Evidence map›Paper›PMID 22907203›Full record

ArticleEuropean biophysics journal : EBJ2012

Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper.

Sarah R Sheftic, Jessica M Snell, Suman Jha, Andrei T Alexandrescu

Abstract read
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In one paragraph

Article in European biophysics journal : EBJ, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. [PSB0739 inhibits formation of semen-derived amyloid fibril].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2018
    Article
  5. Structure, function and antagonism of semen amyloids.Chemical communications (Cambridge, England) · 2018
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Emerging roles of human prostatic Acid phosphatase.Biomolecules & therapeutics · 2013
    Review
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.

Sarah R ShefticDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3125, USA.
Jessica M Snell
Suman Jha
Andrei T Alexandrescu
University of Connecticut · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Semen-derived enhancer of virus infection (SEVI), a naturally occurring peptide fragment of prostatic acid phosphatase, enhances HIV infectivity by forming cationic amyloid fibrils that aid the fusion of negatively charged virion and target cell membranes. Cu(II) and Zn(II) inhibit fibrillization of SEVI in a kinetic assay using the fibril-specific dye ThT. TEM suggests that the metals do not affect fibril morphology. NMR shows that the metals bind to histidines 3 and 23 in the SEVI sequence. ITC experiments indicate that SEVI forms oligomeric complexes with the metals. Dissociation constants are micromolar for Cu(II) and millimolar for Zn(II). Because the Cu(II) and Zn(II) concentrations that inhibit fibrillization are comparable with those found in seminal fluid the metals may modulate SEVI fibrillization under physiological conditions.

Indexed as

AmyloidCopperHistidineHumansMicroscopy, Electron, TransmissionNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Tyrosine PhosphatasesZincAmyloidCopperHistidinePeptide Fragmentsprostatic acid phosphatase (248-286), humanProtein Tyrosine PhosphatasesZinc

Identifiers

PMID22907203
OpenAlexW2054440293

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.