Promiscuous Alzheimer's Amyloid: Yet Another Partner
Abstract
A neuroimmune receptor has high affinity for Alzheimer's β-amyloid aggregates and mediates a synaptotoxic cascade in neurons. [Also see Report by Kim et al. ]
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oAβ induces abnormal elevations in extrasynaptic glutamate and subsequent extrasynaptic NMDAR-mediated excitotoxicity, inhibiting hippocampal LTP.
“oAβ can induce abnormal elevations in extrasynaptic glutamate levels and subsequent extrasynaptic N-methyl-D-aspartic acid receptor (NMDAR)-mediated excitotoxicity, thereby inhibiting hippocampal LTP.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [55]
oAβ disrupts intracellular calcium balance, impairs mitochondrial function, and induces ROS production, leading to neuronal apoptosis and cell death.
“Additionally, oAβ can disrupt intracellular calcium balance, impair mitochondria dysfunction, and induce the production of reactive oxygen species (ROS). All of these events eventually lead to neuronal apoptosis and cell death [55].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [55]
Cites
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962 · see citing works
Self-citationCellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560 · see citing works
Functional requirement for class I MHC in CNS development and plasticity
Huh, G. S., Boulanger, L. M., Du, H., Riquelme, P. A., Brotz, T. M., & Shatz, C. J. (2000) · Science · doi:10.1126/science.290.5499.2155 · Cited by 828 · see citing works
PirB is a Functional Receptor for Myelin Inhibitors of Axonal Regeneration
Atwal, J. K., Pinkston-Gosse, J., Syken, J., Stawicki, S. S., Wu, Y., Shatz, C. J., & Tessier‐Lavigne, M. (2008) · Science · doi:10.1126/science.1161151 · Cited by 503 · see citing works
Reversing EphB2 depletion rescues cognitive functions in Alzheimer model
Cissé, M., Halabisky, B., Harris, J., Devidze, N., Dubal, D. B., Sun, B., Orr, A., Lotz, G., Kim, D. H., Hamto, P., et al. (2011) · Nature · doi:10.1038/nature09635 · Cited by 433 · see citing works
Kim, T., Vidal, G. S., Djurisic, M., William, C. M., Birnbaum, M. E., Garcia, K. C., Hyman, B. T., & Shatz, C. J. (2013) · Science · doi:10.1126/science.1242077 · Cited by 410 · see citing works
PirB restricts ocular-dominance plasticity in visual cortex
Syken, J., GrandPre, T., Kanold, P. O., & Shatz, C. J. (2006) · Science · doi:10.1126/science.1128232 · Cited by 340 · see citing works
Verdier, Y., Zarándi, M., & Penke, B. (2004) · Journal of Peptide Science · doi:10.1002/psc.573 · Cited by 261 · see citing works
Paired immunoglobulin‐like receptors and their MHC class I recognition
Takai, T. (2005) · Immunology · doi:10.1111/j.1365-2567.2005.02177.x · Cited by 168 · see citing works
New developments on the role of NMDA receptors in Alzheimer's disease
Malinow, R. (2012) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.09.001 · Cited by 132 · see citing works
FcγRIIb mediates amyloid-β neurotoxicity and memory impairment in Alzheimer’s disease
Kam, T.-I., Song, S., Gwon, Y., Park, H., Yan, J.-J., Im, I., Choi, J.-W., Choi, T.-Y., Kim, J., Song, D.-K., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66827 · Cited by 128 · see citing works
Synaptic Plasticity Defect Following Visual Deprivation in Alzheimer's Disease Model Transgenic Mice
William, C. M., Andermann, M. L., Goldey, G. J., Roumis, D. K., Reid, R. C., Shatz, C. J., Albers, M. W., Frosch, M. P., & Hyman, B. T. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5369-11.2012 · Cited by 50 · see citing works
(2011) · Nature Neuroscience · doi:10.1038/nn0411-399 · Cited by 25 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Scheltens, P., Blennow, K., Breteler, M. M. B., de Strooper, B., Frisoni, G. B., Salloway, S., & Van der Flier, W. M. (2016) · The Lancet · doi:10.1016/s0140-6736(15)01124-1 · Cited by 3,125 · see citing works
The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease
Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201 · see citing works
Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease
Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994 · see citing works
Compromised MAPK signaling in human diseases: an update
Kim, E., & Choi, E. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1472-2 · Cited by 1,017 · see citing works
The clinical promise of biomarkers of synapse damage or loss in Alzheimer’s disease
