Amyloid β-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin
Open accessAbstract
The accumulation of aggregates of amyloidogenic peptides is associated with numerous human diseases. One well studied example is the association between deposition of amyloid beta (Abeta) and Alzheimer's disease. Insulin degrading enzyme and neprilysin are involved in the clearance of Abeta, and presequence peptidase is suggested to play a role in the degradation of mitochondrial Abeta. Recent structural analyses reveal that these three peptidases contain a catalytic chamber (crypt) that selectively encapsulates and cleaves amyloidogenic peptides, hence the name cryptidase. The substrate selectivity of these cryptidases is determined by the size and charge distribution of their crypt as well as the conformational flexibility of substrates. The interaction of Abeta with the catalytic core of these cryptidases is controlled by conformational changes that make the catalytic chambers accessible for Abeta binding. These new structural and biochemical insights into cryptidases provide potential therapeutic strategies for the control of Abeta clearance.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
IDE degrades Aβ.
“The decreased plaque deposition was also related to increased levels of the proteolytic enzyme insulin-degrading enzyme (IDE) [77], previously reported to degrade Aβ [83].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [83]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147 · see citing works
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160 · see citing works
A genome-wide association study identifies novel risk loci for type 2 diabetes
Sladek, R., Rocheleau, G., Rung, J., Dina, C., Shen, L., Serre, D., Boutin, P., Vincent, D., Belisle, A., Hadjadj, S., et al. (2007) · Nature · doi:10.1038/nature05616 · Cited by 2,993 · see citing works
Handbook of Proteolytic Enzymes
(2004) · Elsevier eBooks · doi:10.1016/c2009-0-03628-9 · Cited by 2,627 · see citing works
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 · see citing works
Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,488 · see citing works
Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431 · see citing works
Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: a case report
Nicoll, J. A. R., Wilkinson, D., Holmes, C., Steart, P., Markham, H., & Weller, R. O. (2003) · Nature Medicine · doi:10.1038/nm840 · Cited by 1,397 · see citing works
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
THE UBIQUITIN 26S PROTEASOME PROTEOLYTIC PATHWAY
Smalle, J., & Vierstra, R. D. (2004) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.55.031903.141801 · Cited by 1,350 · see citing works
Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer’s disease
Meyer-Luehmann, M., Spires-Jones, T. L., Prada, C., Garcia-Alloza, M., de Calignon, A., Rozkalne, A., Koenigsknecht-Talboo, J., Holtzman, D. M., Bacskai, B. J., & Hyman, B. T. (2008) · Nature · doi:10.1038/nature06616 · Cited by 987 · see citing works
Detection, delineation, measurement and display of cavities in macromolecular structures
Kleywegt, G. J., & Jones, T. A. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444993011333 · Cited by 972 · 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
Insulin Degradation: Progress and Potential
Duckworth, W. C., Bennett, R. G., & Hamel, F. G. (1998) · Endocrine Reviews · doi:10.1210/edrv.19.5.0349 · Cited by 875 · see citing works
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
Families of zinc metalloproteases
Hooper, N. M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01079-x · Cited by 790 · 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
Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738 · see citing works
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
Clausen, T., Southan, C., & Ehrmann, M. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00658-5 · Cited by 640 · 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
DeMattos, R. B., Bales, K. R., Cummins, D. J., Paul, S. M., & Holtzman, D. M. (2002) · Science · doi:10.1126/science.1067568 · Cited by 563 · see citing works
Qiu, W. Q., & Folstein, M. F. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.01.004 · Cited by 538 · see citing works
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
Yanagisawa, H., Yanagisawa, M., Kapur, R. P., Richardson, J. A., Williams, S. C., Clouthier, D. E., de Wit, D., Emoto, N., & Hammer, R. E. (1998) · Development · doi:10.1242/dev.125.5.825 · Cited by 490 · see citing works
Bacskai, B. J., Kajdasz, S. T., Christie, R. H., Carter, C., Games, D., Seubert, P. A., Schenk, D., & Hyman, B. T. (2001) · Nature Medicine · doi:10.1038/85525 · Cited by 445 · see citing works
Kurochkin, I. V., & Goto, S. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00387-4 · Cited by 401 · 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
