Evidence map›Paper›PMID 21131363›Full record

ArticleThe Journal of biological chemistry2011

Identification of novel binding partners (annexins) for the cell death signal phosphatidylserine and definition of their recognition motif.

Sabrina Rosenbaum, Sandra Kreft, Julia Etich, Christian Frie, Jacek Stermann, Ivan Grskovic, Benjamin Frey, Dirk Mielenz, Ernst Pöschl, Udo Gaipl and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

28 citing papers in PubMed, 56 citations in OpenAlex.

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  12. The Gustatory Sensory G-Protein GNAT3 Suppresses Pancreatic Cancer Progression in Mice.Cellular and molecular gastroenterology and hepatology · 2021
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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

12 authors at 4 institutions in 3 countries.

Sabrina RosenbaumMedical Faculty, Center for Biochemistry, University of Cologne, 50931 Cologne, Germany.
Sandra Kreft
Julia Etich
Christian Frie
Jacek Stermann
Ivan Grskovic
Benjamin Frey
Dirk Mielenz
Ernst Pöschl
Udo Gaipl
Mats Paulsson
Bent Brachvogel
University of Cologne · DEUniversitätsklinikum Erlangen · DEFriedrich-Alexander-Universität Erlangen-Nürnberg · DEUniversity of East Anglia · GB

Funding

Medical Research Council G0802553
6 · The paper itself

Abstract

Identification and clearance of apoptotic cells prevents the release of harmful cell contents thereby suppressing inflammation and autoimmune reactions. Highly conserved annexins may modulate the phagocytic cell removal by acting as bridging molecules to phosphatidylserine, a characteristic phagocytosis signal of dying cells. In this study five members of the structurally and functionally related annexin family were characterized for their capacity to interact with phosphatidylserine and dying cells. The results showed that AnxA3, AnxA4, AnxA13, and the already described interaction partner AnxA5 can bind to phosphatidylserine and apoptotic cells, whereas AnxA8 lacks this ability. Sequence alignment experiments located the essential amino residues for the recognition of surface exposed phosphatidylserine within the calcium binding motifs common to all annexins. These amino acid residues were missing in the evolutionary young AnxA8 and when they were reintroduced by site directed mutagenesis AnxA8 gains the capability to interact with phosphatidylserine containing liposomes and apoptotic cells. By defining the evolutionary conserved amino acid residues mediating phosphatidylserine binding of annexins we show that the recognition of dying cells represent a common feature of most annexins. Hence, the individual annexin repertoire bound to the cell surface of dying cells may fulfil opsonin-like function in cell death recognition.

Indexed as

Amino Acid MotifsAnimalsAnnexinsApoptosisCalciumEvolution, MolecularMiceNIH 3T3 CellsPhosphatidylserinesProtein BindingSignal TransductionAnnexinsCalciumPhosphatidylserines

Identifiers

PMID21131363
PMCPMC3037683
OpenAlexW2005423745

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.