ArticlePloS one2013
Structural characterization of the self-association of the death domain of p75(NTR.).
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- High-affinity TrkA and p75 neurotrophin receptor complexes: A twisted affair.The Journal of biological chemistry · 2022Review
- Natural Products for Neurodegeneration: Regulating Neurotrophic Signals.Oxidative medicine and cellular longevity · 2021Review
- Revising the mechanism of p75NTR activation: intrinsically monomeric state of death domains invokes the "helper" hypothesis.Scientific reports · 2020Article
- Article
- Myelin-associated glycoprotein modulates apoptosis of motoneurons during early postnatal development via NgR/p75(NTR) receptor-mediated activation of RhoA signaling pathways.Cell death & disease · 2015Article
- NMR Dynamics of Transmembrane and Intracellular Domains of p75NTR in Lipid-Protein Nanodiscs.Biophysical journal · 2015Article
- Heterodimerization of p45-p75 modulates p75 signaling: structural basis and mechanism of action.PLoS biology · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The neurotrophin receptor p75(NTR) conveys multiple signals via its intracellular death domain. However, how the death domain is activated and interacts with downstream adaptors remains unclear. Here, we report two crystal structures of the p75(NTR) death domain in the form of a non-covalent asymmetric dimer and a Cys379-Cys379 disulfide bond linked symmetric dimer, respectively. These two dimer arrangements have not previously been observed in other death domain-containing proteins. Further analysis shows that both the Cys379-Cys379 disulfide linked and non-covalent full-length p75(NTR) dimers are present on the cell surface. These observations suggest that various oligomers may exist simultaneously on the cell surface, and that p75(NTR) activation and signalling may be modulated by neurotrophins or other factors via inducing a shift of the equilibrium between different oligomeric states.
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Registered trials
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