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
Self-citationYoung-Pearse, T. L., Bai, J., Chang, R., Zheng, J. B., LoTurco, J. J., & Selkoe, D. J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4701-07.2007 · Cited by 369 · see citing works
Yasojima, K., Akiyama, H., McGeer, E. G., & McGeer, P. L. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01675-x · Cited by 357 · see citing works
Non-Fc-Mediated Mechanisms Are Involved in Clearance of Amyloid-β<i>In Vivo</i>by Immunotherapy
Bacskai, B. J., Kajdasz, S. T., McLellan, M. E., Games, D., Seubert, P., Schenk, D., & Hyman, B. T. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-18-07873.2002 · Cited by 323 · see citing works
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
Miller, B. C., Eckman, E. A., Sambamurti, K., Dobbs, N., Chow, K. M., Eckman, C. B., Hersh, L. B., & Thiele, D. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031520100 · Cited by 294 · see citing works
Physiological roles for amyloid β peptides
Pearson, H. A., & Peers, C. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.111203 · Cited by 286 · see citing works
Oefner, C., D'Arcy, A., Hennig, M., Winkler, F. K., & Dale, G. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3492 · Cited by 282 · see citing works
Farris, W., Mansourian, S., Leissring, M. A., Eckman, E. A., Bertram, L., Eckman, C. B., Tanzi, R. E., & Selkoe, D. J. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63229-4 · Cited by 269 · see citing works
Insulin increases CSF Aβ42 levels in normal older adults
Watson, G. S., Peskind, E. R., Asthana, S., Purganan, K., Wait, C., Chapman, D., Schwartz, M. W., Plymate, S. R., & Craft, S. (2003) · Neurology · doi:10.1212/01.wnl.0000065916.25128.25 · Cited by 265 · 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
Structure of insulin in 4-zinc insulin
Bentley, G. A., Dodson, E. J., Dodson, G. G., Hodgkin, D. C., & Mercola, D. (1976) · Nature · doi:10.1038/261166a0 · Cited by 256 · see citing works
Taylor, A. B., Smith, B. S., Kitada, S., Kojima, K., Miyaura, H., Otwinowski, Z., Ito, A., & Deisenhofer, J. (2001) · Structure · doi:10.1016/s0969-2126(01)00621-9 · Cited by 246 · see citing works
Yasojima, K., McGeer, E. G., & McGeer, P. L. (2001) · Brain Research · doi:10.1016/s0006-8993(01)03008-6 · Cited by 224 · 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
Electrostatic steering and ionic tethering in enzyme–ligand binding: Insights from simulations
Wade, R. C., Gabdoulline, R. R., Lüdemann, S. K., & Lounnas, V. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5942 · Cited by 200 · see citing works
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
Insulin-degrading enzyme: embarking on amyloid destruction
Kurochkin, I. V. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01876-x · Cited by 178 · see citing works
Structure and Function of HtrA Family Proteins, the Key Players in Protein Quality Control
Kim, D. Y., & Kim, K.-K. (2005) · BMB Reports · doi:10.5483/bmbrep.2005.38.3.266 · Cited by 171 · see citing works
Degradation of Amylin by Insulin-degrading Enzyme
Bennett, R. G., Duckworth, W. C., & Hamel, F. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006170200 · Cited by 170 · see citing works
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
Li, Q., Ali, M. A., & Cohen, J. I. (2006) · Cell · doi:10.1016/j.cell.2006.08.046 · Cited by 154 · see citing works
Human Insulin-Degrading Enzyme Shares Structural and Functional Homologies with E. coli Protease III
Affholter, J. A., Fried, V. A., & Roth, R. A. (1988) · Science · doi:10.1126/science.3059494 · Cited by 148 · see citing works
Cooke, R. M., Harvey, T. S., & Campbell, I. D. (1991) · Biochemistry · doi:10.1021/bi00236a022 · Cited by 143 · see citing works
Ståhl, A.-L., Moberg, P., Ytterberg, J., Panfilov, O., von Löwenhielm, H. B., Nilsson, F. Y., & Glaser, E. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205500200 · Cited by 135 · see citing works
Moberg, P., Ståhl, A.-L., Bhushan, S., Wright, S. J., Eriksson, A., Bruce, B. D., & Glaser, E. G. (2003) · The Plant Journal · doi:10.1046/j.1365-313x.2003.01904.x · Cited by 122 · see citing works
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
The closed structure of presequence protease PreP forms a unique 10 000 Å3 chamber for proteolysis
Johnson, K. A., Bhushan, S., Ståhl, A.-L., Hällberg, B. M., Frohn, A., Glaser, E. G., & Eneqvist, T. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601080 · Cited by 104 · see citing works
Neprylisin decreases uniformly in Alzheimer's disease and in normal aging
Russo, R., Borghi, R., Markesbery, W. R., Tabaton, M., & Piccini, A. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.09.054 · Cited by 87 · see citing works
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
Anti-amyloidogenic therapies: strategies for prevention and treatment of Alzheimer’s disease
