Evidence map›Paper›PMID 33682792›Full record

ArticleActa crystallographica. Section F, Structural biology communications2021

Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy.

Yi Cheng Zeng, Meghna Sobti, Alastair G Stewart

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

Article in Acta crystallographica. Section F, Structural biology communications, 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
0.2field-weighted citation impact, top 48% 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, 3 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

3 authors at 1 institution in 1 country.

Yi Cheng ZengMolecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst, NSW 2010, Australia.ORCID 0000-0001-9964-0929
Meghna SobtiMolecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst, NSW 2010, Australia.ORCID 0000-0001-7086-3467
Alastair G StewartMolecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst, NSW 2010, Australia.ORCID 0000-0002-2070-6030
Victor Chang Cardiac Research Institute · AU

Funding

National Health and Medical Research Council APP1146403National Health and Medical Research Council APP1159347
6 · The paper itself

Abstract

Chaperonins are biomolecular complexes that assist in protein folding. Thermophilic factor 55 (TF55) is a group II chaperonin found in the archaeal genus Sulfolobus that has α, β and γ subunits. Using cryo-electron microscopy, structures of the β-only complex of S. solfataricus TF55 (TF55β) were determined to 3.6-4.2 Å resolution. The structures of the TF55β complexes formed in the presence of ADP or ATP highlighted an open state in which nucleotide exchange can occur before progressing in the refolding cycle.

Indexed as

Cryoelectron MicroscopyAdenosine DiphosphateAdenosine TriphosphateArchaeal ProteinsChaperoninsModels, MolecularProtein ConformationSulfolobus solfataricusAdenosine DiphosphateAdenosine TriphosphateArchaeal ProteinsChaperoninschaperoninscryo-electron microscopy

Identifiers

PMID33682792
PMCPMC7938637
OpenAlexW3133945580

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.