ArticleLife (Basel, Switzerland)2021
Studying GGDEF Domain in the Act: Minimize Conformational Frustration to Prevent Artefacts.
Article in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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Who cites it
6 citing papers in PubMed.
- The versatility of the CHASE domain in one-component systems of c-di-GMP signal transduction fromJournal of bacteriology · 2026Article
- Spatio-genetically coordinated TPR domain-containing proteins modulate c-di-GMP signaling in Vibrio vulnificus.PLoS pathogens · 2025Article
- The GGDEF protein Dgc2 suppresses both motility and biofilm formation in the filamentous cyanobacteriumMicrobiology spectrum · 2023Article
- Illuminating the inner workings of a natural protein switch: Blue-light sensing in LOV-activated diguanylate cyclases.Science advances · 2023Article
- Characterisation of sequence-structure-function space in sensor-effector integrators of phytochrome-regulated diguanylate cyclases.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Sensing the Messenger: Potential Roles of Cyclic-di-GMP in Rickettsial Pathogenesis.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
GGDEF-containing proteins respond to different environmental cues to finely modulate cyclic diguanylate (c-di-GMP) levels in time and space, making the allosteric control a distinctive trait of the corresponding proteins. The diguanylate cyclase mechanism is emblematic of this control: two GGDEF domains, each binding one GTP molecule, must dimerize to enter catalysis and yield c-di-GMP. The need for dimerization makes the GGDEF domain an ideal conformational switch in multidomain proteins. A re-evaluation of the kinetic profile of previously characterized GGDEF domains indicated that they are also able to convert GTP to GMP: this unexpected reactivity occurs when conformational issues hamper the cyclase activity. These results create new questions regarding the characterization and engineering of these proteins for in solution or structural studies.
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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.