Evidence map›Paper›PMID 15170336›Full record

ArticleBiochemistry2004

Recognition of anionic phospholipid membranes by an antihemostatic protein from a blood-feeding insect.

John F Andersen, Nanda P Gudderra, Ivo M B Francischetti, Jesus G Valenzuela, José M C Ribeiro

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–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

32 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. De novo Ixodes ricinus salivary gland transcriptome analysis using two next-generation sequencing methodologies.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  11. Article
  12. Crystallization and preliminary X-ray crystallographic analysis of the membrane-binding haemprotein nitrophorin 7 from Rhodnius prolixus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  13. Article
  14. Article
  15. Structure and mechanism in salivary proteins from blood-feeding arthropods.Toxicon : official journal of the International Society on Toxinology · 2010
    Review
  16. Platelet aggregation inhibitors from hematophagous animals.Toxicon : official journal of the International Society on Toxinology · 2010
    Review
  17. Article
  18. Ultrafast dynamics of diatomic ligand binding to nitrophorin 4.Journal of the American Chemical Society · 2010
    Article
  19. 1H and 13C NMR spectroscopic studies of the ferriheme resonances of three low-spin complexes of wild-type nitrophorin 2 and nitrophorin 2(V24E) as a function of pH.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2009
    Article
  20. Protein dynamics of a beta-sheet protein.European biophysics journal : EBJ · 2009
    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

5 authors.

John F AndersenLaboratory of Malaria and Vector Research, National Institutes of Health, NIAID, Rockville, Maryland 20852, USA. jandersen@niaid.nih.gov
Nanda P Gudderra
Ivo M B Francischetti
Jesus G Valenzuela
José M C Ribeiro

Funding

Vector-Borne Diseases: Biology Of Vector Host RelationshipZ01AI000810 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI RIBEIRO, JOSE M · 1997 to 2008
$3.5M
Molecular approaches to understand vector-host and vector-pathogen interactionsZ01AI000932 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI VALENZUELA, JESUS · 2003 to 2008
$1.9M
Intramural NIH HHS Z01 AI000810Intramural NIH HHS Z99 AI999999
6 · The paper itself

Abstract

The saliva of blood-feeding insects contains a variety of molecules having antihemostatic activity. Here, we describe nitrophorin 7 (NP7), a salivary protein that binds with high affinity to anionic phospholipid membranes. The protein is apparently targeted to the negatively charged surfaces of activated platelets and other cells, where it can serve as a vasodilator, antihistamine, platelet aggregation inhibitor, and anticoagulant. As with other members of the nitrophorin group, NP7 reversibly binds a molecule of NO and binds histamine with high affinity. The protein differs from other nitrophorins in that it binds to membranes containing phosphatidylserine. Sedimentation and surface plasmon resonance experiments, revealed two classes of phospholipid-binding sites having K(d) values of 4.8 and 755 nM. NP7 inhibits prothrombin activation by blocking phospholipid binding sites for the prothrombinase complex on the surfaces of vesicles and activated platelets. As a NO complex, NP7 inhibits collagen and ADP-induced platelet aggregation and induces disaggregation of ADP-stimulated platelets by an NO-mediated mechanism. Molecular modeling of NP7 revealed a putative, positively charged membrane interaction surface comprised mainly of a helix lying outside of the lipocalin beta-barrel structure.

Indexed as

Blood CoagulationAmino Acid SequenceAnimalsBinding SitesBlood PlateletsCell MembraneHemeproteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPhosphatidylserinesPlatelet AggregationProthrombinSalivary GlandsSalivary Proteins and PeptidesSequence Homology, Amino AcidHemeproteinsnitrophorinPhosphatidylserinesProthrombinSalivary Proteins and PeptidesSodium ChlorideThromboplastin

Identifiers

PMID15170336
PMCPMC2915585

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.