the Synaptic Health Endpoints Working Group, Colom-Cadena, M., Spires-Jones, T., Zetterberg, H., Blennow, K., Caggiano, A., DeKosky, S. T., Fillit, H., Harrison, J. E., Schneider, L. S., et al. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00588-4 · Cited by 328 · see citing works
Amyloid-β Receptors: The Good, the Bad, and the Prion Protein
Jarosz-Griffiths, H. H., Noble, E., Rushworth, J. V., & Hooper, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.702704 · Cited by 256 · see citing works
Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism
Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256 · see citing works
Analyzing dendritic spine pathology in Alzheimer’s disease: Problems and opportunities
Dorostkar, M. M., Zou, C., Blazquez-Llorca, L., & Herms, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1449-5 · Cited by 235 · see citing works
Dendritic Spine Pathology in Neurodegenerative Diseases
Herms, J., & Dorostkar, M. M. (2016) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012615-044216 · Cited by 201 · see citing works
Li, R.-Y., Qin, Q., Yang, H.-C., Wang, Y.-Y., Mi, Y.-X., Yin, Y.-S., Wang, M., Yu, C.-J., & Tang, Y. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00542-y · Cited by 204 · see citing works
Goure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt272 · Cited by 190 · see citing works
Actin dynamics and cofilin‐actin rods in alzheimer disease
Bamburg, J. R., & Bernstein, B. W. (2016) · Cytoskeleton · doi:10.1002/cm.21282 · Cited by 181 · see citing works
Izzo, N. J., Staniszewski, A., To, L., Fa, M., Teich, A. F., Saeed, F., Wostein, H., Walko, T., Vaswani, A., Wardius, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111898 · Cited by 180 · see citing works
Ledo, J. H., Azevedo, E. P., Beckman, D., Ribeiro, F. C., Santos, L. E., Razolli, D. S., Kincheski, G. C., Melo, H. M., Bellio, M., Teixeira, A. L., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1269-16.2016 · Cited by 137 · see citing works
Bamburg, J. R., Minamide, L. S., Wiggan, O., Tahtamouni, L. H., & Kuhn, T. B. (2021) · Cells · doi:10.3390/cells10102726 · Cited by 122 · see citing works
Ripoli, C., Cocco, S., Puma, D. D. L., Piacentini, R., Mastrodonato, A., Scala, F., Puzzo, D., D’Ascenzo, M., & Grassi, C. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1201-14.2014 · Cited by 122 · see citing works
Alzheimer's Disease Mechanisms and Emerging Roads to Novel Therapeutics
Sala Frigerio, C., & De Strooper, B. (2016) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-070815-014015 · Cited by 116 · 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
Banik, A., Brown, R. E., Bamburg, J., Lahiri, D. K., Khurana, D., Friedland, R. P., Chen, W., Ding, Y., Mudher, A., Padjen, A. L., et al. (2015) · Journal of Alzheimer’s Disease · doi:10.3233/jad-150136 · Cited by 102 · see citing works
Prion Protein as a Toxic Acceptor of Amyloid-β Oligomers
Purro, S. A., Nicoll, A. J., & Collinge, J. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.11.020 · Cited by 80 · see citing works
Smith, L. M., Kostylev, M. A., Lee, S., & Strittmatter, S. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006252 · Cited by 80 · see citing works
Nuclear Translocation Uncovers the Amyloid Peptide Aβ42 as a Regulator of Gene Transcription*
Barucker, C., Harmeier, A., Weiske, J., Fauler, B., Albring, K. F., Prokop, S., Hildebrand, P. W., Lurz, R., Heppner, F. L., Huber, O., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564690 · Cited by 78 · see citing works
Vargas, L. M., Cerpa, W. F., Muñoz, F. J., Zanlungo, S., & Alvarez, A. R. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.01.023 · Cited by 69 · see citing works
Ribarič, S. (2023) · Biomedicines · doi:10.3390/biomedicines11020355 · Cited by 66 · see citing works
Han, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67 · see citing works
Walsh, K. P., Minamide, L. S., Kane, S. J., Shaw, A. E., Brown, D. R., Pulford, B. E., Zabel, M. D., Lambeth, J. D., Kuhn, T. B., & Bamburg, J. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095995 · Cited by 65 · see citing works
Bharadwaj, P., Solomon, T., Malajczuk, C. J., Mancera, R. L., Howard, M. J., Arrigan, D. W. M., Newsholme, P., & Martins, R. N. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.03.015 · Cited by 60 · see citing works
From Dysbiosis to Neurodegenerative Diseases through Different Communication Pathways: An Overview
