Evidence map›Paper›PMID 25110191›Full record

ReviewNature reviews. Microbiology2014

Discovery of modulators of HIV-1 infection from the human peptidome.

Jan Münch, Ludger Ständker, Wolf-Georg Forssmann, Frank Kirchhoff

Abstract readReview
In one paragraph

Review in Nature reviews. Microbiology, 2014. 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
–field-weighted citation impact
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.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Origins, Technological Advancement, and Applications of Peptidomics.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  6. Peptidomics.Nature reviews. Methods primers · 2023
    Article
  7. Article
  8. Article
  9. Natural cystatin C fragments inhibit GPR15-mediated HIV and SIV infection without interfering with GPR15L signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. [PSB0739 inhibits formation of semen-derived amyloid fibril].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2018
    Article
  15. Structure, function and antagonism of semen amyloids.Chemical communications (Cambridge, England) · 2018
    Review
  16. Review
  17. Article
  18. [Lactic acid inhibits the formation of semen-derived amyloid fibrils].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2017
    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

4 authors.

Jan Münch1] Institute of Molecular Virology, Ulm University Medical Center, 89081 Ulm, Germany. [2] Ulm Peptide Pharmaceuticals, Ulm University, 89081 Ulm, Germany.
Ludger Ständker1] Institute of Molecular Virology, Ulm University Medical Center, 89081 Ulm, Germany. [2] Ulm Peptide Pharmaceuticals, Ulm University, 89081 Ulm, Germany.
Wolf-Georg Forssmann1] Institute of Molecular Virology, Ulm University Medical Center, 89081 Ulm, Germany. [2] Pharis Biotec GmbH, 30625 Hannover, Germany.
Frank Kirchhoff1] Institute of Molecular Virology, Ulm University Medical Center, 89081 Ulm, Germany. [2] Ulm Peptide Pharmaceuticals, Ulm University, 89081 Ulm, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Almost all human proteins are subject to proteolytic degradation, which produces a broad range of peptides that have highly specific and sometimes unexpected functions. Peptide libraries that have been generated from human bodily fluids or tissues are a rich but mostly unexplored source of bioactive compounds that could be used to develop antimicrobial and immunomodulatory therapeutic agents. In this Innovation article, we describe the discovery, optimization and application of endogenous bioactive peptides from human-derived peptide libraries, with a particular focus on the isolation of endogenous inhibitors and promoters of HIV-1 infection.

Indexed as

Host-Pathogen InteractionsAntimicrobial Cationic PeptidesHIV-1HIV InfectionsHumansImmunologic FactorsPeptidesProteomeAntimicrobial Cationic PeptidesImmunologic FactorsPeptidesProteome

Identifiers

PMID25110191
PMCPMC7097597

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.