Evidence map›Paper›PMID 28194151›Full record

ReviewFrontiers in immunology2017

Structure and Dynamics of Antigenic Peptides in Complex with TAP.

Elisa Lehnert, Robert Tampé

Abstract readReview
In one paragraph

Review in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Aberrant SUMOylation Restricts the Targetable Cancer Immunopeptidome.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Biotechnologia · 2025
    Article
  9. Article
  10. Review
  11. Review
  12. Prediction of TAP Transport of Peptides with Variable Length Using TAPREG.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. The Structure and Mechanism of Drug Transporters.Methods in molecular biology (Clifton, N.J.) · 2021
    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

2 authors.

Elisa LehnertInstitute of Biochemistry, Biocenter, Goethe University Frankfurt , Frankfurt , Germany.
Robert TampéInstitute of Biochemistry, Biocenter, Goethe University Frankfurt , Frankfurt , Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transporter associated with antigen processing (TAP) selectively translocates antigenic peptides into the endoplasmic reticulum. Loading onto major histocompatibility complex class I molecules and proofreading of these bound epitopes are orchestrated within the macromolecular peptide-loading complex, which assembles on TAP. This heterodimeric ABC-binding cassette (ABC) transport complex is therefore a major component in the adaptive immune response against virally or malignantly transformed cells. Its pivotal role predestines TAP as a target for infectious diseases and malignant disorders. The development of therapies or drugs therefore requires a detailed comprehension of structure and function of this ABC transporter, but our knowledge about various aspects is still insufficient. This review highlights recent achievements on the structure and dynamics of antigenic peptides in complex with TAP. Understanding the binding mode of antigenic peptides in the TAP complex will crucially impact rational design of inhibitors, drug development, or vaccination strategies.

Indexed as

ABC transporterantigen processingligand bindingmembrane proteinspeptide-loading complexsubstrate-binding site

Identifiers

PMID28194151
PMCPMC5277011

What OpenQuestion holds

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Registered trials

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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.