The DOI matches its Crossref record; 89 of the 89 references it cites were found in a registry or an index.
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.
Overview
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
Verification
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?
The cited source says what the claim attributes to it.
In the citing paper
“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.
Citations
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 46,047
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
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
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
Handbook of Proteolytic Enzymes
(2004) · Elsevier eBooks · doi:10.1016/c2009-0-03628-9 · Cited by 2,623
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
Farris, W., Mansourian, S., Chang, Y., Lindsley, L., Eckman, E. A., Frosch, M. P., Eckman, C. B., Tanzi, R. E., Selkoe, D. J., & Guénette, S. Y. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0230450100 · Cited by 1,526
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 1,506
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
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
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
Items 101–178 of 178
Experimental approaches for altering the expression of Abeta‐degrading enzymes
Loeffler, D. A. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15762 · Cited by 18
Hashimoto, V. L., Abreu, P. A. E., Carvalho, E., Gonçales, A. P., de Morais, Z. M., Vasconcellos, S. A., Romero, E. C., & Ho, P. L. (2013) · Microbial Pathogenesis · doi:10.1016/j.micpath.2013.04.011 · Cited by 17
Houshiheisan compound prescription protects neurovascular units after cerebral ischemia
Zhao, H., Zhang, Q., Wang, H., Wang, L., Zhang, N., & Zhang, Q. (2014) · Neural Regeneration Research · doi:10.4103/1673-5374.131580 · Cited by 17
Characterization of insulin-degrading enzyme-mediated cleavage of Aβ in distinct aggregation states
Hubin, E., Cioffi, F., Rozenski, J., van Nuland, N. A. J., & Broersen, K. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.03.010 · Cited by 16
Mechanisms of peptide hydrolysis by aspartyl and metalloproteases
Paul, T. J., Barman, A., Özbil, M., Bora, R. P., Zhang, T., Sharma, G., Hoffmann, Z., & Prabhakar, R. S. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp02097f · Cited by 16
Beuzelin, C., Evnouchidou, I., Rigolet, P., Cauvet, A., Girard, P.-M., Dardalhon-Cuménal, D., Čulina, S., Gdoura, A., Endert, P. V., & Francesconi, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067705 · Cited by 16
Bora, R. P., & Prabhakar, R. S. (2010) · Biochemistry · doi:10.1021/bi1002103 · Cited by 15
Moon, J. H., Kim, J. M., Lee, U., Kang, J. Y., Kim, M. J., Lee, H. L., Jeong, H. R., Go, M. J., Kim, H., Park, H. W., et al. (2022) · Molecules · doi:10.3390/molecules27165316 · Cited by 15
Town, L., McGlinn, E., Fiorenza, S., Metzis, V., Butterfield, N. C., Richman, J. M., & Wicking, C. (2009) · Developmental Dynamics · doi:10.1002/dvdy.22126 · Cited by 15
Structural analysis of Mycobacterium tuberculosis M13 metalloprotease Zmp1 open states
Liang, W. G., Mancl, J. M., Zhao, M., & Tang, W. (2020) · Structure · doi:10.1016/j.str.2020.12.002 · Cited by 14
Self-citationFamakin, B. M., Mou, Y., Johnson, K. R., Spatz, M., & Hallenbeck, J. M. (2013) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2013.182 · Cited by 14
Insulin-Degrading Enzyme, an Under-Estimated Potential Target to Treat Cancer?
