The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Scavenger receptor-mediated adhesion of microglia to β-amyloid fibrils
Abstract
A pathological hallmark of Alzheimer's disease is the senile plaque, containing beta-amyloid fibrils, microglia and astrocytes. Beta-amyloid fibrils exert a cytotoxic effect on neurons, and stimulate microglia to produce neurotoxins, such as reactive oxygen species. Mononuclear phagocytes, including microglia, express scavenger receptors that mediate endocytosis of oxidized low-density lipoproteins, and adhesion to glucose-modified extra-cellular matrix proteins. Here we report that class A scavenger receptors mediate adhesion of rodent microglia and human monocytes to beta-amyloid fibril-coated surfaces leading to secretion of reactive oxygen species and cell immobilization. Thus, class A scavenger receptors are potential therapeutic targets in Alzheimer's disease.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Aβ clearance involves, in part36, phagocytosis and endocytosis via microglial scavenger receptors (SRs)37,38 and extracellular degradation by Aβ-degrading enzymes6,36.”
From Microglia in neurodegeneration (2018) · cites this paper as [38]
In the citing paper
“SR-A1 is an Aβ-phagocytic receptor37,38 expressed on microglia surrounding Aβ plaques in humans and Aβ-mice.”
From Microglia in neurodegeneration (2018) · cites this paper as [38]
Citations
Cites
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
Activation of microglial cells by β-amyloid protein and interferon-γ
Meda, L., Cassatella, M. A., Szendrei, G. I., Otvos, L., Baron, P., Villalba, M., Ferrari, D., & Rossi, F. (1995) · Nature · doi:10.1038/374647a0 · Cited by 1,314
Characterization of ameboid microglia isolated from developing mammalian brain
Giulian, D., & Baker, T. J. (1986) · Journal of Neuroscience · doi:10.1523/jneurosci.06-08-02163.1986 · Cited by 1,300
Krieger, M., & Krieger, J. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.63.1.601 · Cited by 1,169
Quinn, M. T., Parthasarathy, S., Fong, L. G., & Steinberg, D. I. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.9.2995 · Cited by 1,138
Advanced glycation end products contribute to amyloidosis in Alzheimer disease
Vitek, M. P., Bhattacharya, K., Glendening, J. M., Stopa, E., Vlassara, H., Bucala, R., Manogue, K., & Cerami, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4766 · Cited by 806
Advanced Maillard reaction end products are associated with Alzheimer disease pathology.
Smith, M. A., Taneda, S., Richey, P. L., Miyata, S., Yan, S. D., Stern, D., Sayre, L. M., Monnier, V. M., & Perry, G. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5710 · Cited by 715
Pike, C. J., Walencewicz‐Wasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G., & Cotman, C. W. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64010253.x · Cited by 699
Fraser, I. P., Hughes, D. A., & Gordon, S. (1993) · Nature · doi:10.1038/364343a0 · Cited by 341
Jiang, H., Burdick, D., Glabe, C. G., Cotman, C. W., & Tenner, A. J. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.10.5050 · Cited by 330
Flagged first, then by citations
Research works printed but not linked: 5
- Krieger, M. & Herz, J. A. Rev. Biochem. 63, 601–637 (1994). · DOI
- Narindrasorasak, S. et al. Lab. Invest. 72, 272–282 (1995).
- Elghetany, M. T., Saleem, A. & Ban, K. Annls clin. lab. Sci. 19, 190–195 (1989).
- Christie, R. H., Freeman, M. & Hyman, B. T. Am. J. Path. 148, 399–403 (1996).
- Hartung, H.-P. et al. Lab. Invest. 55, 209–216 (1986).
