Structural changes underlying allostery in group II chaperonins.

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.

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.

Who cites it

1 citing paper in PubMed, 4 citations in OpenAlex.

1. Ring Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin.Structure (London, England : 1993) · 2016
   Article

Corrections and comments

• Comment on
  Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.2011

Authors and funding

1 author at 1 institution in 1 country.

Funding

No grant is acknowledged in the PubMed record.

Abstract