NMR structure of a full‐length single‐pass membrane protein NRADD-Reference-Cited by-同舟云学术

NMR structure of a full‐length single‐pass membrane protein NRADD

Published:2019-05-11 Issue:9 Volume:87 Page:786-790
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Nadezhdin Kirill D.¹²^ORCID,Goncharuk Sergey A.¹,Arseniev Aleksander S.¹²,Mineev Konstantin S.¹²

Affiliation:

1. Laboratory of biomolecular NMR spectroscopyShemyakin—Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences Moscow Russia

2. Department of biological and medical physicsMoscow Institute of Physics and Technology Dolgoprudny Russia

Funder

Russian Science Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.25703

Reference22 articles.

1. PLAIDD,a Type II Death Domain Protein that Interacts with p75 Neurotrophin Receptor

2. Release of a membrane-bound death domain by γ-secretase processing of the p75NTR homolog NRADD

3. A Novel p75 Neurotrophin Receptor-Related Protein, NRH2, Regulates Nerve Growth Factor Binding to the TrkA Receptor

4. The Neurotrophin Receptor Homolog-2 regulates Nerve Growth Factor signaling.

5. NRH2 is a trafficking switch to regulate sortilin localization and permit proneurotrophin-induced cell death

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3. A selective degeneration of cholinergic neurons mediated by NRADD in an Alzheimer's disease mouse model;Cell Insight;2022-12

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