Evidence map›Paper›PMID 9620878›Full record

ArticleThe Biochemical journal1998

Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes.

K B Hendil, S Khan, K Tanaka

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 221 citations in OpenAlex.

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  12. Exploring long-range cooperativity in the 20S proteasome core particle fromProceedings of the National Academy of Sciences of the United States of America · 2020
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  18. Evolution of proteasome regulators in eukaryotes.Genome biology and evolution · 2015
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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 2 countries.

K B HendilAugust Krogh Institute, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen O, Denmark. KBHendil@aki.ku.dk
S Khan
K Tanaka
University of Copenhagen · DKTokyo Metropolitan Institute of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two activators, named PA700 and PA28, are known to bind to 20 S proteasomes, forming two different complexes. The PA700-proteasome complex, also known as the 26 S proteasome, can degrade intact proteins, whereas complexes with PA28 can degrade only peptides. Monoclonal antibodies to 20 S proteasomes or the p45 ATPase subunit (Trip1, Sug1) of PA700 precipitated the same set of proteins from HeLa extracts, including six different ATPase subunits of PA700. This shows that p45 is not present in other protein complexes and suggests that all 26 S proteasome particles contain the same set of ATPase subunits. Interferons alpha and gamma had no effect on the composition of the 26 S proteasome, except for the replacement of subunits delta, MB1 and Z with Lmp2, Lmp7 and MECL1 respectively. Surprisingly, antibodies to PA28 precipitated p42, a component of PA700. Conversely, anti-p45 antibodies precipitated not only 26 S proteasomes but also PA28 alpha, beta and gamma, indicating that 20 S proteasomes can simultaneously bind both PA700 and PA28. PA28 alpha beta is known to be involved in antigen presentation. Conceivably, intact substrate proteins are recognized by PA700 and fed into proteasomes whose cleavage specificity is optimized for antigen presentation on MHC class I by PA28 and three interferon inducible proteasome subunits.

Indexed as

Muscle ProteinsAdenosine TriphosphatasesAntibodies, MonoclonalChromatography, GelCysteine EndopeptidasesElectrophoresis, Gel, Two-DimensionalEnzyme ActivationHeLa CellsHumansInterferon-alphaInterferon-gammaMultienzyme ComplexesPeptide HydrolasesProteasome Endopeptidase ComplexProtein BindingProteinsAdenosine TriphosphatasesAntibodies, MonoclonalATP dependent 26S proteaseCysteine EndopeptidasesInterferon-alphaInterferon-gammaMultienzyme ComplexesMuscle ProteinsPA700 proteasome activatorPeptide HydrolasesProteasome Endopeptidase ComplexProteinsPSME1 protein, human

Identifiers

PMID9620878
PMCPMC1219536
OpenAlexW1904980709

What OpenQuestion holds

Textmetadata
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.