Tau protein promotes microtubule assembly and stability. Tau is abundant in neurons of the central nervous system, and is expressed at low levels in astrocytes and oligodendrocytes. Abnormal hyperphosphorylation, aggregation, and toxic gain of function of tau is associated with several neurological disorders, including Alzheimer’s disease (AD). The major building block of neurofibrillary lesions in AD brains consists of paired helical filaments (PHFs) of abnormally hyperphosphorylated tau. Six isoforms of tau are generated by alternative splicing of the MAPT gene. These isoforms are distinguished by the number of tubulin binding domains, 3 (3R) or 4 (4R), in the C-terminal of the protein and by one (1N), two (2N), or no (0N) inserts in the N-terminal domain.  Tau isoforms are differentially expressed during development.

Dystroglycan is a central component of dystrophin-glycoprotein complex that is encoded by the DAG1 gene. Dystroglycan links the cytoskeletal structure to the extracellular matrix. Dystroglycan is proteolytically cleaved to 2 functional peptides, α- and β-dystroglycan. β-dystroglycan is a transmembrane protein, which acts as a cell adhesion receptor in human tissues. The interactions between β-dystroglycan and dystrophin and Utrophin scaffolds axin to the cytoskeleton. β-dystroglycan has also been reported to play a role in cell adhesion-mediated signaling and is implicated in cell polarity.

Dystroglycan is a central component of dystrophin-glycoprotein complex that is encoded by the DAG1 gene. Dystroglycan links the cytoskeletal structure to the extracellular matrix. Dystroglycan is proteolytically cleaved to 2 functional peptides, α- and β-dystroglycan. β-dystroglycan is a transmembrane protein, which acts as a cell adhesion receptor in human tissues. The interactions between β-dystroglycan and dystrophin and Utrophin scaffolds axin to the cytoskeleton. β-dystroglycan has also been reported to play a role in cell adhesion-mediated signaling and is implicated in cell polarity.

Alpha-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy. Phosphorylation of α-synuclein at Tyr39 may modulate clearance of the protein and contribute to Parkinson’s disease.

Alpha-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy. Phosphorylation of α-synuclein at Tyr39 may modulate clearance of the protein and contribute to Parkinson’s disease.

α-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including  the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, a-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.

α-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including  the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, a-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.

α-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including  the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, a-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.

α-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including  the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, a-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.

Microtubule-associated protein light chain 3, commonly known as LC3, is a central protein in the autophagy pathway and functions in autophagosome biogenesis. LC3 is a member of the ATG8 protein family and expressed as three isoforms: LC3A (MAP1LC3A), LC3B (MAP1LC3B), and LC3C (MAP1LC3C). Newly synthesized LC3 is hydrolyzed by the cysteine protease ATG4B to produce the active cytosolic form termed LC3I. Through a series of reactions involving other ATGs, LC3I becomes attached to phosphatidylethanolamine. This lipid modified form is termed LC3II, and is involved in autophagosomes membrane expansion and fusion events. LC3 is widely used as a marker for autophasomes. Defects in autophagy machinery have been associated with multiples diseases including neurodegenerative disorders.

Microtubule-associated protein light chain 3, commonly known as LC3, is a central protein in the autophagy pathway and functions in autophagosome biogenesis. LC3 is a member of the ATG8 protein family and expressed as three isoforms: LC3A (MAP1LC3A), LC3B (MAP1LC3B), and LC3C (MAP1LC3C). Newly synthesized LC3 is hydrolyzed by the cysteine protease ATG4B to produce the active cytosolic form termed LC3I. Through a series of reactions involving other ATGs, LC3I becomes attached to phosphatidylethanolamine. This lipid modified form is termed LC3II, and is involved in autophagosomes membrane expansion and fusion events. LC3 is widely used as a marker for autophasomes. Defects in autophagy machinery have been associated with multiples diseases including neurodegenerative disorders.

α-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including  the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, a-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-Synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.

α-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including  the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, a-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-Synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.

Neurogranin (NRGN) is the main post-synaptic protein kinase substrate that binds to calmodulin (CaM) in the absence of calcium. It is suggested that NRGN is a direct target for thyroid hormone in the human brain, and that the control of expression of this gene could underlay many of the consequences of hypothyroidism on mental states during development as well as in adult subjects. Neurogranin in CSF has been implicated as a possible marker for synaptic degeneration in Alzheimer’s disease.

Neurogranin (NRGN) is the main post-synaptic protein kinase substrate that binds to calmodulin (CaM) in the absence of calcium. It is suggested that NRGN is a direct target for thyroid hormone in the human brain, and that the control of expression of this gene could underlay many of the consequences of hypothyroidism on mental states during development as well as in adult subjects. Neurogranin in CSF has been implicated as a possible marker for synaptic degeneration in Alzheimer’s disease.

Alpha-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy. Phosphorylation of α-synuclein at Tyr39 may modulate clearance of the protein and contribute to Parkinson's disease.

Alpha-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy. Phosphorylation of α-synuclein at Tyr39 may modulate clearance of the protein and contribute to Parkinson's disease.

Alpha-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.

Alpha-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.

Alpha-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.