Evidence map›Paper›PMID 30362419›Full record

ReviewCurrent drug targets2019

Developing Practical Therapeutic Strategies that Target Protein SUMOylation.

Olivia F Cox, Paul W Huber

Abstract readReview
In one paragraph

Review in Current drug targets, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Annals of translational medicine · 2022
    Article
  5. Review
  6. Article
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

2 authors.

Olivia F CoxDepartment of Chemistry and Biochemistry, Harper Cancer Research Institute, Center for Stem Cells and Regenerative Medicine, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Paul W HuberDepartment of Chemistry and Biochemistry, Harper Cancer Research Institute, Center for Stem Cells and Regenerative Medicine, University of Notre Dame, Notre Dame, Indiana 46556, United States.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modification by small ubiquitin-like modifier (SUMO) has emerged as a global mechanism for the control and integration of a wide variety of biological processes through the regulation of protein activity, stability and intracellular localization. As SUMOylation is examined in greater detail, it has become clear that the process is at the root of several pathologies including heart, endocrine, and inflammatory disease, and various types of cancer. Moreover, it is certain that perturbation of this process, either globally or of a specific protein, accounts for many instances of congenital birth defects. In order to be successful, practical strategies to ameliorate conditions due to disruptions in this post-translational modification will need to consider the multiple components of the SUMOylation machinery and the extraordinary number of proteins that undergo this modification.

Indexed as

AnimalsHumansMolecular Targeted TherapySignal TransductionSmall Ubiquitin-Related Modifier ProteinsSumoylationSmall Ubiquitin-Related Modifier Proteinscancercongenital birth defectsheart developmentheart failureneural tubeneurodegenerative diseaseSENP proteasespina bifida.SUMOSUMO ligase

Identifiers

PMID30362419
PMCPMC6700758

What OpenQuestion holds

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LicenceCC BY-NC
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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.