Evidence map›Paper›PMID 18611372›Full record

ReviewStructure (London, England : 1993)2008

Protein-protein interactions in the membrane: sequence, structural, and biological motifs.

David T Moore, Bryan W Berger, William F DeGrado

Abstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing 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

106 citing papers in PubMed.

  1. Visualization of membrane-stabilized SorCS2Journal of structural biology: X · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Functional unfolding of the integrin αX transmembrane helix.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Cooperative Membrane Binding of HIV-1 Matrix Proteins.The journal of physical chemistry. B · 2024
    Article
  11. Precursor Reagent Hydrophobicity Affects Membrane Protein Footprinting.Journal of the American Society for Mass Spectrometry · 2023
    Article
  12. Article
  13. The Biogenesis of Multipass Membrane Proteins.Cold Spring Harbor perspectives in biology · 2023
    Review
  14. Formation of extramembraneProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Review
  16. Review
  17. Spiers Memorial Lecture: Analysis andFaraday discussions · 2021
    Article
  18. Article
  19. Review
  20. Elucidation of the molecular interactions that enable stable assembly and structural diversity in multicomponent immune receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article

46 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

3 authors.

David T MooreDepartment of Biochemistry and Molecular Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6059, USA.
Bryan W Berger
William F DeGrado

Funding

DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
NIGMS NIH HHS R01 GM054616
6 · The paper itself

Abstract

Single-span transmembrane (TM) helices have structural and functional roles well beyond serving as mere anchors to tether water-soluble domains in the vicinity of the membrane. They frequently direct the assembly of protein complexes and mediate signal transduction in ways analogous to small modular domains in water-soluble proteins. This review highlights different sequence and structural motifs that direct TM assembly and discusses their roles in diverse biological processes. We believe that TM interactions are potential therapeutic targets, as evidenced by natural proteins that modulate other TM interactions and recent developments in the design of TM-targeting peptides.

Indexed as

Amino Acid MotifsAmino Acid SequenceGenetic Diseases, InbornHumansMembrane ProteinsModels, MolecularMolecular Sequence DataMutationProtein Interaction Domains and MotifsReceptors, ImmunologicMembrane ProteinsReceptors, Immunologic

Identifiers

PMID18611372
PMCPMC3771515

What OpenQuestion holds

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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.