Evidence map›Paper›PMID 8548457›Full record

ArticleNature structural biology1996

Structure of a novel extracellular Ca(2+)-binding module in BM-40.

E Hohenester, P Maurer, C Hohenadl, R Timpl, J N Jansonius, J Engel

Abstract read
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In one paragraph

Article in Nature structural biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 2 pooled it
–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

39 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Pooled it
  3. Testican-2 (SPOCK2): A multifunctional matricellular regulator.Matrix biology : journal of the International Society for Matrix Biology · 2026
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  10. TheGenetics · 2019
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  19. Expression, functional, and structural analysis of proteins critical for otoconia development.Developmental dynamics : an official publication of the American Association of Anatomists · 2010
    Article
  20. Structural basis of sequence-specific collagen recognition by SPARC.Proceedings of the National Academy of Sciences of the United States of America · 2008
    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.

E HohenesterDepartment of Structural Biology, University of Basel, Switzerland.
P Maurer
C Hohenadl
R Timpl
J N Jansonius
J Engel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The EF-hand is a highly conserved Ca(2+)-binding motif found in many cytosolic Ca(2+)-modulated proteins. Here we report the crystal structure at 2.0 A resolution of the carboxy-terminal domain of human BM-40 (SPARC, osteonectin), an extracellular matrix protein containing an EF-hand pair. The two EF-hands interact canonically but their detailed structures are unusual. In the first EF-hand a one-residue insertion is accommodated by a cis-peptide bond and by substituting a carboxylate by a peptide carbonyl as a Ca2+ ligand. The second EF-hand is stabilized by a disulphide bond. The EF-hand pair interacts tightly with an amphiphilic amino-terminal helix, reminiscent of target peptide binding by calmodulin. The present structure defines a novel protein module occurring in several other extracellular proteins.

Indexed as

Amino Acid SequenceBinding SitesCalciumCalcium-Binding ProteinsCrystallography, X-RayHumansMolecular Sequence DataOsteonectinProtein ConformationCalciumCalcium-Binding ProteinsOsteonectin

Identifiers

PMID8548457

What OpenQuestion holds

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Registered trials

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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.