Evidence map›Paper›PMID 33536622›Full record

ArticleNature2021

Ubiquitin ligation to F-box protein targets by SCF-RBR E3-E3 super-assembly.

Daniel Horn-Ghetko, David T Krist, J Rajan Prabu, Kheewoong Baek, Monique P C Mulder, Maren Klügel, Daniel C Scott, Huib Ovaa, Gary Kleiger, Brenda A Schulman

Open access · hybridAbstract read
In one paragraph

Article in Nature, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
12.3field-weighted citation impact, top 1% 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

112 citing papers in PubMed, 198 citations in OpenAlex.

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  18. E2 variants for probing E3 ubiquitin ligase activities.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  19. Article
  20. Design and Semisynthesis of Ubiquitin Extension Probes.Methods in molecular biology (Clifton, N.J.) · 2026
    Article

52 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

10 authors at 5 institutions in 3 countries.

Daniel Horn-GhetkoDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0003-2290-2147
David T KristDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.
J Rajan PrabuDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-7726-9310
Kheewoong BaekDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-6853-4936
Monique P C MulderOncode Institute, Department of Cell and Chemical Biology, Chemical Immunology, Leiden University Medical Centre, Leiden, The Netherlands.ORCID http://orcid.org/0000-0001-5386-7132
Maren KlügelDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.
Daniel C ScottDepartment of Structural Biology, St Jude Children's Research Hospital, Memphis, TN, USA.
Huib OvaaOncode Institute, Department of Cell and Chemical Biology, Chemical Immunology, Leiden University Medical Centre, Leiden, The Netherlands.ORCID http://orcid.org/0000-0002-0068-054X
Gary KleigerDepartment of Chemistry and Biochemistry, University of Nevada, Las Vegas, Las Vegas, NV, USA.
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany. schulman@biochem.mpg.de.ORCID http://orcid.org/0000-0002-3083-1126
Max Planck Institute of Biochemistry · DELeiden University · NLSt. Jude Children's Research Hospital · USIllinois College · USUniversity of Nevada, Las Vegas · US

Funding

Mechanisms for poly-ubiquitin chain initiation and elongationR15GM117555 · NIGMS · UNIVERSITY OF NEVADA LAS VEGAS · PI KLEIGER, GARY L. · 2015 to 2018
$785k
European Research Council 281699European Research Council 789016NIGMS NIH HHS R15 GM117555
6 · The paper itself

Abstract

E3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to recruited substrates

Indexed as

UbiquitinationAllosteric RegulationBiocatalysisCryoelectron MicroscopyCyclin EF-Box ProteinsHumansPhosphorylationSKP Cullin F-Box Protein LigasesSubstrate SpecificityUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesARIH1 protein, humanCyclin EF-Box ProteinsSKP Cullin F-Box Protein LigasesUBE2L3 protein, humanUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID33536622
PMCPMC7904520
OpenAlexW3129120649

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.