Hamaguchi, T., Ono, K., & Yamada, M. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5599-9 · Cited by 82 · see citing works
Structural analysis of neprilysin with various specific and potent inhibitors
Oefner, C., Roques, B. P., Fournie-Zaluski, M.-C., & Dale, G. E. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444903027410 · Cited by 81 · see citing works
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 · see citing works
Ståhl, A.-L., Nilsson, S., Lundberg, P., Bhushan, S., Biverstål, H., Moberg, P., Morisset, M., Vener, A. V., Mäler, L., Langel, Ü., et al. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.04.023 · Cited by 78 · see citing works
Structural Determinants of Natriuretic Peptide Receptor Specificity and Degeneracy
He, X. L., Dukkipati, A., & García, K. C. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.060 · Cited by 76 · see citing works
Mueller, D., Schulze, C., Baumeister, H., Buck, F., & Richter, D. (1992) · Biochemistry · doi:10.1021/bi00160a026 · Cited by 74 · see citing works
Sudoh, S., Frosch, M. P., & Wolf, B. A. (2002) · Biochemistry · doi:10.1021/bi011193l · Cited by 73 · see citing works
Atrial natriuretic peptide (ANP) is a high‐affinity substrate for rat insulin‐degrading enzyme
Müller, D., Baumeister, H., Buck, F., & Richter, D. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16374.x · Cited by 72 · see citing works
New Insights into the Roles of Metalloproteinases in Neurodegeneration and Neuroprotection
Turner, A. J., & Nalivaeva, N. N. (2007) · International review of neurobiology · doi:10.1016/s0074-7742(07)82006-x · Cited by 70 · see citing works
Mohajeri, M. H., Wollmer, M. A., & Nitsch, R. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202899200 · Cited by 66 · see citing works
Torres, A. M., Forbes, B. E., Aplin, S. E., Wallace, J. C., Francise, G. L., & Norton, R. S. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(95)80058-1 · Cited by 65 · see citing works
Broh-Kahn, R. H., & MIRSKY, I. A. (1949) · PubMed · Cited by 58 · see citing works
Characterization of Endothelin-converting Enzyme-2
Mzhavia, N., Pan, H., Che, F., Fricker, L. D., & Devi, L. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211242200 · Cited by 55 · see citing works
Li, P., Kuo, W., Yousef, M., Rosner, M. R., & Tang, W. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.083 · Cited by 54 · see citing works
Self-citationSpecificity of mechanisms for plaque removal after Aβ immunotherapy for Alzheimer disease
Akiyama, H., & McGeer, P. L. (2004) · Nature Medicine · doi:10.1038/nm0204-117 · Cited by 51 · see citing works
Degradation Of Insulin-Like Growth Factors I And II By A Human Insulin Degrading Enzyme
Roth, R. A., Mesirow, M. L., Yokono, K., & Baba, S. (1984) · Endocrine Research · doi:10.3109/07435808409035411 · Cited by 51 · see citing works
Emoto, N., Nurhantari, Y., Alimsardjono, H., Xie, J., Yamada, T., Yanagisawa, M., & Matsuo, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1509 · Cited by 50 · see citing works
Functional Human Insulin-Degrading Enzyme Can Be Expressed in Bacteria
Chesneau, V., & Rosner, M. R. (2000) · Protein Expression and Purification · doi:10.1006/prep.2000.1217 · Cited by 47 · see citing works
Mentlein, R., Ludwig, R., & Martensen, I. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70020721.x · Cited by 45 · see citing works
Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV
Oefner, C., Pierau, S., Schulz, H., & Dale, G. E. (2007) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444907036281 · Cited by 43 · see citing works
Terawaki, S., Kitano, K., & Hakoshima, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609232200 · Cited by 42 · see citing works
Hartmann‐Petersen, R., & Gordon, C. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4132-x · Cited by 39 · see citing works
Iwase, A., Shen, R., Navarro, D., & Nanus, D. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m212737200 · Cited by 39 · see citing works
INHIBITION OF INSULIN DEGRADATION BY INSULIN-LIKE GROWTH FACTORS
Misbin, R. I., Almira, E. C., Duckworth, W. C., & Mehl, T. D. (1983) · Endocrinology · doi:10.1210/endo-113-4-1525 · Cited by 36 · see citing works
Misbin, R. I., & Almira, E. C. (1989) · Diabetes · doi:10.2337/diab.38.2.152 · Cited by 33 · see citing works
Bur, D., Dale, G. E., & Oefner, C. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.5.337 · Cited by 29 · see citing works
Leissring, M. A., & Selkoe, D. J. (2006) · Nature · doi:10.1038/nature05210 · Cited by 25 · see citing works
solution Conformation of an Atrial Natriuretic Peptide Variant Selective for the Type A Receptor
Fairbrother, W. J., McDowell, R. S., & Cunningham, B. C. (1994) · Biochemistry · doi:10.1021/bi00196a006 · Cited by 23 · see citing works
Effect of 'Insulinase-Inhibitor' on Destruction of Insulin by Intact Mouse.
