Evidence map›Paper›PMID 8870658›Full record

ArticleThe Biochemical journal1996

Structural requirements for annexin I-S100C complex-formation.

J Seemann, K Weber, V Gerke

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

13 citing papers in PubMed, 89 citations in OpenAlex.

  1. Revisiting the role of Annexins in membrane trafficking.Cellular and molecular life sciences : CMLS · 2025
    Review
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  13. Promoting detachment of neutrophils adherent to murine postcapillary venules to control inflammation: effect of lipocortin 1.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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 at 2 institutions in 1 country.

J SeemannDepartment of Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Federal Republic of Germany.
K Weber
V Gerke
Max Planck Institute for Biophysical Chemistry · DEUniversity of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S100C is a member of the S100 family of EF-hand-type Ca(2+)-binding proteins which are thought to bind to and thereby regulate the activity of cellular target proteins in a Ca(2+)-dependent manner. An intracellular ligand for S100C is the Ca2+/phospholipid-binding protein annexin I and we show here that complex-formation is mediated through unique domains within S100C and annexin I. Using a proteolytically truncated annexin I derivative as well as a number of N-terminal annexin I peptides in liposome co-pelleting and ligand-blotting assays we map the S100C-binding site to the N-terminal 13 residues of annexin I. Similar analyses employing recombinantly expressed S100C mutants reveal that residues D91 to 194 in the unique C-terminal extension of this S100 protein are indispensable for annexin I binding. Interaction between S100C and an N-terminal annexin I peptide containing a tryptoplan at position 11 can also be monitored by fluorescence emission spectroscopy after tryptophan excitation. This analysis indicates that the local environment of the tryptophan in annexin I becomes less aqueous on S100C binding, suggesting a hydrophobic nature of the protein-protein interaction. Thus the structural basis of the annexin 1-S100C complex-formation probably resembles to a large extent that of the well-characterized annexin II-p11 interaction.

Indexed as

AnimalsAnnexin A1Binding SitesBrain ChemistryCalciumCalcium-Binding ProteinsDNA, ComplementaryLiposomesLungPolymerase Chain ReactionProtein ConformationS100 ProteinsSpectrometry, FluorescenceSwineTryptophanAnnexin A1CalciumCalcium-Binding ProteinsDNA, ComplementaryLiposomesS100A11 protein, humanS100 ProteinsTryptophan

Identifiers

PMID8870658
PMCPMC1217744
OpenAlexW2115029490

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.