Evidence map›Paper›PMID 20208521›Full record

ArticleNature chemical biology2010

Chemically ubiquitylated PCNA as a probe for eukaryotic translesion DNA synthesis.

Junjun Chen, Yongxing Ai, Jialiang Wang, Lajos Haracska, Zhihao Zhuang

Abstract read
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In one paragraph

Article in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
7.8field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

70 citing papers in PubMed, 136 citations in OpenAlex.

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  19. Regulation of large and small G proteins by ubiquitination.The Journal of biological chemistry · 2019
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10 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Junjun ChenDepartment of Chemistry and Biochemistry, University of Delaware, Newark, Delaware, USA.
Yongxing Ai
Jialiang Wang
Lajos Haracska
Zhihao Zhuang
University of Delaware · USHungarian Academy of Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rapid growth in ubiquitin biology requires facile chemical approaches for protein ubiquitylation that can overcome the common problem of low yield faced by the enzymatic reaction catalyzed by ubiquitin ligases. We report a chemical approach for monoubiquitylation and SUMOylation of PCNA through disulfide exchange and intein chemistry. We used the chemically ubiquitylated and SUMOylated PCNAs in studying translesion DNA synthesis and revealed a surprising degree of flexibility of the ubiquitin modification.

Indexed as

CysteineDisulfidesDNADNA-Directed DNA PolymeraseEukaryotic CellsInteinsMolecular ProbesProliferating Cell Nuclear AntigenProtein BindingUbiquitinUbiquitinated ProteinsUbiquitinationUbiquitin-Protein LigasesCysteineDisulfidesDNADNA-Directed DNA PolymeraseMolecular ProbesProliferating Cell Nuclear AntigenUbiquitinUbiquitinated ProteinsUbiquitin-Protein Ligases

Identifiers

PMID20208521
OpenAlexW1996703055

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.