Evidence map›Paper›PMID 31487956›Full record

ArticleBiomolecules2019

The Proteasome Lid Triggers COP9 Signalosome Activity during the Transition of

Laylan Bramasole, Abhishek Sinha, Dana Harshuk, Angela Cirigliano, Sylvia Gurevich, Zanlin Yu, Rinat Lift Carmeli, Michael H Glickman, Teresa Rinaldi, Elah Pick

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

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed, 1 pooled it
0.3field-weighted citation impact, top 43% 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

5 citing papers in PubMed, 1 synthesis or guideline pooled it, 10 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025
    Review
  5. Review
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 2 countries.

Laylan BramasoleDepartment of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel.
Abhishek SinhaDepartment of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel.
Dana HarshukDepartment of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel.
Angela CiriglianoDepartment of Biology and Biotechnology "Charles Darwin", La Sapienza University of Rome, 00185 Rome, Italy.
Sylvia GurevichDepartment of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel.
Zanlin YuDepartment of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel.
Rinat Lift CarmeliDepartment of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel.
Michael H GlickmanDepartment of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel.
Teresa RinaldiDepartment of Biology and Biotechnology "Charles Darwin", La Sapienza University of Rome, 00185 Rome, Italy.
Elah PickDepartment of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel. elahpic@research.haifa.ac.il.
Oranim Academic College of Education · ILTechnion – Israel Institute of Technology · ILSapienza University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The class of Cullin-RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating enzymes, a handful of which are associated with the proteasome. The CRL activity is triggered by modification of the Cullin subunit with the ubiquitin-like protein, NEDD8 (also known as Rub1 in

Indexed as

COP9 Signalosome ComplexProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationUbiquitin-Protein LigasesUbiquitinsATP dependent 26S proteaseCOP9 Signalosome ComplexProteasome Endopeptidase ComplexRUB1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein LigasesUbiquitins26S proteasomebudding yeastCdc53CSN (COP9 signalosome)Cullindiauxic shiftNEDD8 (neural precursor cell expressed developmentally down-regulated 8)proteasome lidRpn11Rub1 (Related ubiquitin 1)Sachharomyces cerevisiaeSCF (Skp, Cullin, F-box containing complex)

Identifiers

PMID31487956
PMCPMC6770237
OpenAlexW2972222525

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.