ArticleBiophysical journal1997
Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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.
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.
Who cites it
4 citing papers in PubMed.
- Annexins as Overlooked Regulators of Membrane Trafficking in Plant Cells.International journal of molecular sciences · 2017Review
- Annexin-phospholipid interactions. Functional implications.International journal of molecular sciences · 2013Article
- Apo and calcium-bound crystal structures of Alpha-11 giardin, an unusual annexin from Giardia lamblia.Journal of molecular biology · 2007Article
- Ca(2+) and membrane binding to annexin 3 modulate the structure and dynamics of its N terminus and domain III.Protein science : a publication of the Protein Society · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies have revealed that binding of annexin I to phospholipids induces the formation of a second phospholipid binding site. It is shown that the N terminus on the concave side of membrane-bound annexin I is cleaved much faster by trypsin or cathepsin than the N terminus of the free protein. The reactivity of the unique disulfide bond located near the concave face was similarly increased by membrane binding. These results demonstrate that Ca(2+)-dependent membrane binding induces a conformational change on the concave side of the annexin I molecule and support the notion that this face of the molecule may contribute to the formation of the secondary membrane-binding site.
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