Neurodegenerative diseases are characterized by the misfolding and aggregation of proteins, leading to the loss of neuronal function and eventually cell death.

Amyloid plaques are primarily composed of beta-amyloid peptide, which forms aggregates that are toxic to neurons.

Lewy bodies are a hallmark of Parkinson's disease and contain aggregates of alpha-synuclein protein.

Huntington's disease is caused by an expansion of the CAG trinucleotide repeat in the HTT gene, leading to the production of a mutant huntingtin protein.

Neurofibrillary tangles are composed primarily of hyperphosphorylated tau protein, which aggregates and disrupts neuronal function.

ALS is characterized by a combination of excitotoxicity, oxidative stress, and mitochondrial dysfunction, leading to neuronal damage and motor neuron loss.

Mutations in the SOD1 gene, encoding superoxide dismutase 1, are associated with a familial form of ALS.

Prions are misfolded proteins that can transmit disease by converting normal proteins into their misfolded form, leading to neurodegeneration.

TDP-43 protein aggregates are a hallmark of ALS and are also found in other neurodegenerative diseases.

Chaperone proteins play a crucial role in preventing protein misfolding, assisting in protein folding, and degrading misfolded proteins.

Huntington's disease is caused by an expansion of CAG trinucleotide repeats in the HTT gene, leading to the production of a mutant huntingtin protein with polyglutamine repeats.

Oxidative stress can damage cellular components, contribute to neuronal death, lead to the formation of misfolded proteins, and disrupt mitochondrial function.

Alpha-synuclein aggregates are a hallmark of Parkinson's disease and are found in Lewy bodies.

Inflammation can contribute to neuronal damage and cell death, activate microglia and astrocytes leading to the release of toxic molecules, and disrupt the blood-brain barrier.

Tau protein aggregates are a hallmark of Alzheimer's disease and are found in neurofibrillary tangles.