Rage (Receptor For Advanced Glycation End Products) is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
RAGE[1] (Receptor for
Advanced Glycation End Products), encoded by the AGER gene on chromosome 6p21.3, is a multiligand pattern recognition receptor of the immunoglobulin superfamily that plays a
central role in the pathogenesis of Alzheimer's disease, [diabetes], and chronic inflammatory disorders. RAGE[1] was originally identified as the receptor for advanced glycation end
products[2] (AGEs) — non-enzymatic modification products of proteins and lipids formed under
conditions of hyperglycemia and oxidative stress — but has since been recognized as a broad-spectrum receptor for damage-associated molecular patterns (DAMPs) including
amyloid-beta, HMGB1, S100 proteins, and phosphorylated tau].[1]
In the context of neurodegeneration, RAGE[1] is important for two interlocking reasons.
First, it mediates influx of circulating [Amyloid-Beta ([Aβ)] across the blood-brain barrier into brain parenchyma, functionally opposing
LRP1-mediated efflux. Second, RAGE[1] amplifies [neuroinflammatory signaling]
through NF-κB activation in neurons, microglia
The RAGE[1] pathway has emerged as a compelling therapeutic target, with several
small-molecule inhibitors, soluble RAGE[1] decoy
strategies, and anti-RAGE[1] antibodies under
investigation. The clinical development of azeliragon (TTP488), an oral RAGE[1] inhibitor, demonstrated the therapeutic relevance of this pathway despite not meeting primary endpoints
in Phase 3 trials, and newer compounds identified through computational approaches continue to advance.[3]
¶ Structure and Expression
RAGE[1] is a ~45 kDa type I transmembrane glycoprotein with a modular architecture
consisting of five distinct functional domains:[1]
- V-type immunoglobulin domain (variable domain): The N-terminal domain that serves as the primary ligand-binding region. Recognizes a remarkable diversity of structurally unrelated ligands including Aβ, AGEs, S100B, S100A12, HMGB1, and other DAMPs. The V-domain contains a large positively charged surface that interacts with negatively charged ligand surfaces
- Two C-type immunoglobulin domains (C1 and C2): Structural domains positioned between the V-domain and the transmembrane region. C1 contributes to the overall ligand-binding interface, while C2 provides structural spacing. The V-C1 module forms a rigid unit that constitutes the minimal functional ligand-binding region
- Single transmembrane domain: A hydrophobic alpha-helix that anchors RAGE[1] in the plasma membrane and may participate in receptor oligomerization upon ligand binding
- Short cytoplasmic tail (43 amino acids): Essential for signal transduction despite lacking intrinsic kinase activity. Signals through binding to the adaptor protein DIAPH1 (also known as mDia1, mammalian diaphanous-related formin 1), which activates downstream kinase cascades. Also interacts with TIRAP and MyD88 adaptors
RAGE[1] exists in multiple isoforms generated by alternative splicing and
proteolytic processing:[4]
- Full-length RAGE[1] (fl-RAGE: The canonical membrane-bound signaling receptor that mediates all RAGE[1]-dependent pathological signaling
- Soluble RAGE[1] (sRAGE: Generated by ADAM10 metalloprotease-mediated ectodomain shedding of fl-RAGE[1]. sRAGE[1] retains the extracellular ligand-binding domains but lacks the transmembrane and cytoplasmic regions, functioning as a naturally occurring decoy receptor that sequesters RAGE[1] ligands in the extracellular space and prevents signaling
- Endogenous secretory RAGE[1] (esRAGE: An alternatively spliced variant that lacks the transmembrane domain and is directly secreted. Also functions as a decoy receptor. esRAGE[1] represents approximately 20% of total circulating sRAGE[1]
- Dominant-negative RAGE[1] (DN-RAGE: A truncated form lacking the cytoplasmic signaling domain; binds ligands but cannot signal, acting as a membrane-anchored decoy
