Evidence map›Paper›PMID 10363659›Full record

ReviewMolecular biology reports1999

GFP-labelling of 26S proteasomes in living yeast: insight into proteasomal functions at the nuclear envelope/rough ER.

C Enenkel, A Lehmann, P M Kloetzel

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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

24 citing papers in PubMed, 57 citations in OpenAlex.

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  16. Sts1 plays a key role in targeting proteasomes to the nucleus.The Journal of biological chemistry · 2011
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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.

C EnenkelInstitut für Biochemie, Humboldt Universität, Universitätsklinikum Charité, Berlin, Germany.
A Lehmann
P M Kloetzel
Humboldt-Universität zu Berlin · DECharité - Universitätsmedizin Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

26S proteasomes are multisubunit protease complexes that play the central role in the ubiquitin-dependent protein degradation pathway. The proteolytically active core is formed by the 20S proteasome. Regulatory subunits, principally the 19S cap complex, confer the specificity towards ubiquitinated substrates and an ATP-dependence on proteolysis. Green fluorescence protein (GFP)-tagged versions of either an alpha-subunit of the 20S core or an ATPase subunit of the 19S cap complex were functionally incorporated into the protease complex, thus allowing to monitor the subcellular distribution of 26S proteasomes in living yeast. Our localization studies suggest that proteasomal proteolysis mainly occurs at the nuclear envelope (NE)/rough ER. Implications of proteasomal functions at the NE/rough ER are discussed in the context of published work on ER degradation and with regard to possible targeting mechanisms.

Indexed as

Proteasome Endopeptidase ComplexAdenosine TriphosphatasesAdenosine TriphosphateEndoplasmic Reticulum, RoughGreen Fluorescent ProteinsLuminescent ProteinsNuclear EnvelopePeptide HydrolasesRecombinant Fusion ProteinsYeastsAdenosine TriphosphatasesAdenosine TriphosphateATP dependent 26S proteaseGreen Fluorescent ProteinsLuminescent ProteinsPeptide HydrolasesProteasome Endopeptidase ComplexRecombinant Fusion Proteins

Identifiers

PMID10363659
OpenAlexW66834092

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.