Evidence map›Paper›PMID 26302018›Full record

ArticleJournal of the American Chemical Society2015

Protein-Protein Interactions Mediated by Helical Tertiary Structure Motifs.

Andrew M Watkins, Michael G Wuo, Paramjit S Arora

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Reengineering of a Proteomimetic Pan-Ras Inhibitor into a Ras Degrader.Angewandte Chemie (International ed. in English) · 2025
    Article
  5. Article
  6. Review
  7. Expression of Lanthipeptides in Human Cells.bioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. A Sos proteomimetic as a pan-Ras inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Conformational control in a photoswitchable coiled coil.Chemical communications (Cambridge, England) · 2021
    Article
  16. Article
  17. Article
  18. 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

3 authors.

Andrew M WatkinsDepartment of Chemistry, New York University , New York, New York 10003, United States.
Michael G WuoDepartment of Chemistry, New York University , New York, New York 10003, United States.
Paramjit S AroraDepartment of Chemistry, New York University , New York, New York 10003, United States.

Funding

Biomolecular Recognition with Artificial Alpha-HelicesR01GM073943 · NIGMS · NEW YORK UNIVERSITY · PI ARORA, PARAMJIT S · 2005 to 2018
$4.4M
NIGMS NIH HHS R01 GM073943NIGMS NIH HHS R01GM073943
6 · The paper itself

Abstract

The modulation of protein-protein interactions (PPIs) by means of creating or stabilizing secondary structure conformations is a rapidly growing area of research. Recent success in the inhibition of difficult PPIs by secondary structure mimetics also points to potential limitations, because often, specific cases require tertiary structure mimetics. To streamline protein structure-based inhibitor design, we have previously described the examination of protein complexes in the Protein Data Bank where α-helices or β-strands form critical contacts. Here, we examined coiled coils and helix bundles that mediate complex formation to create a platform for the discovery of potential tertiary structure mimetics. Though there has been extensive analysis of coiled coil motifs, the interactions between pre-formed coiled coils and globular proteins have not been systematically analyzed. This article identifies critical features of these helical interfaces with respect to coiled coil and other helical PPIs. We expect the analysis to prove useful for the rational design of modulators of this fundamental class of protein assemblies.

Indexed as

Protein Structure, TertiaryDimerizationProtein BindingProteinsProteins

Identifiers

PMID26302018
PMCPMC4577960

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.