Mirsky, I. A., Perisutti, G., & DIENGOTT, D. (1955) · Experimental Biology and Medicine · doi:10.3181/00379727-88-21497 · Cited by 13 · see citing works
Flagged first, then by citations
Research works printed but not linked: 15
- [1]Puente XS Sanchez LM Overall CM Lopez-Otin C 2003 Human and mouse proteases: a comparative genomic approach Nat Rev Genet 4 544 58 12838346
- [3]Im H Manolopoulou M Malito E Shen Y Zhao J Neant-Fery M Sun CY Meredith SC Sisodia SS Leissring MA Tang WJ 2007 Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE J Biol Chem 282 25453 63 17613531
- [5]Oefner C D'Arcy A Hennig M Winkler FK Dale GE 2000 Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon J Mol Biol 296 341 9 10669592
- [9]Hartmann-Petersen R Gordon C 2004 Proteins interacting with the 26S proteasome Cell Mol Life Sci 61 1589 95 15224183 PMC11138787
- [21]Tanzi RE Moir RD Wagner SL 2004 Clearance of Alzheimer's Abeta peptide: the many roads to perdition Neuron 43 605 8 15339642
- [26]Rawlings ND Morton FR Barrett AJ 2006 MEROPS: the peptidase database Nucleic Acids Res 34 D270 2 16381862 PMC1347452
- [31]Selkoe DJ 2001 Clearing the brain's amyloid cobwebs Neuron 32 177 80 11683988
- [41]Taubes G 2003 Neuroscience. Insulin insults may spur Alzheimer's disease Science 301 40 1 12843374
- [43]Maskos K Messerschmidt A Dode W Cygler M 2004 Handbook of metalloproteins John Wiley &Sons 3 190 198
- [47]Mzhavia N Berman YL Qian Y Yan L Devi LA 1999 Cloning, expression, and characterization of human metalloprotease 1: a novel member of the pitrilysin family of metalloendoproteases DNA Cell Biol 18 369 80 10360838
- [49]Lustbader JW Cirilli M Lin C Xu HW Takuma K Wang N Caspersen C Chen X Pollak S Chaney M Trinchese F Liu S Gunn-Moore F Lue LF Walker DG Kuppusamy P Zewier ZL Arancio O Stern D Yan SS Wu H 2004 ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease Science 304 448 52 15087549
- [53]Turner AJ Tanzawa K 1997 Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX Faseb J 11 355 64 9141502
- [55]Eckman EA Reed DK Eckman CB 2001 Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme J Biol Chem 276 24540 8 11337485
- [57]Iwata N Takaki Y Fukami S Tsubuki S Saido TC 2002 Region-specific reduction of A beta-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging J Neurosci Res 70 493 500 12391610
- [94]Sticht H Bayer P Willbold D Dames S Hilbich C Beyreuther K Frank RW Rosch P 1995 Structure of amyloid A4-(1–40)-peptide of Alzheimer's disease Eur J Biochem 233 293 8 7588758
Cited by
Sorted by citations
NLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice
Heneka, M. T., Kummer, M. P., Stutz, A., Delekate, A., Schwartz, S., Vieira-Saecker, A., Griep, A., Axt, D., Remus, A., Tzeng, T.-C., et al. (2013) · Nature · doi:10.1038/nature11729 · Cited by 2,898 · see citing works
<p>Alzheimer’s disease: pathogenesis, diagnostics, and therapeutics</p>
Tiwari, S., Atluri, V., Kaushik, A., Yndart, A., & Nair, M. (2019) · International Journal of Nanomedicine · doi:10.2147/ijn.s200490 · Cited by 1,308 · see citing works
The role of microglia in amyloid clearance from the AD brain
Lee, C. Y. D., & Landreth, G. E. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0433-4 · Cited by 701 · see citing works
Is Alzheimer’s disease a type 3 diabetes? A critical appraisal
Kandimalla, R., Thirumala, V., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.018 · Cited by 621 · see citing works
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 · see citing works
IL-33 ameliorates Alzheimer's disease-like pathology and cognitive decline
Fu, A. K. Y., Hung, K.-W., Yuen, M. Y. F., Zhou, X., Mak, D. S. Y., Chan, I. C. W., Cheung, T. H., Zhang, B., Fu, W.-Y., Liew, F. Y., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604032113 · Cited by 369 · see citing works
Natriuretic peptide metabolism, clearance and degradation
Potter, L. R. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08082.x · Cited by 359 · see citing works
Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease
Baranello, R., Bharani, K., Padmaraju, V., Chopra, N., Lahiri, D., Greig, N., Pappolla, M., & Sambamurti, K. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666141218140953 · Cited by 331 · see citing works
Ding, M., Shen, Y., Wang, P., Xie, Z., Xu, S., Zhu, Z., Wang, Y., Lyu, Y., Dewei, W., Xu, L., et al. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2641-5 · Cited by 279 · see citing works
Anti-diabetic activity of insulin-degrading enzyme inhibitors mediated by multiple hormones
Maianti, J. P., McFedries, A., Foda, Z. H., Kleiner, R. E., Du, X. Q., Leissring, M. A., Tang, W., Charron, M. J., Seeliger, M. A., Saghatelian, A., et al. (2014) · Nature · doi:10.1038/nature13297 · Cited by 251 · see citing works
Self-citationHuang, J.-Y., Hirschey, M. D., Shimazu, T., Ho, L., & Verdin, E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.021 · Cited by 231 · see citing works
Peroxisomes in brain development and function
Berger, J., Dorninger, F., Forss-Petter, S., & Kunze, M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.12.005 · Cited by 194 · see citing works
Are amyloid‐degrading enzymes viable therapeutic targets in Alzheimer’s disease?
