Evidence map›Paper›PMID 7552735›Full record

ArticleNature structural biology1995

Dance of the dimers.

J Krebs, M Quadroni, L J Van Eldik

Abstract readNews
PubMed Publisher
In one paragraph

Article in Nature structural biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. S100 proteins in cartilage: role in arthritis.Biochimica et biophysica acta · 2012
    Review
  2. Purification, crystallization and preliminary X-ray diffraction of human S100A15.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006
    Article
  3. Article
  4. Article
  5. 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.

J Krebs
M Quadroni
L J Van Eldik

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structure of the apo form of calcyclin, a member of the S100 family of calcium-binding proteins, reveals a novel dimer fold that may reflect the presence of a new interface for target protein recognition.

Indexed as

Amino Acid SequenceAnimalsCalciumCalcium-Binding ProteinsMolecular Sequence DataProtein ConformationProtein FoldingS100 ProteinsCalciumCalcium-Binding ProteinsS100 Proteins

Identifiers

PMID7552735

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.