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Appears in Networks 3

Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system v1.0.0

This document contains the curation of the review article Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system by Taly et al. 2009

Tau Biochemistry v1.2.5

Tau Biochemistry Section of NESTOR

In-Edges 3

p(HGNC:CHRNB2) association p(HGNCGENEFAMILY:Tubulins) View Subject | View Object

The cytoplasmic domain of the alpha4 nAChR subunit binds the scaffold protein 14-3-3η and the Ca2+ sensor visinin-like protein 1 (ReF. 69), and the beta2 subunit interacts with several cytoskeletal proteins, such as tubulin, dynamin and clathrin, and with G protein systems that are involved in intracellular signalling pathways70. PubMed:19721446

act(p(HGNC:HTRA1)) increases deg(p(HGNCGENEFAMILY:Tubulins)) View Subject | View Object

Tubulin was later identified as a substrate for HTRA1, suggesting HTRA1 may be involved in mediating microtubule function (42, 43). A more recent study showed that HTRA1 can cleave recombinant tau in vitro into multiple fragments of varying sizes, and furthermore can degrade insoluble and fibrillarized tau (16). PubMed:24027553

Out-Edges 1

p(HGNCGENEFAMILY:Tubulins) association p(HGNC:CHRNB2) View Subject | View Object

The cytoplasmic domain of the alpha4 nAChR subunit binds the scaffold protein 14-3-3η and the Ca2+ sensor visinin-like protein 1 (ReF. 69), and the beta2 subunit interacts with several cytoskeletal proteins, such as tubulin, dynamin and clathrin, and with G protein systems that are involved in intracellular signalling pathways70. PubMed:19721446

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.