Evidence map›Paper›PMID 21554755›Full record

ReviewGenome biology2011

The cullin protein family.

Antonio Sarikas, Thomas Hartmann, Zhen-Qiang Pan

Open access · bronzeAbstract readReview
In one paragraph

Review in Genome biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 326 papers.

0numbers the graph read from it
0cells of the map it votes in
326citing papers in PubMed
12.9field-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

326 citing papers in PubMed, 505 citations in OpenAlex.

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  20. Adipose cullin 3 mediates the antiobesity effect of pan neddylation inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

266 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

3 authors at 2 institutions in 2 countries.

Antonio SarikasInstitute of Pharmacology and Toxicology, Technische Universität München, 80802 Munich, Germany. sarikas@ipt.med.tum.de
Thomas Hartmann
Zhen-Qiang Pan
Technical University of Munich · DEIcahn School of Medicine at Mount Sinai · US

Funding

Studies on ROC1-dependent Ubiquitin E3 LigasesR01GM061051 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI PAN, ZHEN-QIANG · 2002 to 2014
$3.4M
The function and regulation of the cullin family E3 ubiquitin ligasesR01CA095634 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI PAN, ZHEN-QIANG · 2003 to 2012
$2.7M
NCI NIH HHS CA095634NCI NIH HHS R01 CA095634NIGMS NIH HHS GM61051NIGMS NIH HHS R01 GM061051
6 · The paper itself

Abstract

Cullin proteins are molecular scaffolds that have crucial roles in the post-translational modification of cellular proteins involving ubiquitin. The mammalian cullin protein family comprises eight members (CUL1 to CUL7 and PARC), which are characterized by a cullin homology domain. CUL1 to CUL7 assemble multi-subunit Cullin-RING E3 ubiquitin ligase (CRL) complexes, the largest family of E3 ligases with more than 200 members. Although CUL7 and PARC are present only in chordates, other members of the cullin protein family are found in Drosophila melanogaster, Caenorhabditis elegans, Arabidopsis thaliana and yeast. A cullin protein tethers both a substrate-targeting unit, often through an adaptor protein, and the RING finger component in a CRL. The cullin-organized CRL thus positions a substrate close to the RING-bound E2 ubiquitin-conjugating enzyme, which catalyzes the transfer of ubiquitin to the substrate. In addition, conjugation of cullins with the ubiquitin-like molecule Nedd8 modulates activation of the corresponding CRL complex, probably through conformational regulation of the interactions between cullin's carboxy-terminal tail and CRL's RING subunit. Genetic studies in several model organisms have helped to unravel a multitude of physiological functions associated with cullin proteins and their respective CRLs. CRLs target numerous substrates and thus have an impact on a range of biological processes, including cell growth, development, signal transduction, transcriptional control, genomic integrity and tumor suppression. Moreover, mutations in CUL7 and CUL4B genes have been linked to hereditary human diseases.

Indexed as

AnimalsCullin ProteinsHumansMultigene FamilyPhylogenyProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalUbiquitinUbiquitinationUbiquitin-Protein LigasesYeastsCullin ProteinsProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID21554755
PMCPMC3218854
OpenAlexW2149931676

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.