide Degradation

Hersh, L. B., & Rodgers, D. W. (2008) · Current Alzheimer Research · doi:10.2174/156720508783954703 · Cited by 127 · see citing works

Effects of prolonged angiotensin-converting enzyme inhibitor treatment on amyloid beta-protein metabolism in mouse models of Alzheimer disease.

Hemming, M. L., Selkoe, D., & Farris, W. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.01.004 · Cited by 126 · see citing works

Normal Cellular Processing of the β‐Amyloid Precursor Protein Results in the Secretion of the Amyloid β Peptide and Related Moleculesa

Haass, C., Hung, A. Y., Schlossmacher, M. G., Oltersdorf, T., Teplow, D. B., & Selkoe, D. J. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb23037.x · Cited by 123 · see citing works

Protective mechanisms by cystatin C in neurodegenerative diseases

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Reducing Amyloid Plaque Burden via Ex Vivo Gene Delivery of an Aβ-Degrading Protease: A Novel Therapeutic Approach to Alzheimer Disease

Hemming, M. L., Patterson, M., Reske-Nielsen, C., Lin, L., Ole Isacson, A., & Selkoe, D. J. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040262 · Cited by 119 · see citing works

Effect of Apolipoprotein E Allele ε4 on the Initial Phase of Amyloid β-Protein Accumulation in the Human Brain

Morishima-Kawashima, M., Oshima, N., Ogata, H., Yamaguchi, H., Yoshimura, M., Sugihara, S., & Ihara, Y. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64847-x · Cited by 119 · see citing works

Deletion of Insulin-Degrading Enzyme Elicits Antipodal, Age-Dependent Effects on Glucose and Insulin Tolerance

Abdul‐Hay, S. O., Kang, D., McBride, M., Li, L., Zhao, J., & Leissring, M. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020818 · Cited by 113 · see citing works

Tissue Plasminogen Activator Requires Plasminogen to Modulate Amyloid‐β Neurotoxicity and Deposition

Tucker, H. M., Kihiko‐Ehmann, M., Wright, S., Rydel, R. E., & Estus, S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752172.x · Cited by 113 · see citing works

Plasmin Cleavage of the Amyloid β-Protein: Alteration of Secondary Structure and Stimulation of Tissue Plasminogen Activator Activity

Nostrand, W. E. V., & Porter, M. D. (1999) · Biochemistry · doi:10.1021/bi990610f · Cited by 113 · see citing works

Designed Inhibitors of Insulin-Degrading Enzyme Regulate the Catabolism and Activity of Insulin

Leissring, M. A., Malito, E., Hédouin, S., Reinstatler, L. S., Sahara, T., Abdul‐Hay, S. O., Choudhry, S., Maharvi, G. M., Fauq, A. H., Huzarska, M. A., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010504 · Cited by 108 · see citing works

Vascular and metabolic dysfunction in Alzheimer’s disease: a review

Murray, I. V. J., Proza, J. F., Sohrabji, F., & Lawler, J. M. (2011) · Experimental Biology and Medicine · doi:10.1258/ebm.2011.010355 · Cited by 104 · see citing works

Genetics of Alzheimer's Disease. A Rapidly Evolving Field

Serretti, A., Olgiati, P., & Ronchi, D. D. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-12108 · Cited by 103 · see citing works

Metabolism of amyloid β peptide and pathogenesis of Alzheimer's disease

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Purification of protease nexin II from human fibroblasts.

Nostrand, W. E. V., & Cunningham, D. D. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47443-1 · Cited by 100 · see citing works

Neuropeptide Y Fragments Derived from Neprilysin Processing Are Neuroprotective in a Transgenic Model of Alzheimer's Disease

Rose, J. B., Crews, L. A., Rockenstein, E. M., Adame, A., Mante, M., Hersh, L. B., Gage, F. H., Spencer, B. J., Potkar, R., Marr, R. A., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4220-08.2009 · Cited by 94 · see citing works

Susceptibility of Amyloid β Peptide Degrading Enzymes to Oxidative Damage: A Potential Alzheimer's Disease Spiral

Shinall, H., Song, E. S., & Hersh, L. B. (2005) · Biochemistry · doi:10.1021/bi050650l · Cited by 94 · see citing works

Cathepsin D is involved in the clearance of Alzheimer's β‐amyloid protein

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Degradation of Soluble and Fibrillar Amyloid β-Protein by Matrix Metalloproteinase (MT1-MMP) in-Vitro

Liao, M.-C., & Nostrand, W. V. V. (2010) · Biochemistry · doi:10.1021/bi901994d · Cited by 91 · see citing works

Insulin-degrading enzyme is exported via an unconventional protein secretion pathway

Zhao, J., Li, L., & Leissring, M. A. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-4 · Cited by 90 · see citing works

Alternative Splicing of Human Insulin-Degrading Enzyme Yields a Novel Isoform with a Decreased Ability To Degrade Insulin and Amyloid β-Protein

Farris, W., Leissring, M. A., Hemming, M. L., Chang, A. Y., & Selkoe, D. J. (2005) · Biochemistry · doi:10.1021/bi0476578 · Cited by 87 · see citing works

Aggregation and catabolism of disease-associated intra-Aβ mutations: reduced proteolysis of AβA21G by neprilysin

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The AβCs of Aβ-cleaving Proteases

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Degradation of Intraendosomal Insulin by Insulin-Degrading Enzyme Without Acidification

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