ArticleJournal of molecular biology2011
Crystal structure of SUMO-modified proliferating cell nuclear antigen.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
18 citing papers in PubMed, 30 citations in OpenAlex.
- Dynamic Assemblies in Genome Maintenance.Advances in experimental medicine and biology · 2026Review
- Functional asymmetry in processivity clamp proteins.Biophysical journal · 2025Review
- Post-Translational Modifications of PCNA: Guiding for the Best DNA Damage Tolerance Choice.Journal of fungi (Basel, Switzerland) · 2022Review
- Conformational Flexibility of Ubiquitin-Modified and SUMO-Modified PCNA Shown by Full-Ensemble Hybrid Methods.Journal of molecular biology · 2018Article
- p15PAF binding to PCNA modulates the DNA sliding surface.Nucleic acids research · 2018Article
- Srs2 promotes synthesis-dependent strand annealing by disrupting DNA polymerase δ-extending D-loops.eLife · 2017Article
- Identification of New Mutations at the PCNA Subunit Interface that Block Translesion Synthesis.PloS one · 2016Article
- Structurally distinct ubiquitin- and sumo-modified PCNA: implications for their distinct roles in the DNA damage response.Structure (London, England : 1993) · 2015Article
- Crystallization and preliminary X-ray analysis of the C-type lectin domain of the spicule matrix protein SM50 from Strongylocentrotus purpuratus.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Distinct structural alterations in proliferating cell nuclear antigen block DNA mismatch repair.Biochemistry · 2013Article
- Readers of PCNA modifications.Chromosoma · 2013Review
- Regulation of PCNA-protein interactions for genome stability.Nature reviews. Molecular cell biology · 2013Review
- DNA polymerase delta in DNA replication and genome maintenance.Environmental and molecular mutagenesis · 2012Review
- SUMO Wrestles with Recombination.Biomolecules · 2012Article
- Article
- PCNA structure and function: insights from structures of PCNA complexes and post-translationally modified PCNA.Sub-cellular biochemistry · 2012Review
- Solution X-ray scattering combined with computational modeling reveals multiple conformations of covalently bound ubiquitin on PCNA.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Eukaryotic proliferating cell nuclear antigen (PCNA) is a replication accessory protein that functions in DNA replication, repair, and recombination. The various functions of PCNA are regulated by posttranslational modifications including mono-ubiquitylation, which promotes translesion synthesis, and sumoylation, which inhibits recombination. To understand how SUMO modification regulates PCNA, we generated a split SUMO-modified PCNA protein and showed that it supports cell viability and stimulates DNA polymerase δ activity. We then determined its X-ray crystal structure and found that SUMO occupies a position on the back face of the PCNA ring, which is distinct from the position occupied by ubiquitin in the structure of ubiquitin-modified PCNA. We propose that the back of PCNA has evolved to be a site of regulation that can be easily modified without disrupting ongoing reactions on the front of PCNA, such as normal DNA replication. Moreover, these modifications likely allow PCNA to function as a tool belt, whereby proteins can be recruited to the replication machinery via the back of PCNA and be held in reserve until needed.
Indexed as
Identifiers
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.