Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry.

Open access · goldAbstract read

In one paragraph

Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.2field-weighted citation impact, top 52% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

Regulating Proteasome Activity.Biomolecules · 2022
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

2 authors at 1 institution in 1 country.

Marta L MendesProteomics of Cellular Signaling, Department of Infection and Immunity, Luxembourg Institute of Health, 1a Rue Thomas Edison, 1445 Strassen, Luxembourg.ORCID 0000-0002-3528-7123

Gunnar DittmarProteomics of Cellular Signaling, Department of Infection and Immunity, Luxembourg Institute of Health, 1a Rue Thomas Edison, 1445 Strassen, Luxembourg.ORCID 0000-0003-3647-8623

Luxembourg Institute of Health · LU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 26S proteasome is a macromolecular complex that degrades proteins maintaining cell homeostasis; thus, determining its structure is a priority to understand its function. Although the 20S proteasome's structure has been known for some years, the highly dynamic nature of the 19S regulatory particle has presented a challenge to structural biologists. Advances in cryo-electron microscopy (cryo-EM) made it possible to determine the structure of the 19S regulatory particle and showed at least seven different conformational states of the proteasome. However, there are still many questions to be answered. Cross-linking mass spectrometry (CLMS) is now routinely used in integrative structural biology studies, and it promises to take integrative structural biology to the next level, answering some of these questions.

Indexed as

Cross-Linking ReagentsCryoelectron MicroscopyCrystallography, X-RayMass SpectrometryPeptidesProteasome Endopeptidase ComplexProtein Structure, QuaternaryATP dependent 26S proteaseCross-Linking ReagentsPeptidesProteasome Endopeptidase Complexcross-linking mass spectrometryelectron microscopyproteasomestructural biologyX-ray crystallography

Identifiers

PMID33801594

DOI10.3390/biom11040505

PMCPMC8067131

OpenAlexW3140240088

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.