Nalivaeva, N., Beckett, C. S., Belyaev, N. D., & Turner, A. J. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07510.x · Cited by 178 · see citing works
Pathological role of hypoxia in Alzheimer's disease
Zhang, X., & Le, W. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.07.033 · Cited by 189 · see citing works
Insulin-Degrading Enzyme in the Fight against Alzheimer's Disease
Kurochkin, I. V., Guarnera, E., & Berezovsky, I. N. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.10.008 · Cited by 185 · see citing works
Toward a comprehensive neurobiology of IGF‐I
Torres‐Alemán, I. (2010) · Developmental Neurobiology · doi:10.1002/dneu.20778 · Cited by 177 · see citing works
Yang, H., Xie, Z., Wei, L. F., Yang, H. N., Yang, S. N., Zhu, Z., Wang, P., Zhao, C., & Bi, J. Z. (2013) · Stem Cell Research & Therapy · doi:10.1186/scrt227 · Cited by 166 · see citing works
Zhang, Z., Liang, W. G., Bailey, L. J., Tan, Y. Z., Wei, H., Wang, A., Farcasanu, M., Woods, V. A., McCord, L. A., Lee, D. E., et al. (2018) · eLife · doi:10.7554/elife.33572 · Cited by 148 · see citing works
Self-citationCosta, A. R., Ferreira‐da‐Silva, F., Saraiva, M. J., & Cardoso, I. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002899 · Cited by 126 · see citing works
Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus
Tang, W. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.11.003 · Cited by 120 · see citing works
Self-citationTzeng, T.-T., Chen, C., Lee, L., Wan-Ping, C., Chung-Kuang, L., Shen, C., Chi-Ying, H. F., Chien-Chih, C., & Shiao, Y. (2016) · Journal of Biomedical Science · doi:10.1186/s12929-016-0266-z · Cited by 122 · see citing works
Stargardt, A., Swaab, D. F., & Bossers, K. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.08.014 · Cited by 109 · 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
Self-citationManolopoulou, M., Guo, Q., Malito, E., Schilling, A. B., & Tang, W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900068200 · Cited by 108 · see citing works
Self-citationFeng, J., Wang, J., Du, Y., Liu, Y., Zhang, W., Chen, J., Liu, Y., Zheng, M., Wang, K., & He, G. (2018) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12983 · Cited by 108 · see citing works
Deprez-Poulain, R. F., Hennuyer, N., Bosc, D., Liang, W. G., Waeckel-Énée, E., Marechal, X., Charton, J., Totobenazara, J., Berte, G., Jahklal, J., et al. (2015) · Nature Communications · doi:10.1038/ncomms9250 · Cited by 97 · see citing works
Self-citationTerzioglu, G., & Young-Pearse, T. L. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00674-9 · Cited by 95 · see citing works
Inflammasome-mediated innate immunity in Alzheimer’s disease
Venegas, C., & Heneka, M. T. (2019) · The FASEB Journal · doi:10.1096/fj.201900439 · Cited by 93 · 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
Guo, Q., Manolopoulou, M., Bian, Y., Schilling, A. B., & Tang, W. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.10.072 · Cited by 87 · see citing works
Self-citationJha, N. K., Jha, S. K., Kumar, D., Kejriwal, N., Sharma, R., Ambasta, R. K., & Kumar, P. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150379 · Cited by 88 · see citing works
Malito, E., Ralat, L. A., Manolopoulou, M., Tsay, J. L., Wadlington, N. L., & Tang, W. (2008) · Biochemistry · doi:10.1021/bi801192h · Cited by 84 · see citing works
Self-citationInsulin-degrading Enzyme Modulates the Natriuretic Peptide-mediated Signaling Response
Ralat, L. A., Guo, Q., Ren, M., Funke, T., Dickey, D. M., Potter, L. R., & Tang, W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173252 · Cited by 78 · see citing works
Self-citationCabrol, C., Huzarska, M. A., Dinolfo, C., Rodríguez, M. C., Reinstatler, L. S., Ni, J., Yeh, L.-A., Cuny, G. D., Stein, R. L., Selkoe, D. J., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005274 · Cited by 77 · see citing works
Yokoyama, H., Okazaki, K., Imai, D., Yamashina, Y., Takeda, R., Naghavi, N., Ota, A., Hirasawa, Y., & Miyagawa, T. (2015) · BMC Geriatrics · doi:10.1186/s12877-015-0058-4 · Cited by 76 · see citing works
He, P., Cheng, X., Staufenbiel, M., Li, R.-N., & Shen, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055091 · Cited by 69 · see citing works
Webster, C. I., Burrell, M. R., Olsson, L., Fowler, S. A., Digby, S., Sandercock, A. M., Snijder, A., Tebbe, J., Haupts, U. M., Grudzinska, J., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104001 · Cited by 73 · see citing works
Grasso, G., Pietropaolo, A., Spoto, G., Pappalardo, G., Tundo, G. R., Ciaccio, C., Coletta, M., & Rizzarelli, E. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201002809 · Cited by 72 · see citing works
Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme
McCord, L. A., Liang, W. G., Dowdell, E., Kalas, V., Hoey, R. J., Koide, A., Koide, S., & Tang, W. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1304575110 · Cited by 73 · see citing works
Self-citationProtease Regulation: The Yin and Yang of Neural Development and Disease
Bai, G., & Pfaff, S. L. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.012 · Cited by 70 · see citing works
Amyloid-β Peptide Is a Substrate of the Human 20S Proteasome
Zhao, X., & Yang, J. (2010) · ACS Chemical Neuroscience · doi:10.1021/cn100067e · Cited by 68 · see citing works
Chapter 22 Structure, Function, and Regulation of Insulin‐Degrading Enzyme
Hulse, R. E., Ralat, L. A., & Wei‐Jen, T. (2009) · Vitamins and hormones · doi:10.1016/s0083-6729(08)00622-5 · Cited by 69 · see citing works
Self-citationRedox-Active Metal Ions and Amyloid-Degrading Enzymes in Alzheimer’s Disease
Kim, N., & Lee, H. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147697 · Cited by 67 · see citing works
Insulin signaling: An opportunistic target to minify the risk of Alzheimer’s disease
Pardeshi, R., Bolshette, N. B., Gadhave, K., Ahire, A., Ahmed, S., Cassano, T., Gupta, V. B., & Lahkar, M. (2017) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2017.05.004 · Cited by 65 · see citing works
Insulin‐degrading enzyme: an ally against metabolic and neurodegenerative diseases
Sousa, L., Guarda, M., Meneses, M. J., Macedo, M. P., & Miranda, H. V. (2021) · The Journal of Pathology · doi:10.1002/path.5777 · Cited by 63 · see citing works
Molecular Basis of Substrate Recognition and Degradation by Human Presequence Protease
King, J. V. L., Liang, W. G., Scherpelz, K. P., Schilling, A. B., Meredith, S. C., & Tang, W. (2014) · Structure · doi:10.1016/j.str.2014.05.003 · Cited by 60 · see citing works
Self-citationSubstrate-selective inhibitors that reprogram the activity of insulin-degrading enzyme
Maianti, J. P., Tan, G. A., Vetere, A., Welsh, A. J., Wagner, B. K., Seeliger, M. A., & Liu, D. R. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0271-0 · Cited by 58 · see citing works
Durham, T. B., Toth, J. L., Klimkowski, V. J., Cao, J. X. C., Siesky, A. M., Alexander-Chacko, J. T., Wu, G. Y., Dixon, J. T., McGee, J. E., Wang, Y., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.638205 · Cited by 51 · see citing works
Chen, L., Wu, X., & Chen, X. D. (2013) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2013.02.003 · Cited by 50 · see citing works
Gupta, S. N., Yadav, K., Mantri, S. S., Singhal, N. K., Ganesh, S., & Sandhir, R. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0985-0 · Cited by 46 · see citing works
Sim, A. Y., Choi, D. H., Kim, J. Y., Kim, E. R., Goh, A. R., Lee, Y., & Lee, J. E. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115755 · Cited by 46 · see citing works
Roles of humanin and derivatives on the pathology of neurodegenerative diseases and cognition
Thiankhaw, K., Chattipakorn, K., Chattipakorn, S. C., & Chattipakorn, N. (2022) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2022.130097 · Cited by 43 · see citing works
DNA-encoded chemical libraries of macrocycles
Connors, W. H., Hale, S. P., & Terrett, N. K. (2015) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2015.02.004 · Cited by 41 · see citing works
Ubiquitin Is a Novel Substrate for Human Insulin-Degrading Enzyme
Ralat, L. A., Kalas, V., Zheng, Z., Goldman, R. D., Sosnick, T. R., & Tang, W. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.12.026 · Cited by 40 · see citing works
Self-citationMetallostasis and amyloid β-degrading enzymes
Grasso, G., Giuffrida, M. L., & Rizzarelli, E. (2012) · Metallomics · doi:10.1039/c2mt20105d · Cited by 40 · see citing works
Zraika, S., Aston-Mourney, K., Marek, P., Hull, R., Green, P., Udayasankar, J., Subramanian, S. L., Raleigh, D., & Kahn, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082032 · Cited by 39 · see citing works
Kaminari, A., Tsilibary, E. C., & Tzinia, A. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-180035 · Cited by 30 · see citing works
Crystal and Solution Structures of a Prokaryotic M16B Peptidase: an Open and Shut Case
Aleshin, A. E., Gramatikova, S. I., Hura, G. L., Bobkov, A. A., Strongin, A. Y., Stec, B., Tainer, J. A., Liddington, R., & Smith, J. W. (2009) · Structure · doi:10.1016/j.str.2009.09.009 · Cited by 38 · see citing works
Ralat, L. A., Ren, M., Schilling, A. B., & Tang, W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.030627 · Cited by 38 · see citing works
Self-citationKochkina, E. G., Plesneva, S. A., Vasilev, D. S., Zhuravin, I. A., Turner, A. J., & Nalivaeva, N. N. (2015) · Biogerontology · doi:10.1007/s10522-015-9569-9 · Cited by 37 · see citing works
