Evidence map›Paper›PMID 2390065›Full record

ArticleThe Biochemical journal1990

Purification and characterization of a major phosphatidylserine-binding phosphoprotein from human platelets.

R Burgener, M Wolf, T Ganz, M Baggiolini

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.3field-weighted citation impact, top 49% 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

21 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Model for the architecture of caveolae based on a flexible, net-like assembly of Cavin1 and Caveolin discs.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Review
  14. The effect of cell subset isolation method on gene expression in leukocytes.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2014
    Article
  15. Seg1 controls eisosome assembly and shape.The Journal of cell biology · 2012
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins.Proceedings of the National Academy of Sciences of the United States of America · 1994
    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

4 authors at 1 institution in 1 country.

R BurgenerTheodor Kocher Institut, Universität Bern, Switzerland.
M Wolf
T Ganz
M Baggiolini
University of Bern · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We describe the isolation, lipid-binding properties and partial amino acid sequence of PS-p68, a novel 68 kDa phosphatidylserine-binding protein from human platelets. PS-p68 is an abundant constituent of platelets, accounting for 0.5-0.75% of total cell protein. It was purified from platelet cytosol by affinity chromatography. Amino acid sequence analysis yielded no similarity to identified proteins. In contrast with most known phospholipid-binding proteins, PS-p68 does not bind Ca2+ and does not require Ca2+ for its binding of phosphatidylserine. Phosphatidylserine binding to PS-p68 was inhibited by phosphatidic acid and by alkylphospholipids. PS-p68 was isolated as a major phosphoprotein from 32P-labelled platelets and was found to function as a protein kinase C substrate in vitro. However, treatment of intact platelets with phorbol 12-myristate 13-acetate, thrombin or carbacyclin did not increase PS-p68 phosphorylation. Platelets appear to be the only blood cells containing PS-p68, which was not detected in neutrophils, monocytes and lymphocytes.

Indexed as

Amino Acid SequenceBlood PlateletsBlood ProteinsCarrier ProteinsCollodionCytosolHumansMolecular Sequence DataPhosphoproteinsPhosphorylationProtein BindingTissue DistributionBlood ProteinsCarrier ProteinsCollodionPhosphoproteins

Identifiers

PMID2390065
PMCPMC1131648
OpenAlexW1936808647

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.