Intili, G., Paladino, L., Rappa, F., Alberti, G., Plicato, A., Calabrò, F., Fucarino, A., Cappello, F., Bucchieri, F., Tomasello, G., et al. (2023) · Biology · doi:10.3390/biology12020195 · Cited by 61 · see citing works
ACU193: An Immunotherapeutic Poised to Test the Amyloid β Oligomer Hypothesis of Alzheimer’s Disease
Krafft, G. A., Jerecı̀ć, J., Siemers, E., & Cline, E. N. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.848215 · Cited by 51 · see citing works
Shaw, A. E., & Bamburg, J. R. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.031 · Cited by 50 · see citing works
Pan, M., Wu, Y., Sun, C., Ma, H., Ye, X., & Li, X. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118002 · Cited by 49 · see citing works
Ganzinger, K. A., Narayan, P. S., Qamar, S., Weimann, L., Ranasinghe, R. T., Aguzzi, A., Dobson, C. M., McColl, J. T., George‐Hyslop, P. S., & Klenerman, D. (2014) · ChemBioChem · doi:10.1002/cbic.201402377 · Cited by 49 · see citing works
QIAD assay for quantitating a compound’s efficacy in elimination of toxic Aβ oligomers
Brener, O., Dunkelmann, T., Gremer, L., van Groen, T., Mirecka, E. A., Kadish, I., Willuweit, A., Kutzsche, J., Jürgens, D., Rudolph, S., et al. (2015) · Scientific Reports · doi:10.1038/srep13222 · Cited by 47 · see citing works
Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease
Colom‐Cadena, M., Toombs, J., Simzer, E. M., Holt, K., McGeachan, R. I., Tulloch, J., Jackson, R. J., Catterson, J. H., Spires-Jones, M. P., Rose, J. L., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-023-02679-6 · Cited by 41 · see citing works
The vexing complexity of the amyloidogenic pathway
Castro, M., Hadziselimovic, A., & Sanders, C. R. (2019) · Protein Science · doi:10.1002/pro.3606 · Cited by 36 · see citing works
PrPC signalling in neurons: From basics to clinical challenges
Hirsch, T. Z., Hernandez-Rapp, J., Martin‐Lannerée, S., Launay, J., & Mouillet‐Richard, S. (2014) · Biochimie · doi:10.1016/j.biochi.2014.06.009 · Cited by 33 · see citing works
Murray, B., Sorci, M., Rosenthal, J., Lippens, J. L., Isaacson, D., Das, P., Fabris, D., Li, S., & Belfort, G. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24995 · Cited by 33 · see citing works
Gwon, Y., Kam, T., Kim, S.-H., Song, S., Park, H., Lim, B., Lee, H., Lee, W., Jo, D., & Jung, Y. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1996-17.2018 · Cited by 32 · see citing works
Hu, T., Wang, S., Chen, C., Sun, J., & Yang, X. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04950 · Cited by 28 · see citing works
Han, F., Zhuang, T.-T., Chen, J., Zhu, X.-L., Cai, Y., & Lu, Y.-P. (2017) · PLoS ONE · doi:10.1371/journal.pone.0185102 · Cited by 26 · see citing works
Therapeutic Strategies Targeting Amyloid-β Receptors and Transporters in Alzheimer’s Disease
Lao, K., Zhang, R., Luan, J., Zhang, Y., & Gou, X. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-200851 · Cited by 25 · see citing works
Pyroglutamylated Amyloid-β Peptide Reverses Cross β-Sheets by a Prion-Like Mechanism
Matos, J. O., Goldblatt, G., Jeon, J., Chen, B., & Tatulian, S. A. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp412743s · Cited by 25 · see citing works
Gholamigeravand, B., Shahidi, ., Amiri, I., Samzadeh‐Kermani, A., Abbasalipourkabir, R., & Asl, S. S. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00713-8 · Cited by 21 · see citing works
Pietropaolo, A., Satriano, C., Strano, G., Mendola, D. L., & Rizzarelli, E. (2015) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2015.08.013 · Cited by 20 · see citing works
Hijacking PrPc-dependent signal transduction: when prions impair Aβ clearance
Hernandez-Rapp, J., Martin‐Lannerée, S., Hirsch, T. Z., Launay, J., & Mouillet‐Richard, S. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00025 · Cited by 21 · see citing works
Wahlberg, E., Rahman, M. M., Lindberg, H., Gunneriusson, E., Schmuck, B., Lendel, C., Sandgren, M. O. J., Löfblom, J., Ståhl, S., & Härd, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-06377-8 · Cited by 19 · see citing works
Ali, A. A., Khalil, M. G., El‐latif, D. M. A., Okda, T. M., Abdelaziz, A. I., Abu‐Elfotuh, K., Kamal, M. M., & Wahid, A. M. (2021) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2021.104557 · Cited by 18 · see citing works
Anand Ganapathy, A., Haripriya, V. M., Acharya, N. S., Somappa, S. B., & Kumaran, A. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23339 · Cited by 17 · see citing works
