Evidence map›Paper›PMID 31098023›Full record

ArticleIUCrJ2019

Cryo-EM reveals the asymmetric assembly of squid hemocyanin.

Yoshikazu Tanaka, Sanae Kato, Markus Stabrin, Stefan Raunser, Takashi Matsui, Christos Gatsogiannis

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Cryo-EM structure of the ClpXP protein degradation machinery.Nature structural & molecular biology · 2019
    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

6 authors at 3 institutions in 2 countries.

Yoshikazu TanakaGraduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai 980-8577, Japan.ORCID https://orcid.org/0000-0002-7893-3236
Sanae KatoFaculty of Fisheries, Kagoshima University, Kagoshima 890-0056, Japan.ORCID https://orcid.org/0000-0003-3017-0281
Markus StabrinMax Planck Institute of Molecular Physiology, Department of Structural Biochemistry, Otto Hahn Strasse 11, Dortmund 44227, Germany.
Stefan RaunserMax Planck Institute of Molecular Physiology, Department of Structural Biochemistry, Otto Hahn Strasse 11, Dortmund 44227, Germany.ORCID https://orcid.org/0000-0001-9373-3016
Takashi MatsuiGraduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai 980-8577, Japan.
Christos GatsogiannisMax Planck Institute of Molecular Physiology, Department of Structural Biochemistry, Otto Hahn Strasse 11, Dortmund 44227, Germany.ORCID https://orcid.org/0000-0002-4922-4545
Max Planck Institute of Molecular Physiology · DETohoku University · JPKagoshima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The oxygen transporter of molluscs, hemocyanin, consists of long pearl-necklace-like subunits of several globular domains. The subunits assemble in a complex manner to form cylindrical decamers. Typically, the first six domains of each subunit assemble together to form the cylinder wall, while the C-terminal domains form a collar that fills or caps the cylinder. During evolution, various molluscs have been able to fine-tune their oxygen binding by deleting or adding C-terminal domains and adjusting their inner-collar architecture. However, squids have duplicated one of the wall domains of their subunits instead. Here, using cryo-EM and an optimized refinement protocol implemented in

Indexed as

cryo-electron microscopymacromolecular machinesprotein structuressingle-particle cryo-EMstructure determination

Identifiers

PMID31098023
PMCPMC6503924
OpenAlexW2935658095

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.