ArticleMolecular cell2012
Ubiquitin, SUMO, and phosphate: how a trio of posttranslational modifiers governs protein fate.
Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- A frameshift variant in specificity protein 1 triggers superactivation of Sp1-mediated transcription in familial bone marrow failure.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- SUMOylation in the control of cholesterol homeostasis.Open biology · 2020Review
- Yy1 regulates Senp1 contributing to AMPA receptor GluR1 expression following neuronal depolarization.Journal of biomedical science · 2019Article
- Suppression of Rac1 Signaling by Influenza A Virus NS1 Facilitates Viral Replication.Scientific reports · 2016Article
- Transcriptomics of Environmental Enrichment Reveals a Role for Retinoic Acid Signaling in Addiction.Frontiers in molecular neuroscience · 2016Article
- N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates.Molecular biology of the cell · 2013Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this issue of Molecular Cell, Guo et al. (2012) demonstrate how a series of sequential posttranslational modifications, phosphorylation, sumoylation, and ubiquitylation, cooperate to target human flap endonuclease FEN1 to degradation by the proteasome at the end of S phase.
Identifiers
22883623What 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.