Evidence map›Paper›PMID 29873340›Full record

ReviewChemical communications (Cambridge, England)2018

Structure, function and antagonism of semen amyloids.

Annika Röcker, Nadia R Roan, Jay Kant Yadav, Marcus Fändrich, Jan Münch

Open access · hybridAbstract readReview
In one paragraph

Review in Chemical communications (Cambridge, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.2field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Amyloid-mediated RNA uptake by sperm for embryonic delivery.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. AuNational science review · 2020
    Article
  16. Article
  17. Article
  18. Review
  19. 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 at 3 institutions in 5 countries.

Annika RöckerInstitute of Molecular Virology, Ulm University Medical Center, 89081 Ulm, Germany. jan.muench@uni-ulm.de.
Nadia R Roan
Jay Kant Yadav
Marcus Fändrich
Jan Münch
Institute of Protein Biochemistry · ITUniversität Ulm · DEGladstone Institutes · US

Funding

Characterization of Exosomes From Semen of Uninfected and HIV-Infected MenR21AI122821 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ROAN, NADIA R · 2016 to 2017
$450k
Characterization of Gallic Acid as a Novel HIV Microbicide CandidateR21AI116252 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ROAN, NADIA R · 2015 to 2016
$436k
NIAID NIH HHS R21 AI116252NIAID NIH HHS R21 AI122821
6 · The paper itself

Abstract

Amyloid fibrils are linear polypeptide aggregates with a cross-β structure. These fibrils are best known for their association with neurodegenerative diseases, such as Alzheimer's or Parkinson's, but they may also be used by living organisms as functional units, e.g. in the synthesis of melanin or in the formation of bacterial biofilms. About a decade ago, in a search for semen factors that modulate infection by HIV-1 (a sexually transmitted virus and the causative agent of the acquired immune deficiency syndrome (AIDS)), it was demonstrated that semen harbors amyloid fibrils capable of markedly increasing HIV infection rates. This discovery not only created novel opportunities to prevent sexual HIV-1 transmission but also stimulated research to unravel the natural role of these factors. We discuss here the identification of these intriguing structures, their molecular properties, and their effects on both sexually transmitted diseases and reproductive health. Moreover, we review strategies to antagonize semen amyloid to prevent sexual transmission of viruses.

Indexed as

Amyloidogenic ProteinsAnimalsHIV-1HIV InfectionsHumansImmunity, InnateMaleProtein AggregatesProtein MultimerizationSemenSeminal Plasma ProteinsAmyloidogenic ProteinsProtein AggregatesSeminal Plasma Proteins

Identifiers

PMID29873340
PMCPMC6033663
OpenAlexW2806497774

What OpenQuestion holds

Textmetadata
LicenceTDM
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.