Receptor for Advanced Glycation End products (RAGE) has been implicated in amyloid β-peptide (Aβ)-induced perturbation relevant to the pathogenesis
RAGE was also shown to mediate the transport of Ab across the blood–brain barrier (BBB) (Deane et al. 2003). The binding of soluble Aβ to soluble RAGE inhibits further aggregation of Aβ peptides, while membrane bound RAGE-Aβ interactions elicit activation of the NF-κB transcription factor promoting sustained chronic neuroinflammation. Atomic force microscopy observations demonstrated that the N-terminal domain of RAGE, by interacting with Aβ, is a powerful inhibitor of Aβ polymerization even at prolonged periods of incubation. Hence, the potential RAGE-Aβ structural interactions were further explored utilizing a series of computational chemistry algorithms. Our modeling suggests that a soluble dimeric RAGE assembly creates a positively charged well into which the negative charges of the N-terminal domain of dimeric Aβ dock.

By virtue of being a transmembrane protein, isolated RAGE is a very insoluble molecule. However, soluble RAGE (sRAGE) can also be produced by recombinant DNA. This molecule, in which the transmembrane domain and cytosolic regions are missing, contains the extracellular V, C and C' Ig-like regions up to residue 342 and conserves all the binding properties of native RAGE.
 Interception of Aβ interaction with RAGE, by infusion of soluble RAGE, decreases Aβ content and amyloid load
when amyloid-β clumps together to form deposits in the brain, it triggers neurodegenerative processes that lead to the loss of memory and cognitive ability that is observed in Alzheimer's disease
 Amyloid deposits can build up in the heart, brain, kidneys, spleen and other parts of the body.
Amyloid beta peptide binding to the receptor for advanced glycation end products (RAGE) is an important microglial activation mechanism
RAGE has been shown to mediate Aβ transport across the BBB and to contribute to pathologic accumulation of the amyloid peptide
Trimers [RAGE Human]2-PeptideN

RAGE polymorphism influences amyloid-RAGE interactions relevant in Alzheimer's disease pathology.
RAGE polymorphism influences amyloid-RAGE interactions relevant in Alzheimer's disease pathology.
Tetramers [RAGE Human]2-[PeptideN]2

RAGE polymorphism influences amyloid-RAGE interactions relevant in Alzheimer's disease pathology.
Receptor for Advanced Glycation End products (RAGE) has been implicated in amyloid β-peptide (Aβ)-induced perturbation relevant to the pathogenesis
[Amyloids(1-19)]2

Receptor for Advanced Glycation End products (RAGE) has been implicated in amyloid β-peptide (Aβ)-induced perturbation relevant to the pathogenesis
Receptor for Advanced Glycation End products (RAGE) has been implicated in amyloid β-peptide (Aβ)-induced perturbation relevant to the pathogenesis
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