Lesire, L., Leroux, F., Deprez-Poulain, R. F., & Deprez, B. P. (2022) · Cells · doi:10.3390/cells11071228 · Cited by 14
Chavan, S. G., & Deobagkar, D. D. (2015) · PLoS ONE · doi:10.1371/journal.pone.0121860 · Cited by 16
Lai, R., Tang, W., & Li, H. (2018) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00406 · Cited by 14
Self-citationBora, R. P., Özbil, M., & Prabhakar, R. S. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0617-2 · Cited by 13
Microglial Lyzl4 Facilitates β‐Amyloid Clearance in Alzheimer's Disease
Pan, J., Zhong, J., Geng, J., Oberhauser, J., Shi, S., & Wan, J. (2024) · Advanced Science · doi:10.1002/advs.202412184 · Cited by 11
Li, N., Yang, G., Wang, Y., Qiao, M., Zhang, P., Shao, J., & Yang, G. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.01.004 · Cited by 12
Blood–Brain Barrier Transport of Alzheimer’s Amyloid β-Peptide
Nelson, A. R., Sagare, A. P., & Zloković, B. V. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00009-5 · Cited by 12
Hydroxypyridinethione Inhibitors of Human Insulin‐Degrading Enzyme
Adamek, R. N., Suire, C. N., Stokes, R. W., Brizuela, M. K., Cohen, S. M., & Leissring, M. A. (2021) · ChemMedChem · doi:10.1002/cmdc.202100111 · Cited by 12
Toxoplasma gondii Toxolysin 4 Contributes to Efficient Parasite Egress from Host Cells
Huynh, M., Roiko, M. S., Gomes, A. D. O., Schinke, E. N., Schultz, A. J., Agrawal, S., Oellig, C. A., Sexton, T. R., Beauchamp, J. M., Laliberté, J., et al. (2021) · mSphere · doi:10.1128/msphere.00444-21 · Cited by 11
Aβ31–35 Decreases Neprilysin-Mediated Alzheimer’s Amyloid-β Peptide Degradation
Leite, J. P., Lete, M. G., Fowler, S. A., Gimeno, A., Rocha, J. F., Sousa, S. F., Webster, C. I., Jiménez‐Barbero, J., & Gales, L. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00432 · Cited by 11
Inhibition of insulin-degrading enzyme in human neurons promotes amyloid-β deposition
Rowland, H. A., Moxon, S. R., Corbett, N. J., Hanson, K., Fisher, K., Kellett, K. A. B., & Hooper, N. M. (2023) · Neuronal Signaling · doi:10.1042/ns20230016 · Cited by 15
Advances and future trends in the detection of beta-amyloid: A comprehensive review
Ganguly, A., Babu, S. S., Ghosh, S. K., Velyutham, R., & Kapusetti, G. (2024) · Medical Engineering & Physics · doi:10.1016/j.medengphy.2024.104269 · Cited by 9
Ha, J. S., Kim, J. M., Park, S. K., Kang, J. Y., Lee, D. S., Lee, U., Kim, D., Choi, S., & Heo, H. J. (2018) · Food & Function · doi:10.1039/c8fo00287h · Cited by 9
de Oliveira, F. F., de Almeida, S. S., Chen, E., Smith, M. D. A. C., & Bertolucci, P. H. F. (2023) · Acta Neuropsychiatrica · doi:10.1017/neu.2023.38 · Cited by 8
Rao, F., Zhang, Z., & Li, J. (2023) · Journal of Mathematical Biology · doi:10.1007/s00285-023-02003-6 · Cited by 8
Development of monoclonal antibodies and quantitative ELISAs targeting insulin-degrading enzyme
DelleDonne, A., Kouri, N., Reinstatler, L. S., Sahara, T., Li, L., Zhao, J., Dickson, D. W., Ertekin‐Taner, N., & Leissring, M. A. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-39 · Cited by 8
Fella, E., Sokratous, K., Papacharalambous, R., Kyriacou, K. C., Phillips, J. A., Sanderson, S. D., Panayiotou, E., & Kyriakides, T. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00138 · Cited by 8
Target Engagement Measures in Preclinical Drug Discovery: Theory, Methods, and Case Studies
Durham, T. B., & Wiley, M. R. (2017) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-319-50042-3_3 · Cited by 7
Differential Effects of Polyphenols on Insulin Proteolysis by the Insulin-Degrading Enzyme
Zheng, Q., Kebede, M. T., Lee, B., Krasinski, C. A., Islam, S., Wurfl, L. A., Kemeh, M. M., Ivancic, V. A., Jakobsche, C. E., Spratt, D. E., et al. (2021) · Antioxidants · doi:10.3390/antiox10091342 · Cited by 7
Insulin-Degrading Enzyme Interacts with Mitochondrial Ribosomes and Respiratory Chain Proteins
