Evidence map›Paper›PMID 33643814›Full record

ReviewActa pharmaceutica Sinica. B2021

Phosphorylation regulates cullin-based ubiquitination in tumorigenesis.

Yifan Chen, Xuejing Shao, Ji Cao, Hong Zhu, Bo Yang, Qiaojun He, Meidan Ying

Open access · diamondAbstract readReview
In one paragraph

Review in Acta pharmaceutica Sinica. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

50 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
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  15. COPS5 is Essential for Sertoli Cell Function and Male Fertility in Mice.bioRxiv : the preprint server for biology · 2025
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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

7 authors at 1 institution in 1 country.

Yifan ChenZhejiang Province Key Laboratory of Anti-Cancer Drug Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Xuejing ShaoZhejiang Province Key Laboratory of Anti-Cancer Drug Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Ji CaoZhejiang Province Key Laboratory of Anti-Cancer Drug Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Hong ZhuZhejiang Province Key Laboratory of Anti-Cancer Drug Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Bo YangZhejiang Province Key Laboratory of Anti-Cancer Drug Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Qiaojun HeZhejiang Province Key Laboratory of Anti-Cancer Drug Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Meidan YingZhejiang Province Key Laboratory of Anti-Cancer Drug Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cullin-RING ligases (CRLs) recognize and interact with substrates for ubiquitination and degradation, and can be targeted for disease treatment when the abnormal expression of substrates involves pathologic processes. Phosphorylation, either of substrates or receptors of CRLs, can alter their interaction. Phosphorylation-dependent ubiquitination and proteasome degradation influence various cellular processes and can contribute to the occurrence of various diseases, most often tumorigenesis. These processes have the potential to be used for tumor intervention through the regulation of the activities of related kinases, along with the regulation of the stability of specific oncoproteins and tumor suppressors. This review describes the mechanisms and biological functions of crosstalk between phosphorylation and ubiquitination, and most importantly its influence on tumorigenesis, to provide new directions and strategies for tumor therapy.

Indexed as

AIRE, autoimmune regulatorAKT, AKT serine/threonine kinaseATR, ataxia telangiectasia-mutated and Rad3-relatedBCL2, BCL2 apoptosis regulatorBMAL1, aryl hydrocarbon receptor nuclear translocator likeCDK2/4, cyclin dependent kinase 2/4CDT2, denticleless E3 ubiquitin protein ligase homologc-Fos, Fos proto-oncogene, AP-1 transcription factor subunitCHK1, checkpoint kinase 1Ci, cubitus interruptusCK1/2, casein kinase I/IICLOCK, clock circadian regulatorCOMMD1, copper metabolism domain containing 1CRL, cullin-RING ligaseCrosstalkCRY1, cryptochrome circadian regulator 1CSN, COP9 signalosomeCullin-RING ligasesDDB1, damage specific DNA binding protein 1DegradationDYRK1A/B, dual-specificity tyrosine-phosphorylation-regulated kinases 1A/BEMT, epithelial–mesenchymal transitionERG, ETS transcription factor ERGERK, mitogen-activated protein kinase 1EXO1, exonuclease 1FBW7, F-box and WD repeat domain containing 7FBXL3, F-box and leucine rich repeat proteinFBXO3/31, F-box protein 3/31FZR1, fizzy and cell division cycle 20 related 1HCC, hepatocellular carcinomasHIB, Hedghog-induced MATH and BTB domain-containing proteinHIF1α, NF-κB and hypoxia inducible factor 1 subunit alphaID2, inhibitor of DNA binding 2JAB1, c-Jun activation domain binding protein-1KBTBD8, kelch repeat and BTB domain containing 8KDM2B, lysine demethylase 2BKEAP1, kelch like ECH associated protein 1KinasesKLHL3, kelch like family member 3KRAS, KRAS proto-oncogene, GTPaseMYC, MYC proto-oncogene, bHLH transcription factorNEDD8, NEDD8 ubiquitin like modifierNOLC1, nucleolar and coiled-body phosphoprotein 1NRF2, nuclear factor, erythroid 2 like 2p130Cas, BCAR1 scaffold protein, Cas family memberPDL1, programmed death ligand 1PhosphorylationPKC, protein kinase CPKM2, pyruvate kinase M2 isoformP-TEFb, positive transcription elongation factor bPYGO2, pygopus 2RA, retinoic acidRARα, RA receptor αRRM2, ribonucleotide reductase regulatory subunit M2SNAIL1, snail family transcriptional repressor 1SOCS6, suppressor of cytokine signaling 6SPOP, speckle-type POZ proteinSRC-3, nuclear receptor coactivator 3Targeted therapyTCN, triciribine hydrateTCOF1, treacle ribosome biogenesis factor 1TRF1, telomeric repeat binding factor 1TumorigenesisUbiquitinationUSP37, ubiquitin specific peptidase 37VHL, von Hippel-Lindau tumor suppressorVps34, phosphatidylinositol 3-kinase catalytic subunit type 3XBP1, X-box binding protein 1ZBTB16, zinc finger and BTB domain containing 16

Identifiers

PMID33643814
PMCPMC7893081
OpenAlexW3087639767

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.