Xu, H., Li, L., Wang, Y., Wang, H., An, D., Heng, B., & Liu, Y. (2018) · Phytotherapy Research · doi:10.1002/ptr.6239 · Cited by 17 · see citing works
Nižetić, D., Chen, C., Hong, W., & Koo, E. H. (2015) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2015.00299 · Cited by 9 · see citing works
Xue, W., He, W., Yan, M., Zhao, H., & Pi, J. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230559 · Cited by 6 · see citing works
Zhang, Z., Ling, Z., Ling, Z., Li, Y., Pan, J., Gao, Q., Zhang, J., Yan, L., Zhang, Z., Li, J., et al. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11363-2 · Cited by 8 · see citing works
The molecular pathology of neurodegenerative and psychiatric disorders
Yan, P., Deng, Y. M., Su, X., Kong, H., Zhang, Y., Li, W., & Kong, E. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-18677-6.00007-5 · Cited by 8 · see citing works
Design of a multi-analyte resonant photonic platform for label-free biosensing
Chen, C., Hou, X., & Si, J. (2019) · Nanotechnology · doi:10.1088/1361-6528/ab0771 · Cited by 8 · see citing works
Chen, C., Wang, K., & Hou, X. (2022) · Optics Express · doi:10.1364/oe.474043 · Cited by 6 · see citing works
Introduction to Neurodegenerative Diseases
Seyedebrahimi, R., Yang, P., Azimzadeh, M., Farsani, M. E., Ababzadeh, S., Kalhor, N., & Sheykhhasan, M. (2024) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/979-8-3693-1281-0.ch002 · Cited by 6 · see citing works
Mei, J., Xu, W., Gao, W., Wang, C., Guan, Y., Ahmad, S., & Ai, H. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp02746e · Cited by 6 · see citing works
Shome, A., Jha, K. T., Chahat, Chawla, V., & Chawla, P. A. (2024) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273315191241002115155 · Cited by 4 · see citing works
Houshmand, F., HASHIM, A. A., MOHAMMAD, H. A., DRISS, F., IRANPOUR, F., AHMADI, R., NAJAFI, N., Altememy, D., & Khosravian, P. (2025) · International Journal of Applied Pharmaceutics · doi:10.22159/ijap.2025v17i2.53076 · Cited by 2 · see citing works
The transmembrane amyloid precursor C99 protein exhibits non-specific interaction with tau
Britton, R. J., Hutchison, J. M., & Sanders, C. R. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.08.075 · Cited by 2 · see citing works
Vasconcelos, B., Bird, M., Stancu, I., Terwel, D., & Dewachter, I. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805120-7.00006-3 · Cited by 2 · see citing works
Peyvand, P., Allami, P., & Rezaei, N. (2025) · Reviews in the Neurosciences · doi:10.1515/revneuro-2025-0025 · Cited by 1 · see citing works
The 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)
Past, Present, and Future: The Behavioral Sciences.
Darley, J. G. (1971) · Contemporary Psychology · doi:10.1037/014015
Emerging therapeutics and future insights into the pathobiology of Alzheimer’s disease
Ullah, S.-K. L. I. (2018) · International Journal of Biosciences (IJB) · doi:10.12692/ijb/12.2.231-246
The neuroscience of Alzheimer’s disease
Spires‐Jones, T. L. (2026) · doi:10.1093/9780198995296.003.0003
Zhong, J., Zhou, X., Yu, W., Xie, X., & Tang, Y. (2026) · Spectroscopy Letters · doi:10.1080/00387010.2026.2737816
- Authors
- Benilova, I., & De Strooper, B.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- Vlaams Instituut voor Biotechnologie (VIB) Center for the Biology of Disease, 3000 Leuven, Belgium, and Center for Human Genetics and Leuven Institute for Neuroscience and Disease (LIND), University of Leuven (KU Leuven) and University Hospitals, 3000 Leuven, Belgium.
- ORCID
- Benilova, Iryna
- Venue
- Science
- Published
- 2013-09-20
- Volume
- 341
- Issue
- 6152
- Pages
- 1354-1355
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2058016020
- Cited by
- 67
- References
- 13
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4 · 2023: 6 · 2022: 3 · 2021: 6 · 2020: 2 · 2019: 3 · 2018: 5 · 2017: 6 · 2016: 6 · 2015: 9 · 2014: 12
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Lirias (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- Alzheimer's disease, amyloid-beta, synaptotoxicity, ligand-receptor interactions, neuroinflammation, synapses
- MeSH terms
- Alzheimer Disease, Animals, Female, Humans, Male, Membrane Glycoproteins, Neuronal Plasticity, Peptide Fragments, Receptors, Immunologic, Synapses, Amyloid beta-Peptides
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