Evidence map›Paper›PMID 9228945›Full record

ArticleNature structural biology1997

Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes.

H Blanchard, P Grochulski, Y Li, J S Arthur, P L Davies, J S Elce, M Cygler

Abstract read
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In one paragraph

Article in Nature structural biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

60 citing papers in PubMed, 205 citations in OpenAlex.

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  9. Review
  10. The role of calcium-calpain pathway in hyperthermia.Frontiers in molecular medicine · 2022
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Structural and functional diversity of EF-hand proteins: Evolutionary perspectives.Protein science : a publication of the Protein Society · 2017
    Review
  16. Article
  17. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

H BlanchardBiotechnology Research Institute, NRC, Montréal, Québec, Canada.
P Grochulski
Y Li
J S Arthur
P L Davies
J S Elce
M Cygler
Biotechnology Research Institute · CAQueen's University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crystal structure of a Ca(2+)-binding domain (dVI) of rat m-calpain has been determined at 2.3 A resolution, both with and without bound Ca2+. The structures reveal a unique fold incorporating five EF-hand motifs per monomer, three of which bind calcium at physiological calcium concentrations, with one showing a novel EF-hand coordination pattern. This investigation gives us a first view of the calcium-induced conformational changes, and consequently an insight into the mechanism of calcium induced activation in calpain. The crystal structures reveal a dVI homodimer which provides a preliminary model for the subunit dimerization in calpain.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalciumCalpainCrystallography, X-RayDimerizationModels, MolecularMolecular Sequence DataProtein ConformationRatsSequence Homology, Amino AcidCalciumCalpain

Identifiers

PMID9228945
OpenAlexW2028507130

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.