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 hyper-phosphorylation, 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.

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 hyper phosphorylation, 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.

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 hyper phosphorylation, 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.

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 hyper-phosphorylation, 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.

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 hyper-phosphorylation, 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.

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.

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.

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 hyper-phosphorylation, 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.

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 hyper-phosphorylation, 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.

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 hyper phosphorylation, 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.

 

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 hyper phosphorylation, 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.

 

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 hyper-phosphorylation, 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.

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 hyper-phosphorylation, 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.

Myelin basic protein (MBP) is a protein involved in the myelination of nerves in the central nervous system (CNS). MBP functions to maintain the correct structure of myelin, through its interaction with the lipids in the myelin membrane. The myelin sheath is made up of MBP and lipids, and acts as an insulator to increase the velocity of axonal impulse conduction. MBP plays a central role in the demyelinating disease multiple sclerosis (MS). A hallmark of the disease is the loss of the myelin sheath surrounding nerves, thought to be induced by antibodies against MBP.

Myelin basic protein (MBP) is a protein involved in the myelination of nerves in the central nervous system (CNS). MBP functions to maintain the correct structure of myelin, through its interaction with the lipids in the myelin membrane. The myelin sheath is made up of MBP and lipids, and acts as an insulator to increase the velocity of axonal impulse conduction. MBP plays a central role in the demyelinating disease multiple sclerosis (MS). A hallmark of the disease is the loss of the myelin sheath surrounding nerves, thought to be induced by antibodies against MBP.

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 hyper-phosphorylation, 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.

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 hyper-phosphorylation, 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.

TFAM (Transcription Factor A, Mitochondrial) binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation, and DNA replication and repair. The protein is required for accurate and efficient promoter recognition by mitochondrial RNA polymerase. Sequence polymorphisms in the TFAM gene are associated with Alzheimer's and Parkinson's diseases. Other diseases associated with TFAM include Mitochondrial DNA Depletion Syndrome, Hepatocerebral Form and Deoxyguanosine Kinase Deficiency.

TFAM (Transcription Factor A, Mitochondrial) binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation, and DNA replication and repair. The protein is required for accurate and efficient promoter recognition by mitochondrial RNA polymerase. Sequence polymorphisms in the TFAM gene are associated with Alzheimer's and Parkinson's diseases. Other diseases associated with TFAM include Mitochondrial DNA Depletion Syndrome, Hepatocerebral Form and Deoxyguanosine Kinase Deficiency.

TFAM (Transcription Factor A, Mitochondrial) binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation, and DNA replication and repair. The protein is required for accurate and efficient promoter recognition by mitochondrial RNA polymerase. Sequence polymorphisms in the TFAM gene are associated with Alzheimer's and Parkinson's diseases. Other diseases associated with TFAM include Mitochondrial DNA Depletion Syndrome, Hepatocerebral Form and Deoxyguanosine Kinase Deficiency.