Evidence map›Paper›PMID 24699079›Full record

ReviewNature structural & molecular biology2014

Lysine-targeting specificity in ubiquitin and ubiquitin-like modification pathways.

Francesca Mattiroli, Titia K Sixma

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing 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

109 citing papers in PubMed.

  1. Article
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  11. Synthesizing Defined Ubiquitin-Modified SUMO Dimers.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  12. Article
  13. Review
  14. Review
  15. Article
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  19. Glycation in the cardiomyocyte.Vitamins and hormones · 2024
    Review
  20. Article

49 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

2 authors.

Francesca Mattiroli1] Division of Biochemistry, Cancer Genomics Center, Netherlands Cancer Institute, Amsterdam, The Netherlands. [2].
Titia K SixmaDivision of Biochemistry, Cancer Genomics Center, Netherlands Cancer Institute, Amsterdam, The Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin and ubiquitin-like modifications are central to virtually all cellular signaling pathways. They occur primarily on lysine residues of target proteins and stimulate a large number of downstream signals. The diversity of these signals depends on the type, location and dynamics of the modification, but the role of the exact site of modification and the selectivity for specific lysines are poorly understood. Here we review the current literature on lysine specificity in these modifications, and we highlight the known signaling mechanisms and the open questions that pose future challenges to ubiquitin research.

Indexed as

Models, BiologicalHumansLysineSignal TransductionSmall Ubiquitin-Related Modifier ProteinsSubstrate SpecificityUbiquitinUbiquitinationUbiquitin-Protein LigasesLysineSmall Ubiquitin-Related Modifier ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID24699079

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.