Evidence map›Paper›PMID 26185901›Full record

ReviewThe FEBS journal2015

Mapping the SUMOylated landscape.

Karolin Eifler, Alfred C O Vertegaal

Open access · hybridAbstract readReview
In one paragraph

Review in The FEBS journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

50 citing papers in PubMed, 85 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Karolin EiflerDepartment of Molecular Cell Biology, Leiden University Medical Center, Leiden, The Netherlands.
Alfred C O VertegaalDepartment of Molecular Cell Biology, Leiden University Medical Center, Leiden, The Netherlands.
Leiden University Medical Center · NL

Funding

European Research Council 310913
6 · The paper itself

Abstract

SUMOylation is a post-translational modification that regulates a multitude of cellular processes, including replication, cell-cycle progression, protein transport and the DNA damage response. Similar to ubiquitin, SUMO (small ubiquitin-like modifier) is covalently attached to target proteins in a reversible process via an enzymatic cascade. SUMOylation is essential for nearly all eukaryotic organisms, and deregulation of the SUMO system is associated with human diseases such as cancer and neurodegenerative diseases. Therefore, it is of great interest to understand the regulation and dynamics of this post-translational modification. Within the last decade, mass spectrometry analyses of SUMO proteomes have overcome several obstacles, greatly expanding the number of known SUMO target proteins. In this review, we briefly outline the basic concepts of the SUMO system, and discuss the potential of proteomic approaches to decipher SUMOylation patterns in order to understand the role of SUMO in health and disease.

Indexed as

SumoylationHumansLigasesPeptide HydrolasesProtein Processing, Post-TranslationalProteinsProteomicsSmall Ubiquitin-Related Modifier ProteinsLigasesPeptide HydrolasesProteinsSmall Ubiquitin-Related Modifier Proteinscross-talkgroup modificationmass spectrometrypost-translational modificationproteomicssite-specificsmall ubiquitin-like modifierSUMOubiquitin

Identifiers

PMID26185901
PMCPMC4869838
OpenAlexW1866623334

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.