Evidence map›Paper›PMID 30700555›Full record

ArticleThe Journal of biological chemistry2019

Replication protein A dynamically regulates monoubiquitination of proliferating cell nuclear antigen.

Mark Hedglin, Mahesh Aitha, Anthony Pedley, Stephen J Benkovic

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

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  10. Insights in Post-Translational Modifications: Ubiquitin and SUMO.International journal of molecular sciences · 2022
    Review
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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

4 authors at 1 institution in 1 country.

Mark HedglinFrom the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802 muh218@psu.edu.ORCID 0000-0003-2599-1691
Mahesh AithaFrom the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802.
Anthony PedleyFrom the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802.ORCID 0000-0003-1034-5072
Stephen J BenkovicFrom the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802.
Pennsylvania State University · US

Funding

PHOSPHATE ACTIVATION MECHANISMSR01GM013306 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI BENKOVIC, STEPHEN J · 1985 to 2022
$10.0M
NIGMS NIH HHS R01 GM013306
6 · The paper itself

Abstract

DNA damage tolerance permits bypass of DNA lesions encountered during S-phase and may be carried out by translesion DNA synthesis (TLS). Human TLS requires selective monoubiquitination of proliferating cell nuclear antigen (PCNA) sliding clamps encircling damaged DNA. This posttranslational modification (PTM) is catalyzed by Rad6/Rad18. Recent studies revealed that replication protein A (RPA), the major ssDNA-binding protein, is involved in the regulation of PCNA monoubiquitination and interacts directly with Rad18 on chromatin and in the nucleoplasm. However, it is unclear how RPA regulates this critical PTM and what functional role(s) these interactions serve. Here, we developed an

Indexed as

Protein Interaction MapsUbiquitinationDNA-Binding ProteinsDNA, Single-StrandedHumansProliferating Cell Nuclear AntigenReplication Protein AUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesDNA-Binding ProteinsDNA, Single-StrandedProliferating Cell Nuclear AntigenRAD18 protein, humanReplication Protein AUBE2A protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligasescell cycleDNA-binding proteinDNA damageDNA polymeraseDNA replicationE3 ubiquitin ligasePCNA monoubiquitinationposttranslational modification (PTM)proliferating cell nuclear antigen (PCNA)Rad6/Rad18replication protein A (RPA)sliding clamptranslesion DNA synthesis (TLS)ubiquitin-conjugating enzyme (E2 enzyme)ubiquitylation (ubiquitination)

Identifiers

PMID30700555
PMCPMC6442069
OpenAlexW2911650042

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.