ArticleProtein science : a publication of the Protein Society2002
The EF-hand domain: a globally cooperative structural unit.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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
47 citing papers in PubMed, 116 citations in OpenAlex.
- Calcium Buffering in Astrocytes and Its Relevance for Experimental Data Interpretation and Computational Modeling.Journal of neurochemistry · 2026Review
- Calcium signaling regulates apoptosis-induced proliferation in Drosophila.PLoS biology · 2026Article
- Comprehensive in-silico characterization and expression pattern of calmodulin genes under various abiotic and biotic stresses in Indian mustard (Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Article
- Genome-wide association study and haplotype analysis reveal novel candidate genes for resistance to powdery mildew in soybean.Frontiers in plant science · 2024Article
- The divergent ER-mitochondria encounter structures (ERMES) are conserved in parabasalids but lost in several anaerobic lineages with hydrogenosomes.BMC biology · 2023Article
- Article
- Novel kinetoplastid-specific cAMP binding proteins identified by RNAi screening for cAMP resistance inFrontiers in cellular and infection microbiology · 2023Article
- A competition smFRET assay to study ligand-induced conformational changes of the dengue virus protease.Protein science : a publication of the Protein Society · 2023Article
- Utilizing an artificial intelligence system to build the digital structural proteome of reef-building corals.GigaScience · 2022Article
- The Function and Regulation of SAPCD2 in Physiological and Oncogenic Processes.Journal of Cancer · 2022Review
- Article
- Large Rab GTPases: Novel Membrane Trafficking Regulators with a Calcium Sensor and Functional Domains.International journal of molecular sciences · 2021Review
- Comparative Genomics Reveals 13 Different Isoforms of Mytimycins (A-M) inInternational journal of molecular sciences · 2021Article
- Calmodulin complexes with brain and muscle creatine kinase peptides.Current research in structural biology · 2021Article
- Biochemical Characterization and Crystal Structure of a Novel NADInternational journal of molecular sciences · 2020Article
- Cytosolic CaCold Spring Harbor perspectives in biology · 2020Review
- Article
- Profiles of soluble proteins in chemosensory organs of three members of the afro-tropical Anopheles gambiae complex.Comparative biochemistry and physiology. Part D, Genomics & proteomics · 2017Article
- Binding of transition metals to S100 proteins.Science China. Life sciences · 2016Review
- Kinetic regulation of multi-ligand binding proteins.BMC systems biology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
EF-hand Ca(2+)-binding proteins participate in both modulation of Ca(2+) signals and direct transduction of the ionic signal into downstream biochemical events. The range of biochemical functions of these proteins is correlated with differences in the way in which they respond to the binding of Ca(2+). The EF-hand domains of calbindin D(9k) and calmodulin are homologous, yet they respond to the binding of calcium ions in a drastically different manner. A series of comparative analyses of their structures enabled the development of hypotheses about which residues in these proteins control the calcium-induced changes in conformation. To test our understanding of the relationship between protein sequence and structure, we specifically designed the F36G mutation of the EF-hand protein calbindin D(9k) to alter the packing of helices I and II in the apoprotein. The three-dimensional structure of apo F36G was determined in solution by nuclear magnetic resonance spectroscopy and showed that the design was successful. Surprisingly, significant structural perturbations also were found to extend far from the site of mutation. The observation of such long-range effects provides clear evidence that four-helix EF-hand domains should be treated as a single globally cooperative unit. A hypothetical mechanism for how the long-range effects are transmitted is described. Our results support the concept of energetic and structural coupling of the key residues that are crucial for a protein's fold and function.
Indexed as
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.