ArticleThe EMBO journal2004
Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.
Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 77 citations in OpenAlex.
- The PINK1-VCP-p47 pathway protects against tau-induced dendritic shrinkage in cortical neurons through interaction with STIP1.Neurobiology of disease · 2026Article
- Plant UBX domain-containing proteins use distinct strategies to stably engage the unfoldase CDC48A.Plant & cell physiology · 2026Article
- Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy.The Biochemical journal · 2025Review
- AAA+ ATPase chaperone p97/VCPNature communications · 2024Article
- p37 regulates VCP/p97 shuttling and functions in the nucleus and cytosol.Science advances · 2024Article
- The SPATA5-SPATA5L1 ATPase complex directs replisome proteostasis to ensure genome integrity.Cell · 2024Article
- Exploring the role of ubiquitin regulatory X domain family proteins in cancers: bioinformatics insights, mechanisms, and implications for therapy.Journal of translational medicine · 2024Review
- Deubiquitinases in cancer.Nature reviews. Cancer · 2023Review
- Cooperative assembly of p97 complexes involved in replication termination.Nature communications · 2022Article
- In silico prediction, characterization, docking studies and molecular dynamics simulation of human p97 in complex with p37 cofactor.BMC molecular and cell biology · 2022Article
- Article
- Conserved L464 in p97 D1-D2 linker is critical for p97 cofactor regulated ATPase activity.The Biochemical journal · 2021Article
- Structural and Functional Analysis of Disease-Linked p97 ATPase Mutant Complexes.International journal of molecular sciences · 2021Article
- Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins.Computational and structural biotechnology journal · 2021Review
- An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cdc48 cofactor Shp1 regulates signal-induced SCFProceedings of the National Academy of Sciences of the United States of America · 2020Article
- p47 licenses activation of the immune deficiency pathway in the tickProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Multiple UBXN family members inhibit retrovirus and lentivirus production and canonical NFκΒ signaling by stabilizing IκBα.PLoS pathogens · 2017Article
- UBXD Proteins: A Family of Proteins with Diverse Functions in Cancer.International journal of molecular sciences · 2016Review
- Altered cofactor regulation with disease-associated p97/VCP mutations.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The principal role of the p97-p47 complex is in regulation of membrane fusion events. Mono-ubiquitin recognition by p47 has also been shown to be crucial in the p97-p47-mediated Golgi membrane fusion events. Here, we describe the high-resolution solution structures of the N-terminal UBA domain and the central domain (SEP) from p47. The p47 UBA domain has the characteristic three-helix bundle fold and forms a highly stable complex with ubiquitin. We report the interaction surfaces of the two proteins and present a structure for the p47 UBA-ubiquitin complex. The p47 SEP domain adopts a novel fold with a betabetabetaalphaalphabeta secondary structure arrangement, where beta4 pairs in a parallel fashion to beta1. Based on biophysical studies, we demonstrate a clear propensity for the self-association of p47. Furthermore, p97 N binding abolishes p47 self-association, revealing the potential interaction surfaces for recognition of other domains within p97 or the substrate.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.