Evidence map›Paper›PMID 2320573›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1990

Isolation of a 5-kilodalton actin-sequestering peptide from human blood platelets.

D Safer, R Golla, V T Nachmias

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
7.9field-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

47 citing papers in PubMed, 172 citations in OpenAlex.

  1. Article
  2. The role ofJournal of gastrointestinal oncology · 2025
    Article
  3. Article
  4. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Expression pattern of thymosin beta 4 in the adult human liver.European journal of histochemistry : EJH · 2011
    Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

D SaferDepartment of Anatomy, School of Medicine, University of Pennsylvania, Philadelphia 19104-6058.
R Golla
V T Nachmias
University of Pennsylvania · US

Funding

VASCULAR SMOOTH MUSCLEP01HL015835 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI GOLDMAN, YALE E · 1985 to 2002
$5.5M
CROSSBRIDGE STRUCTURE &GEOMETRYR29AR038976 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI SAFER, DANIEL · 1987 to 1991
–
BIOMEDICAL RESEARCH SUPPORTS07RR005415 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI RUBENSTEIN, ARTHUR H. · 1985 to 1992
–
NCRR NIH HHS S07-RR-05415-28NHLBI NIH HHS HL15835NIAMS NIH HHS AR38976
6 · The paper itself

Abstract

Resting human platelets contain approximately 0.3 mM unpolymerized actin. When freshly drawn and washed platelets are treated with saponin, 85-90% of the unpolymerized actin diffuses out. Analysis by polyacrylamide gel electrophoresis under nondenaturing conditions shows that the bulk of this unpolymerized actin migrates with a higher mobility than does pure G-actin, profilactin, or actin-gelsolin complex. When muscle G-actin is added to fresh or boiled saponin extract, the added muscle actin is shifted to the high-mobility form. The saponin extract contains an acidic peptide having a molecular mass in the range of 5 kDa, which has been purified to homogeneity by reverse-phase HPLC. This peptide also shifts muscle actin to the high-mobility form. Addition of either boiled saponin extract or the purified peptide to muscle G-actin also strongly and stoichiometrically inhibits salt-induced polymerization, as assayed by falling-ball viscometry and by sedimentation. We conclude that this peptide binds to the bulk of the unpolymerized actin in platelets and prevents it from polymerizing.

Indexed as

ActinsAmino AcidsAnimalsBlood PlateletsChromatography, High Pressure LiquidElectrophoresis, Polyacrylamide GelHumansImmunoblottingKineticsMacromolecular SubstancesMicrofilament ProteinsMolecular WeightMusclesMyosinsRabbitsActinsAmino AcidsMacromolecular SubstancesMicrofilament ProteinsMyosins

Identifiers

PMID2320573
PMCPMC53724
OpenAlexW2087120364

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.