Evidence map›Paper›PMID 28216640›Full record

ArticleScientific reports2017

The ubiquitin ligase Cullin5

Indranil Paul, Tanveer S Batth, Diego Iglesias-Gato, Amna Al-Araimi, Ibrahim Al-Haddabi, Amira Alkharusi, Gunnar Norstedt, Jesper V Olsen, Fahad Zadjali, Amilcar Flores-Morales

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 39 citations in OpenAlex.

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  14. The STK38-XPO1 axis, a new actor in physiology and cancer.Cellular and molecular life sciences : CMLS · 2021
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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

10 authors at 3 institutions in 3 countries.

Indranil PaulNovo Nordisk Foundation Center for Protein Research, Department of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen N, Denmark.
Tanveer S BatthNovo Nordisk Foundation Center for Protein Research, Department of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen N, Denmark.
Diego Iglesias-GatoDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, c/o the Danish Cancer Society, Strandboulevarden 49, DK-2100 Copenhagen Ø, Denmark.
Amna Al-AraimiCollege of Medicine and Health Sciences, Sultan Qaboos University, P.O. box 35, P.C 123, Muscat, Oman.
Ibrahim Al-HaddabiCollege of Medicine and Health Sciences, Sultan Qaboos University, P.O. box 35, P.C 123, Muscat, Oman.
Amira AlkharusiCollege of Medicine and Health Sciences, Sultan Qaboos University, P.O. box 35, P.C 123, Muscat, Oman.
Gunnar NorstedtCollege of Medicine and Health Sciences, Sultan Qaboos University, P.O. box 35, P.C 123, Muscat, Oman.
Jesper V OlsenNovo Nordisk Foundation Center for Protein Research, Department of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen N, Denmark.
Fahad ZadjaliCollege of Medicine and Health Sciences, Sultan Qaboos University, P.O. box 35, P.C 123, Muscat, Oman.
Amilcar Flores-MoralesNovo Nordisk Foundation Center for Protein Research, Department of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen N, Denmark.
Sultan Qaboos University · OMUniversity of Copenhagen · DKNovo Nordisk Foundation · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SOCS2 is a pleiotropic E3 ligase. Its deficiency is associated with gigantism and organismal lethality upon inflammatory challenge. However, mechanistic understanding of SOCS2 function is dismal due to our unawareness of its protein substrates. We performed a mass spectrometry based proteomic profiling upon SOCS2 depletion and yield quantitative data for ~4200 proteins. Through this screen we identify a novel target of SOCS2, the serine-threonine kinase NDR1. Over-expression of SOCS2 accelerates turnover, while its knockdown stabilizes, endogenous NDR1 protein. SOCS2 interacts with NDR1 and promotes its degradation through K48-linked ubiquitination. Functionally, over-expression of SOCS2 antagonizes NDR1-induced TNFα-stimulated NF-κB activity. Conversely, depletion of NDR1 rescues the effect of SOCS2-deficiency on TNFα-induced NF-κB transactivation. Using a SOCS2

Indexed as

AnimalsCell Line, TumorColitisDisease Models, AnimalEnzyme StabilityGene Expression RegulationHEK293 CellsHumansMaleMass SpectrometryMiceNF-kappa BProstatic NeoplasmsProtein Serine-Threonine KinasesProteomicsSuppressor of Cytokine Signaling ProteinsNF-kappa BProtein Serine-Threonine KinasesSOCS2 protein, humanSTK38 protein, humanSuppressor of Cytokine Signaling ProteinsTNF protein, humanTumor Necrosis Factor-alpha

Identifiers

PMID28216640
PMCPMC5316984
OpenAlexW2590187755

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.