Yilmaz, A., Guerrera, I. C., Waeckel-Énée, E., Lipecka, J., Bertocci, B., & Endert, P. V. (2023) · Biomolecules · doi:10.3390/biom13060890 · Cited by 7
QM/MM Simulations of Amyloid-β 42 Degradation by IDE in the Presence and Absence of ATP
da Cruz, C. H. B., & Seabra, G. D. M. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci500544c · Cited by 6
Reddy, B., Kelawala, D. N., Shah, T. V., Patel, A. B., Patil, D. B., Parikh, P. V., Patel, N., Parmar, N. R., Mohapatra, A., Singh, K. M., et al. (2015) · Mammalian Genome · doi:10.1007/s00335-015-9607-6 · Cited by 6
Amyloid Beta Dynamics in Biological Fluids—Therapeutic Impact
Schreiner, T. G., & Popescu, B. O. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10245986 · Cited by 5
Modulation of the Activity of the Insulin-Degrading Enzyme by Aβ Peptides
Kemeh, M. M., & Lazo, N. D. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00384 · Cited by 5
Genetic, Biochemical and Histopathological Aspects of Familiar Alzheimer's Disease
Ortíz, G. G., Pacheco-Moisés, F. P., González-Renovato, E. D., Figuera, L. E., Macías-Islas, M. Á., Mireles-Ramírez, M. A., Flores-Alvarado, L. J., Sánchez-López, A. L., Nuño-Penilla, D. G., Velázquez-Brizuela, I. E., et al. (2015) · InTech eBooks · doi:10.5772/59809 · Cited by 5
Axonal Transport of Neprilysin in Rat Sciatic Nerves
Ohkushi, G., Suzuki, N., Kobayashi, S., & Chikuma, T. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0202-6 · Cited by 4
Key Enzymes and Proteins in Amyloid-Beta Production and Clearance
Santos, C. R. A., Cardoso, I., & Gonçalves, I. (2011) · InTech eBooks · doi:10.5772/17646 · Cited by 5
In Vitro Degradation of Insulin-like Peptide 3 by Insulin-degrading Enzyme
Zhang, W., Luo, X. L., & Guo, Z. (2010) · The Protein Journal · doi:10.1007/s10930-009-9226-8 · Cited by 4
Huang, B., & Tang, G. (2026) · Pathology - Research and Practice · doi:10.1016/j.prp.2026.156564 · Cited by 3
Fluorimetric Assay for Measuring Neprilysin Activity Using HPLC
Takahashi, G., Tabata, M., Taguchi, K., & Chikuma, T. (2015) · Chromatographia · doi:10.1007/s10337-015-2856-4 · Cited by 3
Nozari, A., Sharma, A., Wang, Z., Feng, L., Muresanu, D. F., Tian, Z. R., Lafuente, J. V., Buzoianu, A. D., Wiklund, L., & SHARMA, H. S. (2023) · Advances in neurobiology · doi:10.1007/978-3-031-32997-5_7 · Cited by 3
Xu, M., Xu, Q., Wang, M., Qiu, S., Xu, D., Zhang, W., Wang, W., He, J., Wang, Q., Ran, T., et al. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.03.020 · Cited by 2
Mancl, J. M., Wu, X., Zhao, M., & Tang, W. (2025) · eLife · doi:10.7554/elife.106044.4 · Cited by 2
Self-citationCharacterization of Protein-Metabolite and Protein-Substrate Interactions of Disease Genes
McFedries, A. (2014) · Digital Access to Scholarship at Harvard (DASH) (Harvard University) · Cited by 2
Okumura, M., Kuramochi, T., Lin, Y., Furukawa, R., Mizutani, K., Yokoyama, T., Kim, M., Lim, M. H., Yi, H., Arai, K., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.08.536135 · Cited by 2
Mancl, J. M., Wu, X., Zhao, M., & Tang, W. (2025) · eLife · doi:10.7554/elife.106044 · Cited by 2
Self-citationKhan, M. S., Ahmad, A., Nasiripour, S., & Bopassa, J. C. (2026) · Journal of dementia and Alzheimer's disease · doi:10.3390/jdad3010005 · Cited by 1
Groubman, M. A., Kamanina, Y. V., Petrushanko, I. Y., Rubtsov, A. M., & Lopina, O. D. (2010) · Biochemistry (Moscow) · doi:10.1134/s000629791010010x · Cited by 1
Полтавцева, Р. А., Bobkova, N. V., Zhdanova, D. Y., Svirshchevskaya, E. V., & Sukhikh, G. T. (2021) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747821050068 · Cited by 2
Dimerization and dynamics of angiotensin-I converting enzyme revealed by cryo-EM and MD simulationsPreprint
Mancl, J. M., Wu, X., Zhao, M., & Tang, W. (2025) · eLife · doi:10.7554/elife.106044.2 · Cited by 1