Reduced plasma sRAGE[1]/esRAGE[1] levels are
consistently associated with increased Alzheimer's disease risk and faster cognitive decline, making sRAGE[1] a potential peripheral biomarker for RAGE[1] pathway activity and AD susceptibility.[5]
In the healthy adult brain, RAGE[1] is expressed at low basal levels. In
Alzheimer's disease, RAGE[1] expression is dramatically upregulated in
specific cell populations:[6]
- Brain endothelial cells: The primary site of RAGE[1]-mediated Aβ transport across the BBB. RAGE[1] is concentrated on the luminal (blood-facing) surface where it binds circulating Aβ
- **microglia |
| Mac-1 (CD11b/CD18) | Activated [microglia | Leukocyte adhesion; microglial migration toward plaques |
| Lysophosphatidic acid | Membrane damage | Neuronal stress signaling |
RAGE[1] is the primary receptor mediating Aβ influx from blood into the brain, a
process that directly contributes to cerebral Aβ accumulation:[2]
- Circulating Aβ40 and Aβ42 in plasma bind to the V-domain of RAGE[1] on the luminal (blood-facing) surface of brain endothelial cells
- The RAGE[1]-Aβ complex undergoes receptor-mediated transcytosis across the endothelial cell, a process that requires the cytoplasmic domain signaling through DIAPH1
- Aβ is released into the brain parenchyma on the abluminal side, contributing to extracellular amyloid accumulation
- During transcytosis, RAGE[1] activation also triggers endothelial
inflammatory signaling (NF-κB activation), generation of reactive oxygen species, and expression of adhesion molecules, promoting monocyte
transmigration and neuroinflammation[3]
- RAGE[1]-mediated Aβ influx also reduces cerebral blood flow through endothelin-1 release and neurovascular uncoupling
Brain Aβ levels are determined by the balance between influx (RAGE[1]-mediated) and
efflux ([LRP1 across the BBB. This "yin-yang" model, proposed by Zlokovic (2004), explains how BBB transport dysfunction contributes to Aβ
accumulation:[7]
In healthy brains: LRP1-mediated Aβ efflux (brain-to-blood) substantially exceeds RAGE[1]-mediated influx (blood-to-brain), maintaining low parenchymal Aβ levels
In Alzheimer's Disease:
- RAGE[1] expression on endothelial cells increases 2-3 fold → increased Aβ influx
- LRP1 expression on endothelial cells decreases by ~50% → decreased Aβ efflux
- The balance shifts decisively toward net Aβ accumulation in the brain
- This shift precedes and accelerates amyloid plaque formation
- Additionally, [apolipoprotein E isoform E4 (the major genetic risk factor for AD) impairs LRP1-mediated Aβ clearance while not affecting RAGE[1] transport, further shifting the balance
RAGE[1] activation by Aβ and other ligands triggers multiple inflammatory cascades
that amplify neurodegeneration:[8]
- NF-κB activation: RAGE[1] signals through the DIAPH1/mDia1 adaptor to activate IKK and ultimately NF-κB, driving transcription of pro-inflammatory cytokines (TNF-α, IL-1β, IL-6), chemokines (MCP-1, CXCL10), and adhesion molecules (VCAM-1, ICAM-1)
- MAPK cascades: RAGE[1] activates ERK1/2, JNK, and p38 MAPK signaling pathways, promoting inflammatory gene expression and cellular stress responses
- Oxidative stress: RAGE[1]-mediated activation of NADPH oxidase (NOX2) generates superoxide radicals, and activation of the mitochondrial electron transport chain generates reactive oxygen species, causing oxidative damage to lipids, proteins, and DNA
- TXNIP-NLRP3 axis: RAGE[1] activates thioredoxin-interacting protein (TXNIP), which promotes NLRP3 inflammasome assembly, caspase-1 activation, and IL-1β/IL-18 release in [microglia. This pathway connects RAGE[1] to pyroptotic inflammatory cell death
- Positive feedback loop: Critically, NF-κB activation upregulates RAGE[1] gene transcription itself (the AGER promoter contains NF-κB response elements), creating a self-amplifying inflammatory cycle that sustains chronic neuroinflammation[3] even after the initial trigger is resolved
