Evidence map›Paper›PMID 24297894›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Protein recognition and selection through conformational and mutually induced fit.

Qian Wang, Pengzhi Zhang, Laurel Hoffman, Swarnendu Tripathi, Dirar Homouz, Yin Liu, M Neal Waxham, Margaret S Cheung

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 55 citations in OpenAlex.

  1. An AlphaFold guided model for the evolution of the CaMKII interactome.bioRxiv : the preprint server for biology · 2025
    Article
  2. Article
  3. Article
  4. Assessing the Role of Calmodulin's Linker Flexibility in Target Binding.International journal of molecular sciences · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Assemblies of calcium/calmodulin-dependent kinase II with actin and their dynamic regulation by calmodulin in dendritic spines.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. A mutually induced conformational fit underlies CaThe Journal of biological chemistry · 2019
    Article
  10. Article
  11. Molecular mechanisms of the interhead coordination by interhead tension in cytoplasmic dyneins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Review
  13. Article
  14. Molecular mechanism of multispecific recognition of Calmodulin through conformational changes.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Opposing Intermolecular Tuning of CaBiophysical journal · 2017
    Article
  16. Article
  17. Article
  18. Review
  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

8 authors at 3 institutions in 2 countries.

Qian WangDepartment of Physics, University of Houston, Houston, TX 77204.
Pengzhi Zhang
Laurel Hoffman
Swarnendu Tripathi
Dirar Homouz
Yin Liu
M Neal Waxham
Margaret S Cheung
University of Houston · USThe University of Texas at Austin · USKhalifa University of Science and Technology · AE

Funding

Principles for Tuning Target Selectivity in Signaling ProteinsR01GM097553 · NIGMS · UNIVERSITY OF WASHINGTON · PI CHEUNG, MARGARET SHUN · 2011 to 2022
$2.7M
NIGMS NIH HHS 1R01GM097553NIGMS NIH HHS R01 GM097553
6 · The paper itself

Abstract

Protein-protein interactions drive most every biological process, but in many instances the domains mediating recognition are disordered. How specificity in binding is attained in the absence of defined structure contrasts with well-established experimental and theoretical work describing ligand binding to protein. The signaling protein calmodulin presents a unique opportunity to investigate mechanisms for target recognition given that it interacts with several hundred different targets. By advancing coarse-grained computer simulations and experimental techniques, mechanistic insights were gained in defining the pathways leading to recognition and in how target selectivity can be achieved at the molecular level. A model requiring mutually induced conformational changes in both calmodulin and target proteins was necessary and broadly informs how proteins can achieve both high affinity and high specificity.

Indexed as

Models, MolecularAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 1CalmodulinMammalsPeptidesProtein BindingProtein ConformationCalcium-Calmodulin-Dependent Protein Kinase Type 1CalmodulinPeptidescalmodulin binding targetcoarse-grained molecular simulationsconformational flexibilityhydrophobic motifstopped-flow fluorescence techniques

Identifiers

PMID24297894
PMCPMC3870683
OpenAlexW1990189688

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.