The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
RAGE in tissue homeostasis, repair and regeneration
Open accessAbstract
RAGE (receptor for advanced glycation end-products) is a multiligand receptor of the immunoglobulin superfamily involved in inflammation, diabetes, atherosclerosis, nephropathy, neurodegeneration, and cancer. Advanced glycation end-products, high mobility group box-1 (amphoterin), β-amyloid fibrils, certain S100 proteins, and DNA and RNA are RAGE ligands. Upon RAGE ligation, adaptor proteins (i.e., diaphanous-1, TIRAP, MyD88 and/or other as yet unidentified adaptors) associate with RAGE cytoplasmic domain resulting in signaling. However, RAGE activation may not be restricted to pathological statuses, the receptor being involved in tissue homeostasis and regeneration/repair upon acute injury, and in resolution of inflammation. RAGE effects are strongly dependent on the cell type and the context, which may condition therapeutic strategies aimed at reducing RAGE signaling.
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Cites
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Self-citationHMGB1 and RAGE in Inflammation and Cancer
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Understanding RAGE, the receptor for advanced glycation end products
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Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases
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Advanced glycation endproducts and their receptor RAGE in Alzheimer's disease
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“Indeed, the participation of RAGE signaling in neurodegenerative diseases via direct effects on neurons and indirect effects through microglia and astrocyte activation is long recognized [17,80,81].”
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Cited by
Perrone, A., Giovino, A., Benny, J., & Martinelli, F. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/3818196 · Cited by 459
RAGE regulation and signaling in inflammation and beyond
Kierdorf, K., & Fritz, G. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.1012519 · Cited by 428
Role of S100 proteins in health and disease
Gonzalez, L. L., Garrie, K., & Turner, M. D. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118677 · Cited by 361
Hussain, G., Wang, J., Rasul, A., Anwar, H., Qasim, M., Zafar, S., Aziz, N., Razzaq, A., Hussain, R., de Aguilar, J.-L. G., et al. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.35653 · Cited by 323
C1q: A fresh look upon an old molecule
Thielens, N. M., Tedesco, F., Bohlson, S. S., Gaboriaud, C., & Tenner, A. J. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.05.025 · Cited by 237
“by acting as a phosphatidylserine (PS) receptor (reviewed in (Sorci et al., 2013).”
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Metadata
- Authors
- Sorci, G., Riuzzi, F., Giambanco, I., & Donato, R.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 1833
- Issue
- 1
- Pages
- 101-109
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2054346127
- Cited by
- 227
- References
- 17
- FWCI
- 9.16
- Type
- journal article
- Language
- en
- Open access
- bronze
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