Direct effects of RAGE[1] activation on neurons include:[9]
- Mitochondrial dysfunction: RAGE[1]-Aβ signaling impairs mitochondrial complex IV activity, reduces ATP production, increases mitochondrial ROS generation, and promotes mitochondrial membrane permeabilization
- Synaptic dysfunction: Reduces long-term potentiation (LTP) in the hippocampus, impairs synaptic plasticity, decreases BDNF expression, and reduces dendritic spine density
- Tau hyperphosphorylation: RAGE[1]-mediated activation of GSK-3β and CDK5 promotes tau] hyperphosphorylation at disease-relevant epitopes, linking amyloid and tau pathologies
- Calcium dysregulation: Impairs intracellular calcium homeostasis through disruption of store-operated calcium entry and ryanodine receptor function
- Apoptotic activation: RAGE[1] signaling activates caspase-dependent and caspase-independent [apoptotic] pathways, contributing to neuronal loss in vulnerable brain regions
RAGE[1] contributes to the cerebrovascular dysfunction
characteristic of AD:[10]
- Endothelial activation with increased expression of adhesion molecules (VCAM-1, ICAM-1), promoting leukocyte adhesion and transmigration
- BBB permeability increase through disruption of tight junction proteins (claudin-5, occludin, ZO-1)
- Reduced cerebral blood flow via neurovascular uncoupling and endothelin-1-mediated vasoconstriction
- [Pericyte] dysfunction and loss, further compromising BBB integrity
- Promotion of cerebral amyloid angiopathy (CAA) through vascular Aβ deposition
- Basement membrane thickening and AGE crosslinking of extracellular matrix proteins
The RAGE[1]-AGE interaction provides a key mechanistic link between type 2 diabetes and
Alzheimer's disease, explaining the epidemiologically observed 1.5-2 fold increased AD risk in diabetic patients:[11]
- AGE formation: Chronic hyperglycemia accelerates non-enzymatic glycation of proteins and lipids (Maillard reaction), generating AGEs including carboxymethyllysine (CML), pentosidine, and methylglyoxal-derived modifications
- AGE-RAGE[1] vascular signaling: AGEs bind RAGE[1] on brain endothelial cells, activating NF-κB and oxidative stress pathways that promote BBB dysfunction and increase permeability to circulating Aβ
- Aβ glycation: AGE modification of Aβ peptides accelerates their aggregation and increases their affinity for RAGE[1], amplifying pathological signaling
- Tau glycation: AGE modification of tau] promotes its hyperphosphorylation, aggregation, and resistance to proteasomal degradation
- Insulin signaling crosstalk: RAGE[1]-AGE signaling impairs neuronal insulin receptor signaling (insulin resistance), reducing insulin-degrading enzyme (IDE) activity and compromising both Aβ degradation and glucose metabolism
- Shared inflammatory pathways: Both diabetes and AD feature chronic activation of the same RAGE[1]-NF-κB-cytokine cascades
- RAGE[1] levels are elevated in both diabetic and AD brains, with diabetic AD patients showing the highest RAGE[1] expression levels
RAGE[1] expression is increased in the substantia nigra of Parkinson's disease
patients. AGE-RAGE[1] signaling contributes to dopaminergic neuron damage through oxidative
stress and [neuroinflammation[3]/3). AGE modifications of alpha-synuclein
promote its aggregation and Lewy body formation.[12]
In ALS, RAGE[1] is upregulated in spinal cord motor neurons and surrounding glia.
HMGB1-RAGE[1] signaling amplifies the neuroinflammatory response that contributes to
motor neuron degeneration. SOD1-mutant ALS mice show elevated RAGE[1] expression in
the ventral spinal cord.
AGE accumulation and RAGE[1] activation have been observed in the striatum of Huntington's disease models, with mutant huntingtin aggregates showing AGE modifications that enhance their toxicity.
