Evidence map›Paper›PMID 33521680›Full record

ArticleSTAR protocols2021

An optimized protocol for acquiring and processing cryo-EM data of human 26S proteasome with M1-Ub

Xiang Chen, Dan Shi, Ping Zhang, Kylie J Walters

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in STAR protocols, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 100% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Article
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

4 authors at 3 institutions in 1 country.

Xiang ChenProtein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Dan ShiCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Ping ZhangKinase Complexes Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Kylie J WaltersProtein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
National Cancer Institute · USCenter for Cancer Research · USNational Institutes of Health · US

Funding

Ubiquitin signaling for protein degradationZIABC011490 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WALTERS, KYLIE · 2013 to 2025
$21.1M
CCR NIH HHS HHSN261200800001CIntramural NIH HHS ZIA BC011490NCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

The 26S proteasome is specialized for regulated protein degradation. It is formed by a regulatory particle (RP) that recognizes ubiquitinated substrates and caps a hollow cylindrical core particle (CP) where substrates are proteolyzed. Structural heterogeneity caused by dynamics makes it challenging to observe ubiquitin chains at the RP by cryogenic electron microscopy (cryo-EM). Here, we present a cryo-EM-based protocol we applied to study the human 26S proteasome with ubiquitin chains by using non-cleavable M1-linked hexaubiquitin (M1-Ub

Indexed as

Cryoelectron MicroscopyModels, MolecularPolyubiquitinProteasome Endopeptidase ComplexHumansATP dependent 26S proteasePolyubiquitinProteasome Endopeptidase ComplexBiophysicsCryo-EMProtein biochemistryStructural biology

Identifiers

PMID33521680
PMCPMC7820132
OpenAlexW3121544639

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.