Evidence map›Paper›PMID 10363642›Full record

ReviewMolecular biology reports1999

Functional analysis of the proteasome regulatory particle.

M H Glickman, D M Rubin, H Fu, C N Larsen, O Coux, I Wefes, G Pfeifer, Z Cjeka, R Vierstra, W Baumeister and 2 more

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biology reports, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.4field-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

29 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Proteotoxic stress and the ubiquitin proteasome system.Seminars in cell & developmental biology · 2024
    Review
  3. Transcriptomic Response of the Liver Tissue inAnimals : an open access journal from MDPI · 2023
    Article
  4. Article
  5. Review
  6. Article
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  8. Review
  9. Article
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  17. Review
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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

12 authors at 5 institutions in 3 countries.

M H GlickmanDept. of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
D M Rubin
H Fu
C N Larsen
O Coux
I Wefes
G Pfeifer
Z Cjeka
R Vierstra
W Baumeister
V Fried
D Finley
Harvard University · USMax Planck Institute of Biochemistry · DEUniversity of Wisconsin–Madison · USCentre de Recherche en Biologie cellulaire de Montpellier · FRNew York Medical College · US

Funding

NASL REPEAT DOMAIN AND PROTEASOME FUNCTIONF32GM019359 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI LARSEN, CHRISTOPHER N. · 1998 to 1999
–
NIGMS NIH HHS F32 GM019359
6 · The paper itself

Abstract

We have developed S. cerevisiae as a model system for mechanistic studies of the 26S proteasome. The subunits of the yeast 19S complex, or regulatory particle (RP), have been defined, and are closely related to those of mammalian proteasomes. The multiubiquitin chain binding subunit (S5a/Mcb1/Rpn10) was found, surprisingly, to be nonessential for the degradation of a variety of ubiquitin-protein conjugates in vivo. Biochemical studies of proteasomes from deltarpn10 mutants revealed the existence of two structural subassemblies within the RP, the lid and the base. The lid and the base are both composed of 8 subunits. By electron microscopy, the base and the lid correspond to the proximal and distal masses of the RP, respectively. The base is sufficient to activate the 20S core particle for degradation of peptides, but the lid is required for ubiquitin-dependent degradation. The lid subunits share sequence motifs with components of the COP9/signalosome complex, suggesting that these functionally diverse particles have a common evolutionary ancestry. Analysis of equivalent point mutations in the six ATPases of the base indicate that they have well-differentiated functions. In particular, mutations in one ATPase gene, RPT2, result in an unexpected defect in peptide hydrolysis by the core particle. One interpretation of this result is that Rpt2 participates in gating of the channel through which substrates enter the core particle.

Indexed as

Adenosine TriphosphatasesAnimalsCysteine EndopeptidasesHumansMultienzyme ComplexesProteasome Endopeptidase ComplexProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinsAdenosine TriphosphatasesCysteine EndopeptidasesMultienzyme ComplexesProteasome Endopeptidase ComplexProteinsRpt2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitins

Identifiers

PMID10363642
OpenAlexW12673267

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.