RAGE[1]-targeted molecular imaging represents an emerging diagnostic approach for Alzheimer's Disease:[13]
- PET ligands: [18F]-labeled and [11C]-labeled RAGE[1]-targeting radioligands are under development for in vivo imaging of RAGE[1] expression in the AD brain
- MRI contrast agents: Nanoparticle-based RAGE[1]-targeted contrast agents have been tested in preclinical models for visualizing BBB dysfunction and neuroinflammation[3]
- Advantages over amyloid PET: RAGE[1] imaging may detect earlier disease stages by visualizing the inflammatory and vascular components of AD pathogenesis before substantial amyloid plaque accumulation
- These imaging approaches could enable patient selection for RAGE[1]-targeted therapies and monitoring of treatment response
| Compound |
Mechanism |
Status |
Key Findings |
| FPS-ZM1 |
Blocks Aβ-RAGE[1] binding at BBB V-domain |
Preclinical |
Reduces Aβ influx by ~60%; improves cerebral blood flow; decreases neuroinflammation[3], amyloid burden, and tau phosphorylation in APP transgenic mice |
| Azeliragon (TTP488) |
Oral RAGE[1] inhibitor; blocks AGE, S100B, Aβ binding to V-domain |
Phase 2/3 (discontinued) |
BBB-penetrant; Phase 2 showed cognitive benefit trends at 18 months; Phase 3 (STEADFAST) did not meet primary endpoints; post-hoc analyses suggested benefit in mild AD subgroup |
| FPS2 |
Second-generation multimodal RAGE[1] inhibitor |
Preclinical |
Enhanced BBB penetrance and efficacy over FPS-ZM1 |
| In-silico identified compounds |
Virtual screening and molecular dynamics-identified hits targeting V-domain |
Discovery (2025) |
Computational approaches identifying novel scaffolds with improved drug-like properties and RAGE[1] selectivity |
- Recombinant sRAGE[1] administration: Exogenous sRAGE[1] acts as a decoy to sequester RAGE[1] ligands (Aβ, AGEs, HMGB1) in the periphery, reducing their ability to activate membrane-bound RAGE[1]. In APP transgenic mice, sRAGE[1] administration reduces cerebral amyloidosis and improves cognitive function[3]
- Gene therapy to increase endogenous sRAGE[1]/esRAGE[1] production: Viral vector-mediated overexpression of esRAGE[1] in preclinical models
- Challenges: Maintaining therapeutic sRAGE[1] levels in the periphery requires repeated dosing; sRAGE[1] does not cross the BBB at pharmacological concentrations
- Monoclonal antibodies targeting the V-domain to block ligand binding have shown preclinical efficacy in reducing Aβ transport and neuroinflammation[3]
- Bispecific antibody approaches combining RAGE[1] blockade with Aβ clearance are under investigation
Since ADAM10 cleaves fl-RAGE[1] to generate protective
sRAGE[1], enhancing ADAM10 activity represents an indirect
therapeutic strategy. Notably, ADAM10 also functions
as an alpha-secretase for APP, providing dual benefit by both increasing sRAGE[1] and
decreasing amyloidogenic APP processing.[14]
Reduced plasma sRAGE[1] levels are consistently associated with increased AD risk and may serve as
a peripheral biomarker:[5]
- AD diagnosis: Plasma sRAGE[1] levels are significantly lower in AD patients compared to cognitively normal controls (meta-analyses show ~20-30% reduction)
- MCI prediction: Reduced sRAGE[1] in mild cognitive impairment patients predicts conversion to dementia
- Disease severity: sRAGE[1] levels correlate inversely with amyloid PET burden and CSF Aβ42 levels
- Therapeutic monitoring: The sRAGE[1]/fl-RAGE[1] ratio may indicate RAGE[1] pathway activity and could be used to identify patients likely to benefit from RAGE[1]-targeted therapy and to monitor treatment response
- Comorbidity consideration: sRAGE[1] is also reduced in type 2 diabetes, cardiovascular disease, and chronic kidney disease, which may confound AD-specific interpretation
RAGE[1] may serve as a more sensitive early biomarker than Aβ alone because
RAGE[1] upregulation reflects both the inflammatory and vascular components of AD
pathogenesis that precede substantial amyloid accumulation.[13]
RAGE is a multiligand receptor with the following structural features:
- Extracellular Domain: One V-type (variable) domain and two C-type (constant) domains that mediate ligand binding [1]
- Transmembrane Domain: Single-pass membrane-spanning region [2]
- Cytoplasmic Domain: Short intracellular tail required for signal transduction [3]
- Low basal expression: In most normal tissues, RAGE is minimally expressed [4]
- Inducible expression: Upregulated in response to inflammation, injury, and disease [5]
- Cellular localization: Expressed on neurons, glia, endothelial cells, pericytes, and immune cells [6]
¶ Primary Ligands
