Evidence map›Paper›PMID 17139257›Full record

ArticleThe EMBO journal2006

hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37.

Xiao-Bo Qiu, Song-Ying Ouyang, Chao-Jun Li, Shiying Miao, Linfang Wang, Alfred L Goldberg

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed, 2 pooled it
5.4field-weighted citation impact, top 4% 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

148 citing papers in PubMed, 2 syntheses or guidelines pooled it, 239 citations in OpenAlex.

  1. Pooled it
  2. The 6q22.33 locus and breast cancer susceptibility.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2009
    Pooled it
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  6. Review
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  12. Review
  13. Prediction of Disordered Linkers Using APOD.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

88 more citing papers are in PubMed but not listed here.

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

6 authors at 4 institutions in 2 countries.

Xiao-Bo QiuNational Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College, Tsinghua University, 5 Dongdan Santiao, Beijing, China. xbqiu@yahoo.com
Song-Ying Ouyang
Chao-Jun Li
Shiying Miao
Linfang Wang
Alfred L Goldberg
Chinese Academy of Medical Sciences & Peking Union Medical College · CNTsinghua University · CNHarvard University · USNanjing Normal University · CN

Funding

MECHANISMS OF ATP-DEPENDENT PROTEOLYTIC ENZYMESR01GM046147 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLDBERG, ALFRED L · 1992 to 2004
$1.8M
NIGMS NIH HHS 5R01 GM 46147-10NIGMS NIH HHS R01 GM046147
6 · The paper itself

Abstract

The 26S proteasome catalyzes the degradation of most proteins in mammalian cells. To better define its composition and associated regulatory proteins, we developed affinity methods to rapidly purify 26S proteasomes from mammalian cells. By this approach, we discovered a novel 46-kDa (407 residues) subunit of its 19S regulatory complex (previously termed ADRM1 or GP110). As its N-terminal half can be incorporated into the 26S proteasome and is homologous to Rpn13, a 156-residue subunit of the 19S complex in budding yeast, we renamed it human Rpn13 (hRpn13). The C-terminal half of hRpn13 binds directly to the proteasome-associated deubiquitinating enzyme, UCH37, and enhances its isopeptidase activity. Knockdown of hRpn13 in 293T cells increases the cellular levels of ubiquitin conjugates and decreases the degradation of short-lived proteins. Surprisingly, an overproduction of hRpn13 also reduced their degradation. Furthermore, transfection of the C-terminal half of hRpn13 slows proteolysis and induces cell death, probably by acting as a dominant-negative form. Thus in human 26S proteasomes, hRpn13 appears to be important for the binding of UCH37 to the 19S complex and for efficient proteolysis.

Indexed as

Amino Acid SequenceAnimalsCarbon-Nitrogen LyasesCarboxypeptidasesCarrier ProteinsCell DeathChromatography, AffinityConserved SequenceEukaryotic CellsEvolution, MolecularHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMass SpectrometryMembrane GlycoproteinsMice26S proteasome non-ATPase regulatory subunit 13ADRM1 protein, humanCarbon-Nitrogen LyasesCarboxypeptidasesCarrier ProteinsIntracellular Signaling Peptides and ProteinsisopeptidaseMembrane GlycoproteinsProteasome Endopeptidase ComplexProtein SubunitsUbiquitinUbiquitin ThiolesteraseUCHL5 protein, human

Identifiers

PMID17139257
PMCPMC1698896
OpenAlexW2014630160

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.