ArticleBMC biology2012
Protein dynamics and conformational selection in bidirectional signal transduction.
Article in BMC biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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.
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.
Who cites it
33 citing papers in PubMed, 69 citations in OpenAlex.
- A Computational Approach to Characterize the Protein S-Mer Tyrosine Kinase (PROS1-MERTK) Protein-Protein Interaction Dynamics.Cell biochemistry and biophysics · 2025Article
- Accessing Transient Binding Pockets by Protein Engineering and Yeast Surface Display Screening.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Mixed mechanism of conformational selection and induced fit as a molecular recognition process in the calreticulin family of proteins.PLoS computational biology · 2022Article
- Inhibition of Nonfunctional Ras.Cell chemical biology · 2021Review
- Editing Domain Motions Preorganize the Synthetic Active Site of Prolyl-tRNA Synthetase.ACS catalysis · 2020Article
- Probing the Structural Dynamics of theFrontiers in molecular biosciences · 2020Article
- Antagonistic Control of Genetic Circuit Performance for Rapid Analysis of Targeted Enzyme Activity in Living Cells.Frontiers in molecular biosciences · 2020Article
- Network analysis of dynamically important residues in protein structures mediating ligand-binding conformational changes.European biophysics journal : EBJ · 2019Article
- Article
- Homology modeling in a dynamical world.Protein science : a publication of the Protein Society · 2017Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- EphA4-deleted microenvironment regulates cancer development and leukemoid reaction of the isografted 4T1 murine breast cancer via reduction of an IGF1 signal.Cancer medicine · 2016Article
- Using Local States To Drive the Sampling of Global Conformations in Proteins.Journal of chemical theory and computation · 2016Article
- Evolutionary Conserved Positions Define Protein Conformational Diversity.PLoS computational biology · 2016Article
- Article
- CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state.Database : the journal of biological databases and curation · 2016Article
- Oncogenic mutations weaken the interactions that stabilize the p110α-p85α heterodimer in phosphatidylinositol 3-kinase α.The FEBS journal · 2015Article
- cNMA: a framework of encounter complex-based normal mode analysis to model conformational changes in protein interactions.Bioinformatics (Oxford, England) · 2015Article
- Oligomerization and nanocluster organization render specificity.Biological reviews of the Cambridge Philosophical Society · 2015Review
- Information flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations.Frontiers in plant science · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein conformational dynamics simultaneously allow promiscuity and specificity in binding. The multiple conformations of the free EphA4 ligand-binding domain observed in two new EphA4 crystal structures provide a unique insight into the conformational dynamics of EphA4 and its signaling pathways. The heterogeneous ensemble and loop dynamics explain how the EphA4 receptor is able to bind multiple A- and B-ephrin ligands and small molecules via conformational selection, which helps to fine-tune cellular signal response in both receptor and ligand cells.
Identifiers
What OpenQuestion holds
Registered trials
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.