Evidence map›Paper›PMID 39456142›Full record

ArticleBiomolecules2024

A Bacterial Platform for Studying Ubiquitination Cascades Anchored by SCF-Type E3 Ubiquitin Ligases.

Zuo-Xian Pu, Jun-Li Wang, Yu-Yang Li, Luo-Yu Liang, Yi-Ting Tan, Ze-Hui Wang, Bao-Lin Li, Guang-Qin Guo, Li Wang, Lei Wu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Article
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.

Zuo-Xian PuMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.ORCID 0000-0003-4312-9181
Jun-Li WangMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.ORCID 0000-0001-6424-3747
Yu-Yang LiMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.
Luo-Yu LiangMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.
Yi-Ting TanMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.
Ze-Hui WangMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.
Bao-Lin LiMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.
Guang-Qin GuoMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.ORCID 0000-0001-6562-5130
Li WangSchool of Chemical Engineering Ocean and Life Science, Dalian University of Technology, Panjin 124221, China.ORCID 0000-0001-6567-2578
Lei WuMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.ORCID 0000-0002-1067-3095

Funding

Fundamental Research Funds for the Central Universities lzujbky-2023-22, lzujbky-2023-it20Natural Science Foundation of Gansu Province 22JR5RA462, 23JRRA1141
6 · The paper itself

Abstract

Ubiquitination is one of the most important post-translational modifications in eukaryotes. The ubiquitination cascade includes ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The E3 ligases, responsible for substrate recognition, are the most abundant and varied proteins in the cascade and the most studied. SKP1-CUL1-F-Box (SCF)-type E3 ubiquitin ligases are multi-subunit RING (Really Interesting New Gene) E3 ubiquitin ligases, composed of CUL1 (Cullin 1), RBX1 (RING BOX 1), SKP1 (S-phase Kinase-associated Protein 1), and F-box proteins. In vitro ubiquitination assays, used for studying the specific recognition of substrate proteins by E3 ubiquitin ligases, require the purification of all components involved in the cascade, and for assays with SCF-type E3 ligases, additional proteins (several SCF complex subunits). Here, the

Indexed as

Escherichia coliSKP Cullin F-Box Protein LigasesUbiquitinationCullin ProteinsHumansUbiquitin-Protein LigasesCullin 1Cullin ProteinsSKP Cullin F-Box Protein LigasesUbiquitin-Protein Ligasesauto-ubiquitination of TIR1AUX/IAAsco-expression recombinant proteinsdetection of ubiquitinationDuet expression system

Identifiers

PMID39456142
PMCPMC11505812

What Socratic 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 Socratic graph.