Çakır, B., Dağliyan, O., Dağyildiz, E., Barış, İ., Kavaklı, İ. H., Kızılel, S., & Türkay, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031787 · Cited by 37 · see citing works
Charton, J., Gauriot, M., Guo, Q., Hennuyer, N., Marechal, X., Dumont, J., Hamdane, M., Pottiez, V., Landry, V., Spérandio, O., et al. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.04.009 · Cited by 36 · see citing works
Self-citationGlycan Mimetics from Natural Products: New Therapeutic Opportunities for Neurodegenerative Disease
Wang, W., Gopal, S., Pocock, R., & Xiao, Z. (2019) · Molecules · doi:10.3390/molecules24244604 · Cited by 35 · see citing works
Gough, M., Parr-Sturgess, C. A., & Parkin, E. T. (2010) · Biochemistry Research International · doi:10.1155/2011/721463 · Cited by 34 · see citing works
Huang, L., Liu, X., Cheng, B., & Huang, K. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.01.007 · Cited by 34 · see citing works
The Origins of Specificity in the Microcin-Processing Protease TldD/E
Ghilarov, D., Serebryakova, M. V., Stevenson, C. E. M., Hearnshaw, S. J., Volkov, D. S., Maxwell, A., Lawson, D. M., & Severinov, K. (2017) · Structure · doi:10.1016/j.str.2017.08.006 · Cited by 34 · see citing works
The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme
de Tullio, M. B., Morelli, L., & Castaño, E. M. (2008) · Prion · doi:10.4161/pri.2.2.6710 · Cited by 34 · see citing works
Malgieri, G., & Grasso, G. (2013) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2013.10.008 · Cited by 33 · see citing works
Zhang, X., Liao, Z., Wu, P., Chen, L., & Chen, X. D. (2018) · Food Research International · doi:10.1016/j.foodres.2017.12.082 · Cited by 32 · see citing works
Zeng, H., Li, P., Zhou, L., & Ding, K. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.05.212 · Cited by 32 · see citing works
Shi, X., Zhang, H., Zhou, Z., Ruan, Y., Pang, J., Zhang, L., Zhai, W., & Hu, Y. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.12.099 · Cited by 31 · see citing works
Intracellular FRET-based Screen for Redesigning the Specificity of Secreted Proteases
Guerrero, J. L., O'Malley, M. A., & Daugherty, P. S. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b01051 · Cited by 29 · see citing works
Kim, J. M., Lee, U., Kang, J. Y., Park, S. K., Shin, E. J., Kim, H., Kim, C. W., Kim, M.-J., & Heo, H. J. (2020) · Antioxidants · doi:10.3390/antiox9100976 · Cited by 30 · see citing works
Hu, Z.-Y., Liu, G., Cheng, X., Huang, Y. Y., Yang, S., Shan-yi, Q., Sun, L., Zhou, W., & Zhang, Y. (2011) · Experimental Gerontology · doi:10.1016/j.exger.2011.09.009 · Cited by 30 · see citing works
Impaired brain plasticity as a potential therapeutic target for treatment and prevention of dementia
Rajji, T. K. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2019.1550074 · Cited by 29 · see citing works
Charton, J., Gauriot, M., Totobenazara, J., Hennuyer, N., Dumont, J., Bosc, D., Marechal, X., Bakali, J. E., Herlédan, A., Wen, X., et al. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.12.005 · Cited by 29 · see citing works
Self-citationLeal, N. S., Dentoni, G., Schreiner, B., Kämäräinen, O., Partanen, N., Herukka, S., Koivisto, A. M., Hiltunen, M., Rauramaa, T. H., Leinonen, V., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0605-2 · Cited by 29 · see citing works
Liu, M., Guo, H., Li, C., Wang, D., Wu, J., Wang, C., Xu, J., & Ren-an, Q. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-015-0906-y · Cited by 28 · see citing works
Nitric Oxide Decreases the Enzymatic Activity of Insulin Degrading Enzyme in APP/PS1 Mice
Kummer, M. P., Hülsmann, C., Hermes, M., Axt, D., & Heneka, M. T. (2012) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-011-9339-7 · Cited by 26 · see citing works
Liang, W. G., Ren, M., Zhao, F., & Tang, W. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.01.012 · Cited by 26 · see citing works
Self-citationHigh resolution crystal structure of substrate-free human neprilysin
Moss, S., Subramanian, V., & Acharya, K. R. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.06.004 · Cited by 25 · see citing works
Insulin-Degrading Enzyme: Paradoxes and Possibilities
Leissring, M. A. (2021) · Cells · doi:10.3390/cells10092445 · Cited by 25 · see citing works
Guan, C., Dang, R., Cui, Y., Liu, L., Chen, X., Wang, X., Zhu, J., Li, D., Li, J., & Wang, D. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178271 · Cited by 26 · see citing works
Hu, Q., Jayasinghe‐Arachchige, V. M., Sharma, G., Serafim, L. F., Paul, T. J., & Prabhakar, R. S. (2020) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1466 · Cited by 25 · see citing works
