complex(GO:axon)

Entity

Name

axon

Namespace

go

Namespace Version

20180921

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

TAU Interactions Section of NESTOR

Tau Modifications Sections of NESTOR

Tau protein plays a role in the extension and maintenance of neuronal processes through a direct association with microtubules. It is found in the axonal microtubules of mature neurons (Binder et al ., 1985) and in the axonlike elongated neurite processes synthesized by differentiating neurons in culture. To address this issue, three different tau protein fragments were synthesized in vitro: (a) the tau protein repeat domain (residues 237 to 367); (b) the amino terminal half of tau protein (residues 1-237) ; and (c) the carboxy terminal nonrepeat domain of tau protein (residues 358 to 430). From these results, we conclude the repeat domain contributes most of the binding energy for microtubules. PubMed:1918161

Several lines of evidence in other tauopathies suggest that tau oligomer formation induces neurotoxicity and that tau oligomer-mediated neurotoxicity involves induction of axonal dysfunction through exposure of an N-terminal motif in tau, the phosphatase-activating domain (PAD). PubMed:26671985

Several lines of evidence in other tauopathies suggest that tau oligomer formation induces neurotoxicity and that tau oligomer-mediated neurotoxicity involves induction of axonal dysfunction through exposure of an N-terminal motif in tau, the phosphatase-activating domain (PAD). PubMed:26671985

Several lines of evidence in other tauopathies suggest that tau oligomer formation induces neurotoxicity and that tau oligomer-mediated neurotoxicity involves induction of axonal dysfunction through exposure of an N-terminal motif in tau, the phosphatase-activating domain (PAD). PubMed:26671985

Tau protein plays a role in the extension and maintenance of neuronal processes through a direct association with microtubules. It is found in the axonal microtubules of mature neurons (Binder et al ., 1985) and in the axonlike elongated neurite processes synthesized by differentiating neurons in culture. To address this issue, three different tau protein fragments were synthesized in vitro: (a) the tau protein repeat domain (residues 237 to 367); (b) the amino terminal half of tau protein (residues 1-237) ; and (c) the carboxy terminal nonrepeat domain of tau protein (residues 358 to 430). From these results, we conclude the repeat domain contributes most of the binding energy for microtubules. PubMed:1918161

Several lines of evidence in other tauopathies suggest that tau oligomer formation induces neurotoxicity and that tau oligomer-mediated neurotoxicity involves induction of axonal dysfunction through exposure of an N-terminal motif in tau, the phosphatase-activating domain (PAD). PubMed:26671985