Evidence map›Paper›PMID 26997268›Full record

ArticleCell reports2016

Assembly of an Evolutionarily Conserved Alternative Proteasome Isoform in Human Cells.

Achuth Padmanabhan, Simone Anh-Thu Vuong, Mark Hochstrasser

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.

  1. Pooled it
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  5. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
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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

3 authors at 2 institutions in 1 country.

Achuth PadmanabhanDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.
Simone Anh-Thu VuongDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.
Mark HochstrasserDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA. Electronic address: mark.hochstrasser@yale.edu.
Whitney Museum of American Art · USYale University · US

Funding

Function and Assembly of Eukaryotic ProteasomesR01GM083050 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 2008 to 2019
$3.8M
Degradation of Short Lived Regulatory Protein in YeastR37GM046904 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 2009 to 2018
$3.6M
DEGRADTION OF SHORT-LIVED REGULATORY PROTEINS IN YEASTR01GM046904 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 1992 to 2020
$3.6M
NIGMS NIH HHS GM083050NIGMS NIH HHS R01 GM046904NIGMS NIH HHS R01 GM083050NIGMS NIH HHS R37 GM046904
6 · The paper itself

Abstract

Targeted intracellular protein degradation in eukaryotes is largely mediated by the proteasome. Here, we report the formation of an alternative proteasome isoform in human cells, previously found only in budding yeast, that bears an altered subunit arrangement in the outer ring of the proteasome core particle. These proteasomes result from incorporation of an additional α4 (PSMA7) subunit in the position normally occupied by α3 (PSMA4). Assembly of "α4-α4" proteasomes depends on the relative cellular levels of α4 and α3 and on the proteasome assembly chaperone PAC3. The oncogenic tyrosine kinases ABL and ARG and the tumor suppressor BRCA1 regulate cellular α4 levels and formation of α4-α4 proteasomes. Cells primed to assemble α4-α4 proteasomes exhibit enhanced resistance to toxic metal ions. Taken together, our results establish the existence of an alternative mammalian proteasome isoform and suggest a potential role in enabling cells to adapt to environmental stresses.

Indexed as

Biological EvolutionBRCA1 ProteinCadmium ChlorideCell Line, TumorCell SurvivalDown-RegulationHEK293 CellsHeLa CellsHumansImmunoblottingMolecular ChaperonesProteasome Endopeptidase ComplexProtein IsoformsProtein SubunitsReal-Time Polymerase Chain ReactionRNA InterferenceBRCA1 ProteinCadmium ChlorideMolecular ChaperonesProteasome Endopeptidase ComplexProtein IsoformsProtein SubunitsRNA, MessengerRNA, Small InterferingSaccharomyces cerevisiae Proteins

Identifiers

PMID26997268
PMCPMC4828729
OpenAlexW2299008096

What OpenQuestion holds

Textmetadata
LicenceTDM
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.