Evidence map›Paper›PMID 33402098›Full record

ReviewCellular & molecular biology letters2021

Beyond K48 and K63: non-canonical protein ubiquitination.

Michal Tracz, Wojciech Bialek

Abstract readLetterReview
In one paragraph

Review in Cellular & molecular biology letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 210 papers.

0numbers the graph read from it
0cells of the map it votes in
210citing 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

210 citing papers in PubMed.

  1. Article
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  12. [Ubiquitination-mediated regulation of T cell homeostasis and autoimmune diseases].Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2026
    Review
  13. Article
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  15. Article
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  20. Ubiquitin-Specific Protease 49 Interacts with Bax to Modulate Apoptosis.International journal of molecular sciences · 2026
    Article

150 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.

Michal TraczFaculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.ORCID http://orcid.org/0000-0001-7510-5024
Wojciech BialekFaculty of Biotechnology, University of Wroclaw, Wroclaw, Poland. wojciech.bialek@uwr.edu.pl.ORCID http://orcid.org/0000-0002-3390-5450

Funding

Narodowe Centrum Nauki 2015/19/D/NZ1/02790
6 · The paper itself

Abstract

Protein ubiquitination has become one of the most extensively studied post-translational modifications. Originally discovered as a critical element in highly regulated proteolysis, ubiquitination is now regarded as essential for many other cellular processes. This results from the unique features of ubiquitin (Ub) and its ability to form various homo- and heterotypic linkage types involving one of the seven different lysine residues or the free amino group located at its N-terminus. While K48- and K63-linked chains are broadly covered in the literature, the other types of chains assembled through K6, K11, K27, K29, and K33 residues deserve equal attention in the light of the latest discoveries. Here, we provide a concise summary of recent advances in the field of these poorly understood Ub linkages and their possible roles in vivo.

Indexed as

UbiquitinationAnimalsDNA DamageHumansImmunity, InnateLysineNeurodegenerative DiseasesProteinsLysineProteinsAtypical ubiquitinationNon-canonicalUbiquitinUbiquitin chains

Identifiers

PMID33402098
PMCPMC7786512

What OpenQuestion holds

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Registered trials

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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.