Structure and dynamics of human Nedd4-1 WW3 in complex with the αENaC PY motif-Reference-Cited by-同舟云学术

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Structure and dynamics of human Nedd4-1 WW3 in complex with the αENaC PY motif

Published:2013-08 Issue:8 Volume:1834 Page:1632-1641
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Bobby Romel,Medini Karima,Neudecker Philipp,Lee Tet Verne,Brimble Margaret A.,McDonald Fiona J.,Lott J. Shaun,Dingley Andrew J.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference82 articles.

1. The ubiquitin code;Komander;Annu. Rev. Biochem.,2012

2. Role of the ubiquitin system in regulating ion transport;Rotin;Pflugers Arch.,2011

3. The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture;Ingham;Oncogene,2004

4. Identification of a set of genes with developmentally down-regulated expression in the mouse brain;Kumar;Biochem. Biophys. Res. Commun.,1992

5. WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome;Staub;EMBO J.,1996

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1. Ion channel inhibition by targeted recruitment of NEDD4-2 with divalent nanobodies;2024-05-31

2. Nedd4-1 regulates human sodium-dependent vitamin C transporter-2 functional expression in neuronal and epithelial cells;The Journal of Nutritional Biochemistry;2023-10

3. Phage display identification of nanomolar ligands for human NEDD4-WW3: Energetic and dynamic implications for the development of broad-spectrum antivirals;International Journal of Biological Macromolecules;2022-05

4. Predicting PY motif-mediated protein-protein interactions in the Nedd4 family of ubiquitin ligases;PLOS ONE;2021-10-12

5. Bioinformatic and computational analysis reveals the prevalence and nature of PY motif-mediated protein-protein interactions in the Nedd4 family of ubiquitin ligases;2020-11-12

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