Evidence map›Paper›PMID 22090109›Full record

ArticleJournal of virology2012

Naturally occurring fragments from two distinct regions of the prostatic acid phosphatase form amyloidogenic enhancers of HIV infection.

Franziska Arnold, Jacqueline Schnell, Onofrio Zirafi, Christina Stürzel, Christoph Meier, Tanja Weil, Ludger Ständker, Wolf-Georg Forssmann, Nadia R Roan, Warner C Greene and 2 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

64 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
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  7. Review
  8. Article
  9. Semen: A modulator of female genital tract inflammation and a vector for HIV-1 transmission.American journal of reproductive immunology (New York, N.Y. : 1989) · 2021
    Review
  10. Article
  11. Article
  12. Article
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  15. Article
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  18. Article
  19. Enhancement of Ebola virus infection by seminal amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. Structure, function and antagonism of semen amyloids.Chemical communications (Cambridge, England) · 2018
    Review

4 more citing papers are in PubMed but not listed here.

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

12 authors at 3 institutions in 2 countries.

Franziska ArnoldInstitute of Molecular Virology, Ulm University Medical Center, Ulm, Germany.
Jacqueline Schnell
Onofrio Zirafi
Christina Stürzel
Christoph Meier
Tanja Weil
Ludger Ständker
Wolf-Georg Forssmann
Nadia R Roan
Warner C Greene
Frank Kirchhoff
Jan Münch
Universität Ulm · DEGladstone Institutes · USMedizinische Hochschule Hannover · DE

Funding

Virology CoreP30AI027763 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STEVEN Grant DEEKS · 1988 to 2026
$93.6M
NIAID NIH HHS P30 AI027763
6 · The paper itself

Abstract

Semen is the major vector for HIV-1 transmission. We previously isolated C-proximal fragments of the prostatic acid phosphatase (PAP) from semen which formed amyloid fibrils that potently enhanced HIV infection. Here, we used the same methodology and identified another amyloidogenic peptide. Surprisingly, this peptide is derived from an N-proximal fragment of PAP (PAP85-120) and forms, similar to the C-proximal fragments, positively charged fibrillar structures that increase virion attachment to cells. Our results provide a first example for amyloid formation by fragments of distinct regions of the same precursor and further emphasize the possible importance of amyloidogenic peptides in HIV transmission.

Indexed as

Acid PhosphataseAmino Acid MotifsAmino Acid SequenceAmyloidCell LineHIV-1HIV InfectionsHumansMaleMolecular Sequence DataPeptide FragmentsProtein Tyrosine PhosphatasesSemenSequence AlignmentVirus AttachmentAcid PhosphataseAmyloidPeptide Fragmentsprostatic acid phosphataseProtein Tyrosine Phosphatases

Identifiers

PMID22090109
PMCPMC3255800
OpenAlexW2171545866

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.