Self-citationDimerization and dynamics of angiotensin-I converting enzyme revealed by cryo-EM and MD simulationsPreprint
Mancl, J. M., Wu, X., Zhao, M., & Tang, W. (2025) · eLife · doi:10.7554/elife.106044.3 · Cited by 1
Self-citationThe dynamic nature of amyloid-beta protein aggregation and its association to Alzheimer’s disease
Vilaprinyó-Pascual, S. (2015) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya)
Genetic variation in genes involved in Abeta-degradation in Alzheimer disease
Blomqvist, M. '. M. '. (2009) · Figshare
Kinetic and docking studies of inhibitors targeting the catalytic zinc in MA clan enzymes
Sjøli, S. (2011) · NORA - Norwegian Open Research Archives
NATRIURETIC PEPTIDES MODULATE HEART RATE, ELECTRICAL CONDUCTION AND ARRHYTHMOGENSIS IN VIVO
Vella, K. (2013) · Library and Archives Canada (Government of Canada)
Singh, P., Maurer‐Stroh, S., Kurochkin, I. V., Eisenhaber, B., & Eisenhaber, F. (2014) · Springer eBooks · doi:10.1007/978-3-7091-1788-0_9
BACE1 Inhibitors: Attractive Therapeutics for Alzheimer’s Disease
Decourt, B., Macias, M. P., Sabbagh, M. N., & Adem, A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803959-5.50010-6
The interplay between mitochondria-endoplasmic reticulum contacts and Alzheimer’s disease
Leal, S., & João, N. (2019) · Figshare
The Viability of Treatment Conditioned to the Pathophysiology of Alzheimer’s Disease
de Oliveira, F. F. (2022) · Springer eBooks · doi:10.1007/978-3-030-94383-7_3
Sharma, H. S., Feng, L., Muresanu, D. F., Tian, Z. R., Lafuente, J. V., Buzoianu, A. D., Nozari, A., Bryukhovetskiy, I., Manzhulo, I., Wiklund, L., et al. (2023) · International review of neurobiology · doi:10.1016/bs.irn.2023.05.018
Geijtenbeek, K. W., Aranda, A. S., Sanz, A. S., Janzen, J., Bury, A. E., Kors, S., Amery, N. A., Schmitz, N. C. M., Reits, E. A., & Schipper-Krom, S. (2024) · Journal of Huntington s Disease · doi:10.3233/jhd-230583
Mancl, J. M., Liang, W. G., Bayhi, N. L., Wei, H., Budell, W. C., Mendez, J. H., Sosnick, T. R., Carragher, B. O., Potter, C. S., & Tang, W. (2026) · eLife · doi:10.7554/elife.105761.4
Self-citationMancl, J. M., Liang, W. G., Bayhi, N. L., Wei, H., Carragher, B. O., Potter, C. S., & Tang, W. (2025) · eLife · doi:10.7554/elife.105761.1
Self-citationMancl, J. M., Liang, W. G., Bayhi, N. L., Wei, H., Budell, W. C., Mendez, J. H., Sosnick, T. R., Carragher, B., Potter, C. S., & Tang, W.-J. (2025) · eLife · doi:10.7554/elife.105761
Self-citationDimerization and dynamics of angiotensin-I converting enzyme revealed by cryoEM and MD simulationsPreprint
Mancl, J. M., Wu, X., Zhao, M., & Tang, W. (2025) · eLife · doi:10.7554/elife.106044.1
Self-citationHeydarian, D., Flavel, M., Munasinghe, M., Jois, M., & Thomas, J. (2025) · Journal of Ageing and Longevity · doi:10.3390/jal5020012
Insulin-degrading enzyme/insulysin
Leissring, M. A. (2025) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-443-28849-4.00266-6
Mancl, J. M., Liang, W. G., Bayhi, N. L., Wei, H., Budell, W. C., Mendez, J. H., Sosnick, T. R., Carragher, B. O., Potter, C. S., & Tang, W. (2025) · eLife · doi:10.7554/elife.105761.2
Self-citationJarząb, M., & Skórko‐Glonek, J. (2025) · Biomolecules · doi:10.3390/biom15121697
Neurodegeneration Protein Structure
Mishra, A., Tiwari, P., Singh, D., & Kadiri, S. K. (2025) · IGI Global eBooks · doi:10.4018/979-8-3373-4627-4.ch008
Mancl, J. M., Liang, W. G., Bayhi, N. L., Wei, H., Budell, W. C., Mendez, J. H., Sosnick, T. R., Carragher, B. O., Potter, C. S., & Tang, W. (2026) · eLife · doi:10.7554/elife.105761.3
Self-citationBindingDB Entry 50002487: Stabilized β-Hairpin Peptide Inhibits Insulin Degrading Enzyme.
BindingDB (2020) · UC San Diego · doi:10.7270/q22n54xf
Metadata
- 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
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › 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