Evidence map›Paper›PMID 32375056›Full record

ArticleStructure (London, England : 1993)2020

The Extent of Extended-Ubiquitin Binding to the Proteasome.

Jeroen Roelofs

Open access · bronzeAbstract readComment
PubMed Publisher
In one paragraph

Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Jeroen RoelofsDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, 3901 Rainbow Blvd, Kansas City, KS 66160, USA. Electronic address: jroelofs@kumc.edu.
University of Kansas Medical Center · US

Funding

Mechanism of degradation of the proteasome through autophagyR01GM118660 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI ROELOFS, JEROEN · 2016 to 2020
$1.5M
NIGMS NIH HHS R01 GM118660
6 · The paper itself

Abstract

In this issue of Structure, Lu et al. (2020) describe an NMR-based study showing the proteasome ubiquitin receptor hRpn13 bound to an extended conformation of K48-diubiquitin that is different from previously described structures of K48-diubiquitin. Observed dynamic binding properties suggest an ability of substrates to hop between proteasome ubiquitin receptors.

Indexed as

Proteasome Endopeptidase ComplexUbiquitinMolecular ConformationProtein BindingUbiquitinsProteasome Endopeptidase ComplexUbiquitinUbiquitins

Identifiers

PMID32375056
OpenAlexW3022730318

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.