Evidence map›Paper›PMID 25059657›Full record

ArticleThe Journal of biological chemistry2014

Harnessing the unique structural properties of isolated α-helices.

Carter J Swanson, Sivaraj Sivaramakrishnan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.4field-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

45 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. "Design principles of a membrane-spanning ubiquitin ligase".bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. cAMP signaling: a remarkably regional affair.Trends in biochemical sciences · 2024
    Review
  9. Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Resource for FRET-Based Biosensor Optimization.Frontiers in cell and developmental biology · 2022
    Review
  16. Article
  17. Article
  18. β2-adrenoceptor ligand efficacy is tuned by a two-stage interaction with the Gαs C terminus.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  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 at 1 institution in 1 country.

Carter J SwansonFrom the Departments of Biophysics.
Sivaraj SivaramakrishnanFrom the Departments of Biophysics, Cell and Developmental Biology, and Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109 sivaraj@umich.edu.
University of Michigan–Ann Arbor · US

Funding

The kinase toolbox: Mapping the spatial and temporal regulation of cell signalingDP2CA186752 · NCI · UNIVERSITY OF MINNESOTA · PI SIVARAMAKRISHNAN, SIVARAJ · 2013 to 2013
$2.3M
Probing molecular mechanisms of GPCR functional selectivity in live cellsR01GM105646 · NIGMS · UNIVERSITY OF MINNESOTA · PI SIVARAMAKRISHNAN, SIVARAJ · 2014 to 2017
$1.1M
NCI NIH HHS 1DP2 CA186752-01NCI NIH HHS DP2 CA186752NIGMS NIH HHS 1-R01-GM-105646-01-A1NIGMS NIH HHS R01 GM105646
6 · The paper itself

Abstract

The α-helix is a ubiquitous secondary structural element that is almost exclusively observed in proteins when stabilized by tertiary or quaternary interactions. However, beginning with the unexpected observations of α-helix formation in the isolated C-peptide in ribonuclease A, there is growing evidence that a significant percentage (0.2%) of all proteins contain isolated stable single α-helical domains (SAH). These SAH domains provide unique structural features essential for normal protein function. A subset of SAH domains contain a characteristic ER/K motif, composed of a repeating sequence of ∼4 consecutive glutamic acids followed by ∼4 consecutive basic arginine or lysine (R/K) residues. The ER/K α-helix, also termed the ER/K linker, has been extensively characterized in the context of the myosin family of molecular motors and is emerging as a versatile structural element for protein and cellular engineering applications. Here, we review the structure and function of SAH domains, as well as the tools to identify them in natural proteins. We conclude with a discussion of recent studies that have successfully used the modular ER/K linker for engineering chimeric myosin proteins with altered mechanical properties, as well as synthetic polypeptides that can be used to monitor and systematically modulate protein interactions within cells.

Indexed as

Protein Structure, SecondaryAmino Acid MotifsArginineCircular DichroismC-PeptideHumansLysineProtein Interaction Domains and MotifsProtein Structure, TertiaryRibonuclease, PancreaticStructure-Activity RelationshipArginineC-PeptideLysineRibonuclease, PancreaticBiosensorCoiled-coilER/K Alpha-HelixER/K LinkerFluorescence Resonance Energy Transfer (FRET)MyosinProtein-Protein InteractionProtein StructureSingle Alpha-helical Domain (SAH)

Identifiers

PMID25059657
PMCPMC4162150
OpenAlexW2029758652

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.