Cited by
Sorted by citations
Items 701–723 of 723
(2003) · Studies in interface science · doi:10.1016/s1383-7303(03)80026-1
Platt, N., & Gordon, S. (2002) · Wiley eBooks · doi:10.1002/0471203076.emm1068
Therapeutic and immunomodulatory functions of the translocator protein in Alzheimer's disease
Fairley, L. H. (2022) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/160865
Chronic neuronal perturbation mediated by RAGE, a receptor for β-sheet fibrils and S100/calgranulins
Yan, S. D., Schmidt, A. M., & Stern, D. M. (2001) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8297-2_18
Aerbajinai, W., Zhu, J., Chin, K., & Rodgers, G. P. (2024) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiae197
Ikezu, T. (2024) · Springer eBooks · doi:10.1007/978-3-031-68237-7_22
Long-Term Potentiation and Aβ: Targeting Aβ Species, Cellular Mechanisms and Putative Receptors
Rowan, M. J., Klyubin, I. V., Cullen, W. K., Hu, N., & Anwyl, R. (2008) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-540-76330-7_12
Schröder, N., Schaffrath, A., Welter, J. A., Putzka, T., Griep, A., Ziegler, P., Brandt, E., Samer, S., Heneka, M. T., Kaddatz, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.12195510
Clayton, K. A., Delpech, J.-C., Herron, S., Iwahara, N., Ericsson, M., Saito, T., Saido, T. C., Ikezu, S., & Ikezu, T. (2021) · Figshare · doi:10.6084/m9.figshare.14267041
The Scavenger Function of LSECs, a Regulator of Liver Diseases
Zhou, J., Zhang, L., Wang, J., Zhang, C., & Tian, C. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48080802
Li, H., Cheng, Y., Lin, X., Feng, Y., Du, B., Dou, B., Sheng, Z., Xu, F., & Geng, D. (2026) · Research Square · doi:10.21203/rs.3.rs-10975363/v1
Lubrich, C., Böttcher, N., Rößler, J., Basta‐Kaim, A., Pufe, T., Kipp, M., & Brandenburg, L. (2026) · Journal of Alzheimer s Disease Reports · doi:10.1177/25424823261494918
Molekulargenetik und Molekularbiologie der Alzheimer-Krankheit
Sandbrink, R., & Beyreuther, K. T. (1999) · Springer eBooks · doi:10.1007/978-3-642-60175-0_7
Potential biomarkers for Alzheimer's disease and mild cognitive impairment
Mitchell, M. B. (2009)
Papel do receptor B2 para as cininas na neuroinflamação induzida pelo peptídeo beta-amilóide
Bicca, M. A. (2012) · Americanae (AECID Library)
Proinflammatory actions of derivatives of the β amyloid precursor protein
Barger, S. W. (2001) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8350-4_8
Macrophages: Microbial Recognition and Response
Plüddemann, A., & Gordon, S. (2014) · ASM Press eBooks · doi:10.1128/9781555816650.ch2
Zujovic (2000) · doi:10.1002/(sici)1098-1136(20000215)29:4
Cole (2000) · doi:10.1002/1097-0029(20000815)50:4
Klegeris (1997) · doi:10.1002/(sici)1097-4547(19970715)49:2
Metadata
- Authors
- Khoury, J. E., Hickman, S. E., Thomas, C. A., Cao, L., Silverstein, S. C., & Loike, J. D.
- Affiliations
- Columbia University (US)
- Venue
- Nature
- Published
- 1996-08
- Volume
- 382
- Issue
- 6593
- Pages
- 716-719
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2045560271
- Cited by
- 727
- References
- 21
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 12 · 2023: 10 · 2022: 18 · 2021: 19 · 2020: 20 · 2019: 15 · 2018: 12 · 2017: 10 · 2016: 18 · 2015: 21 · 2014: 20 · 2013: 22 · 2012: 31
- FWCI
- 29.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Keywords
- scavenger receptors, scavenger receptor A, microglia, amyloid-beta fibrils, Alzheimer's disease, amyloid plaques, reactive oxygen species, monocytes, cell immobilization, therapeutic target
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Cell Adhesion, Cell Line, Cell Movement, Collagen, Humans, Ligands, Membrane Proteins, Molecular Sequence Data, Monocytes, Peptides, Receptors, Immunologic, Amyloid beta-Peptides, Reactive Oxygen Species, Microglia, Receptors, Lipoprotein, Receptors, Scavenger, Scavenger Receptors, Class A, Scavenger Receptors, Class B, Mice, Rats
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