Evidence map›Paper›PMID 31879273›Full record

ReviewThe Journal of biological chemistry2020

Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.

Justin M Westerfield, Francisco N Barrera

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

43 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
  2. Article
  3. bioRxiv : the preprint server for biology · 2026
    Article
  4. [Npj imaging · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. A systematic analysis of human hormone receptors.Science China. Life sciences · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Inconspicuous Yet Indispensable: The Coronavirus Spike Transmembrane Domain.International journal of molecular sciences · 2023
    Review
  20. 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

2 authors at 1 institution in 1 country.

Justin M WesterfieldDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996.
Francisco N BarreraDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996. Electronic address: fbarrera@utk.edu.
University of Tennessee at Knoxville · US

Funding

Transmembrane Peptides for Targeting Acidosis - Equipment SupplementR01GM120642 · NIGMS · UNIVERSITY OF TENNESSEE KNOXVILLE · PI BARRERA, FRANCISCO NICOLAS · 2016 to 2020
$1.7M
NIGMS NIH HHS R01 GM120642
6 · The paper itself

Abstract

Single-pass membrane receptors contain extracellular domains that respond to external stimuli and transmit information to intracellular domains through a single transmembrane (TM) α-helix. Because membrane receptors have various roles in homeostasis, signaling malfunctions of these receptors can cause disease. Despite their importance, there is still much to be understood mechanistically about how single-pass receptors are activated. In general, single-pass receptors respond to extracellular stimuli via alterations in their oligomeric state. The details of this process are still the focus of intense study, and several lines of evidence indicate that the TM domain (TMD) of the receptor plays a central role. We discuss three major mechanistic hypotheses for receptor activation: ligand-induced dimerization, ligand-induced rotation, and receptor clustering. Recent observations suggest that receptors can use a combination of these activation mechanisms and that technical limitations can bias interpretation. Short peptides derived from receptor TMDs, which can be identified by screening or rationally developed on the basis of the structure or sequence of their targets, have provided critical insights into receptor function. Here, we explore recent evidence that, depending on the target receptor, TMD peptides cannot only inhibit but also activate target receptors and can accommodate novel, bifunctional designs. Furthermore, we call for more sharing of negative results to inform the TMD peptide field, which is rapidly transforming into a suite of unique tools with the potential for future therapeutics.

Indexed as

Amino Acid SequenceErbB ReceptorsHumansIntegrinsPeptidesProtein ConformationProtein Conformation, alpha-HelicalProtein Interaction MapsProtein MultimerizationReceptors, Antigen, T-CellSignal TransductionEGFR protein, humanErbB ReceptorsIntegrinsPeptidesReceptors, Antigen, T-Cellcell signalingconformational changeepidermal growth factor receptor (EGFR)integrinoligomerizationprotein–protein interactionreceptor tyrosine kinaseT-cell receptor (TCR)transmembrane domaintransmembrane receptorα-helical

Identifiers

PMID31879273
PMCPMC7029107
OpenAlexW2998721770

What Socratic 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 Socratic graph.