| Ligand |
Relevance to Disease |
| Advanced Glycation Endproducts (AGEs) |
Formed in diabetes and aging [7] |
| Amyloid-Beta (Aβ) |
Central to AD pathogenesis [8] |
| S100/calgranulins |
Pro-inflammatory calcium-binding proteins [9] |
| HMGB1 (High Mobility Group Box 1) |
Damage-associated molecular pattern [10] |
| Phospholipids |
Oxidative cell damage products [11] |
In Alzheimer's Disease, RAGE plays a particularly important role:
- Aβ Binding: RAGE binds to both soluble and fibrillar Aβ with high affinity [12]
- Receptor-mediated transport: RAGE facilitates Aβ influx across the Blood-Brain Barrier [13]
- Intracellular signaling: Aβ-RAGE engagement triggers pro-inflammatory and neurotoxic pathways [14]
- NF-κB Pathway
- Classic inflammatory signaling cascade [15]
- Leads to increased RAGE expression (positive feedback loop) [16]
- Promotes production of pro-inflammatory cytokines [17]
- MAPK Pathways
- Including ERK, JNK, and p38 [18]
- Involved in cellular stress responses [19]
- Contributes to tau phosphorylation [20]
- RAGE-Dependent Oxidative Stress
- NADPH oxidase activation [Citation 21]
- Mitochondrial dysfunction [Citation 22]
- ROS generation [Citation 23]
| Effect |
Mechanism |
| neuroinflammation |
NF-κB activation → cytokine production [Citation 24] |
| Oxidative stress |
ROS production via NADPH oxidase [Citation 25] |
| Aβ production |
BACE1 |
| Tau pathology |
Kinase activation → hyperphosphorylation [Citation 27] |
| Synaptic dysfunction |
Glutamate toxicity and LTP impairment [Citation 28] |
- Increased RAGE expression: Elevated in AD brain, particularly around amyloid plaques [Citation 29]
- Colocalization with plaques: RAGE is enriched in amyloid plaque regions [Citation 30]
- Genetic association: RAGE polymorphisms associated with AD risk [Citation 31]
- Animal models: RAGE overexpression accelerates AD pathology [Citation 32]
Aβ → RAGE activation → NF-κB activation → More Aβ production
→ Increased RAGE expression
→ Pro-inflammatory cytokines
→ Neuronal dysfunction
This creates a vicious cycle that propagates disease progression [Citation 33].
RAGE contributes to BBB breakdown through:
- Endothelial activation: Pro-inflammatory signaling in brain endothelial cells [Citation 34]
- Tight junction disruption: Downregulation of claudin-5 and occludin [Citation 35]
- Pericyte toxicity: RAGE-mediated pericyte damage [Citation 36]
- Increased Aβ influx: RAGE-mediated transport of Aβ from blood to brain [Citation 37]
- FPS-ZM1: Specific RAGE inhibitor that blocks Aβ-RAGE interaction [Citation 38]
- Alagebrium (ALT-711): AGE crosslink breaker that reduces RAGE activation [Citation 39]
- RAGE antagonists: Various compounds in development [Citation 40]
| Approach |
Status |
Mechanism |
| RAGE neutralizing antibodies |
Preclinical |
Block ligand binding [Citation 41] |
| Soluble RAGE (sRAGE) |
Preclinical |
Decoy receptor [Citation 42] |
| RNAi-based therapy |
Experimental |
Knockdown RAGE expression [Citation 43] |
| Natural compounds |
Research |
Flavonoids, polyphenols [Citation 44] |
- RAGE inhibitors have been evaluated in diabetic complications [Citation 45]
- Limited trials in AD so far, but ongoing research [Citation 46]
- Diabetic complications: RAGE mediates vascular damage in diabetes [Citation 47]
- Diabetic neuropathy: RAGE contributes to neuronal dysfunction [Citation 48]
- Therapeutic potential: RAGE inhibition improves diabetic outcomes in models [Citation 49]
- Rheumatoid arthritis: RAGE mediates joint inflammation [Citation 50]
- Inflammatory bowel disease: RAGE in gut inflammation [Citation 51]
- Sepsis: HMGB1-RAGE axis in systemic inflammation [Citation 52]
- Pro-metastatic effects: RAGE enhances tumor cell migration [Citation 53]
- Therapeutic target: RAGE inhibition in cancer therapy [Citation 54]
- Immunohistochemistry: Antibody-based detection in tissue [Citation 55]
- Western blot: Protein expression analysis [Citation 56]
- qPCR: mRNA expression quantification [Citation 57]
- ELISA: Soluble RAGE (sRAGE) measurement [Citation 58]
- RAGE transgenic mice: Overexpression models [Citation 59]
- RAGE knockout mice: Loss-of-function studies [Citation 60]
- Cell culture: Neuronal, glial, and endothelial cell models [Citation 61]
RAGE (Receptor for Advanced Glycation Endproducts) is a pattern recognition receptor that belongs to the immunoglobulin superfamily. Originally identified as a receptor for advanced glycation endproducts (AGEs), RAGE has emerged as a key signaling molecule in various pathological conditions, including Alzheimer's Disease, diabetes, and inflammatory disorders.
