Evidence map›Paper›PMID 10393958›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Megakaryocyte hyperplasia and enhanced agonist-induced platelet activation in vasodilator-stimulated phosphoprotein knockout mice.

W Hauser, K P Knobeloch, M Eigenthaler, S Gambaryan, V Krenn, J Geiger, M Glazova, E Rohde, I Horak, U Walter and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 224 citations in OpenAlex.

  1. Trial
  2. CNP-induced cGMP signaling reduces growth cone stiffness and CaFrontiers in molecular neuroscience · 2026
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  13. A modular toolkit to inhibit proline-rich motif-mediated protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Review
  15. Vasodilator-stimulated phosphoprotein protects against vascular inflammation and insulin resistance.American journal of physiology. Endocrinology and metabolism · 2014
    Article
  16. The integrin adhesome: from genes and proteins to human disease.Nature reviews. Molecular cell biology · 2014
    Review
  17. Article
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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

11 authors at 1 institution in 1 country.

W HauserInstitut für Klinische Biochemie und Pathobiochemie und, Josef-Schneider Strasse 2, 97080 Würzburg, Germany.
K P Knobeloch
M Eigenthaler
S Gambaryan
V Krenn
J Geiger
M Glazova
E Rohde
I Horak
U Walter
M Zimmer
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vasodilator-stimulated phosphoprotein (VASP), a substrate of cAMP- and cGMP-dependent protein kinases, is associated with focal adhesions, cell-cell contacts, microfilaments, and highly dynamic membrane regions. VASP, which is expressed in most cell types and in particularly high levels in human platelets, binds to profilin, zyxin, vinculin, F-actin, and the Listeria monocytogenes surface protein ActA. VASP is a member of the enabled (Ena)/VASP protein family and is thought to be involved in actin filament formation and integrin alphaIIbbeta3 inhibition in human platelets. To gain further insight into the in vivo function of this protein, VASP-deficient mice were generated by homologous recombination. VASP-/- mice demonstrated hyperplasia of megakaryocytes in bone marrow and spleen but exhibited no other macroscopic or microscopic abnormalities. Activation of platelets with thrombin induced a more than 2-fold higher surface expression of P-selectin and fibrinogen binding in VASP-deficient platelets in comparison to wild type. These data support the concept that VASP is a negative modulator of platelet and integrin alphaIIbbeta3 activation. Although the limited phenotypic differences between wild-type and VASP-/- mice suggested functional compensation of VASP by members of the Ena/VASP family, alterations in the expression levels of mammalian enabled (Mena) and Ena-VASP-like (Evl) protein were not detected. VASP-deficient mice may provide an interesting model system for diseases in which enhanced platelet activation plays a major role.

Indexed as

AnimalsBlood PlateletsCarrier ProteinsCell Adhesion MoleculesDNA, ComplementaryDNA PrimersFemaleHumansHyperplasiaMaleMegakaryocytesMiceMice, KnockoutMicrofilament ProteinsOrgan SpecificityPhosphoproteinsCarrier ProteinsCell Adhesion MoleculesDNA, ComplementaryDNA PrimersMicrofilament ProteinsPhosphoproteinsVasodilator-Stimulated Phosphoprotein

Identifiers

PMID10393958
PMCPMC22198
OpenAlexW2104539000

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.