The solution of nitrogen inversion in amidases
Syrén, P. (2013) · FEBS Journal · doi:10.1111/febs.12241 · Cited by 23 · see citing works
Azam, M. S., Wahiduzzaman, M., Reyad‐ul‐Ferdous, M., Islam, M. N., & Roy, M. (2022) · Pharmaceutical Research · doi:10.1007/s11095-022-03237-7 · Cited by 23 · see citing works
Crystal structure of peptide‐bound neprilysin reveals key binding interactions
Moss, S., Subramanian, V., & Acharya, K. R. (2019) · FEBS Letters · doi:10.1002/1873-3468.13602 · Cited by 22 · see citing works
Target Enzymes Considered for the Treatment of Alzheimer’s Disease and Parkinson’s Disease
Kim, N., & Lee, H. J. (2020) · BioMed Research International · doi:10.1155/2020/2010728 · Cited by 21 · see citing works
Epigenetic modifications of chronic hypoxia-mediated neurodegeneration in Alzheimer’s disease
Liu, H., & Le, W. (2014) · Translational Neurodegeneration · doi:10.1186/2047-9158-3-7 · Cited by 21 · see citing works
Liang, W. G., Wijaya, J., Wei, H., Noble, A. J., Mancl, J. M., Mo, S., Lee, D. E., King, J. V. L., Pan, M., Liu, C., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29322-4 · Cited by 21 · see citing works
Self-citationDistinct chemical factors in hydrolytic reactions catalyzed by metalloenzymes and metal complexes
Serafim, L. F., Jayasinghe‐Arachchige, V. M., Wang, L., Rathee, P., Yang, J., Moorkkannur, S. N., & Prabhakar, R. S. (2023) · Chemical Communications · doi:10.1039/d3cc01380d · Cited by 20 · see citing works
Tundo, G. R., Grasso, G., Persico, M., Tkachuk, O., Bellia, F., Bocedi, A., Marini, S., Parravano, M., Graziani, G., Fattorusso, C., et al. (2023) · Biomolecules · doi:10.3390/biom13101492 · Cited by 20 · see citing works
Structural changes in intermediate filament networks alter the activity of insulin‐degrading enzyme
Chou, Y.-H., Kuo, W.-L., Rosner, M. R., Tang, W., & Goldman, R. D. (2009) · The FASEB Journal · doi:10.1096/fj.09-137455 · Cited by 20 · see citing works
Self-citationShropshire, T. D., Reifert, J. R., Rajagopalan, S., Baker, D. A., Feinstein, S. C., & Daugherty, P. S. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0230 · Cited by 20 · see citing works
Stabilized β-Hairpin Peptide Inhibits Insulin Degrading Enzyme
Yang, D., Qin, W., Shi, X., Zhu, B., Xie, M., Zhao, H., Teng, B., Wu, Y., Zhao, R., Yin, F., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00418 · Cited by 19 · see citing works
Roles of Natriuretic Peptides and the Significance of Neprilysin in Cardiovascular Diseases
Nakagawa, H., & Saito, Y. (2022) · Biology · doi:10.3390/biology11071017 · Cited by 19 · see citing works
Cerasuolo, M., Auriemma, M. C., Meo, I. D., Lenti, C., Papa, M., Paolisso, G., & Rizzo, M. R. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146693 · Cited by 18 · see citing works
Azargoonjahromi, A. (2024) · Journal of Pharmacy and Pharmacology · doi:10.1093/jpp/rgae066 · Cited by 17 · see citing works
Yasmin, S., Ashique, S., Taj, T., Garg, A. K., Das, J., Shorog, E., Bhui, U., Pal, R., Selim, S., Panigrahy, U. P., et al. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149400 · Cited by 17 · see citing works
The influence of insulin infusion on the metabolism of amyloid β peptides in plasma
Karczewska‐Kupczewska, M., Lelental, N., Adamska, A., Nikołajuk, A., Kowalska, I., Górska, M., Zimmermann, R., Kornhuber, J., Strączkowski, M., & Lewczuk, P. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.01.013 · Cited by 17 · see citing works
- Authors
- Malito, E., Hulse, R. E., & Tang, W.-J.
- Affiliations
- University of Chicago (US)
- Corresponding author
- Tang, W.-J.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2008-05-13
- Volume
- 65
- Issue
- 16
- Pages
- 2574-2585
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC2756532
- OpenAlex
- W2007899228
- Cited by
- 176
- References
- 89
- Citations by year
- 2026: 4 · 2025: 13 · 2024: 5 · 2023: 14 · 2022: 8 · 2021: 9 · 2020: 5 · 2019: 6 · 2018: 12 · 2017: 7 · 2016: 9 · 2015: 17 · 2014: 12 · 2013: 12 · 2012: 6
- FWCI
- 8.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01 GM81539, T32GM007839, R01GM081539, T32GM07839)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
- Keywords
- amyloid-beta, insulin-degrading enzyme, neprilysin, amyloid-beta clearance, Alzheimer's disease, substrate specificity, conformational flexibility, peptide aggregation
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Humans, Insulysin, Molecular Sequence Data, Protein Processing, Post-Translational, Substrate Specificity, Neprilysin, Amyloid beta-Peptides
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