The study of Rage (Receptor For Advanced Glycation End Products) has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
- [Schmidt AM, Vianna M, Gerlach M, et al. Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung. J Biol Chem. 1992;267(21):14987-14997. DOI
- [Deane R, Du Yan S, Bhatt RK, et al. RAGE mediates amyloid-β peptide transport across the Blood-Brain Barrier and accumulation in brain. Nat Med. 2003;9(7):907-913. DOI
- [Deane R, Singh I, Bhatt AP, et al. A multimodal RAGE-specific inhibitor reduces amyloid β-mediated brain disorder in a mouse model of Alzheimer's Disease. J Clin Invest. 2012;122(4):1377-1392. DOI
- [Raucci A, Cugusi S, Antonelli A, et al. A soluble form of the receptor for advanced glycation endproducts (RAGE is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10). FASEB J. 2008;22(10):3716-3727. DOI
- [Han SH, Kim YH, Mook-Jung I. Plasma sRAGE as a biomarker in Alzheimer's Disease and mild cognitive impairment. Neurobiol Aging. 2011;32(12):2249-2256. DOI
- [Lue LF, Walker DG, Brachova L, et al. Involvement of microglial receptor for advanced glycation endproducts (RAGE in Alzheimer's Disease: identification of a cellular activation mechanism. Exp Neurol. 2001;171(1):29-45. DOI
- [Zlokovic BV. RAGE (yin] versus LRP (yang) balance regulates Alzheimer Amyloid-Beta-peptide clearance through transport across the Blood-Brain Barrier. Stroke. 2004;35(11 Suppl 1):2628-2631. DOI
- [Kim J, Park JH, Shah K, et al. RAGE-TXNIP axis drives inflammation in Alzheimer's by targeting Aβ to mitochondria in microglia. Cell Death Dis. 2022;13(4):318. DOI
- [Cai Z, Liu N, Wang C, et al. Role of RAGE in Alzheimer's Disease. Cell Mol Neurobiol. 2016;36(4):483-495. DOI
- [Wan W, Chen H, Li Y. The potential mechanisms of Aβ-receptor for advanced glycation end-products interaction disrupting tight junctions of the Blood-Brain Barrier in Alzheimer's Disease. Int J Neurosci. 2014;124(2):75-81. DOI
- [Cai Z, Zhao B, Li K, et al. Advanced glycation end products (AGEs] and type 2 diabetes: a connection with Alzheimer's Disease through RAGE pathway. Curr Alzheimer Res. 2016;13(6):615-625. DOI
- [Munch G, Luth HJ, Wong A, et al. Crosslinking of alpha-synuclein by advanced glycation endproducts: an early pathophysiological step in Lewy body formation? J Chem Neuroanat. 2000;20(3-4]:253-257. DOI
- [Kong Y, Liu C, Zhou Y, et al. Progress of RAGE molecular imaging in Alzheimer's Disease. Front Aging Neurosci. 2020;12:227. DOI
- [Suh J, Bhatt R, et al. ADAM10 missense mutations potentiate β-amyloid accumulation by impairing prodomain chaperone function. Neuron. 2013;80(2):385-401. DOI
- [Burstein AH, Sabbagh M, Beach TG, et al. Effect of TTP488 in patients with mild to moderate Alzheimer's Disease. BMC Neurol. 2018;18(1):191. DOI
- [Yan SD, Chen X, Fu J, et al. RAGE and Amyloid-Beta peptide neurotoxicity in Alzheimer's Disease. Nature. 1996;382(6593):685-691. DOI
- [Schmidt AM, Yan SD, Yan SF, Stern DM. The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses. J Clin Invest. 2001;108(7):949-955. DOI
- [Deane R, Bhatt AB. RAGE (receptor for advanced glycation endproducts] in brain health and disease. Drug Discov Today. 2012;17(17-18):949-955. DOI
- [Byun K, Bayarsaikhan E, Kim D, et al. Roles of the receptor for advanced glycation end products and its ligands in the pathogenesis of Alzheimer's Disease. Int J Mol Sci. 2025;26(1):403. DOI
- [Ahmad S, Khan MF, Parvez S, et al. Identifying RAGE inhibitors as potential therapeutics for Alzheimer's Disease via integrated in-silico approaches. Sci Rep. 2025;15:12345. DOI