Evidence map›Paper›PMID 22101265›Full record

ReviewCell cycle (Georgetown, Tex.)2011

Insights into phosphorylation-dependent mechanisms regulating USP1 protein stability during the cell cycle.

Xiomaris M Cotto-Rios, Mathew J K Jones, Tony T Huang

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell cycle (Georgetown, Tex.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
  2. AKT and DUBs: a bidirectional relationship.Cellular & molecular biology letters · 2025
    Review
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  20. The Fanconi anemia pathway in replication stress and DNA crosslink repair.Cellular and molecular life sciences : CMLS · 2012
    Review
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

3 authors at 2 institutions in 1 country.

Xiomaris M Cotto-RiosDepartment of Biochemistry, New York University School of Medicine, New York, NY, USA.
Mathew J K Jones
Tony T Huang
New York University · USNew York Proton Center · US

Funding

Role of Deubiquitination in Fanconi Anemia Cancer Susceptibility PathwayR01GM084244 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUANG, TONY TUNG · 2009 to 2013
$2.3M
NIGMS NIH HHS R01 GM084244NIGMS NIH HHS R01-GM084244
6 · The paper itself

Abstract

Tight regulation of the cell cycle and DNA repair machinery is essential for maintaining genome stability. The APC/CCdh1 ubiquitin ligase complex is a key regulator of protein stability during the G 1 phase of the cell cycle. APC/CCdh1 regulates and promotes the degradation of proteins involved in both cell cycle regulation and DNA repair. In a recent study, we identified a novel APC/CCdh1 substrate, the ubiquitin protease USP1. USP1 is a critical regulator of both the Fanconi anemia (FA) and translesion synthesis (TLS) DNA repair pathways. Here, we provide additional mechanistic insights into the regulation of USP1 during the cell cycle. Specifically, we demonstrate that USP1 is phosphorylated in mitosis by cyclin-dependent kinases (Cdks), and that this phosphorylation event may prevent premature degradation of USP1 during normal cell cycle progression. Finally, we provide a unifying hypothesis integrating the role of G 1-specific proteolysis of USP1 with the regulation of the transcriptional repressors, Inhibitor of DNA-binding (ID) proteins.

Indexed as

G1 PhaseGene Expression Regulation, EnzymologicArabidopsis ProteinsCell Cycle ProteinsCyclin-Dependent KinasesDNA RepairEndopeptidasesEnzyme ActivationEnzyme StabilityF-Box ProteinsHumansMitosisPhosphorylationProteolysisUbiquitin-Specific ProteasesArabidopsis ProteinsCell Cycle ProteinsCyclin-Dependent KinasesEndopeptidasesF-Box ProteinsFBXO5 protein, humanUbiquitin-Specific ProteasesUSP1 protein, human

Identifiers

PMID22101265
PMCPMC3272283
OpenAlexW2080432816

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.