ReviewCurrent opinion in chemical biology2026
GTP hydrolysis-powered zinc metallochaperones as molecular switches.
Review in Current opinion in chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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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0 citing papers in PubMed.
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Authors and funding
4 authors.
Funding
Abstract
Late d-block first row transition metals from manganese to copper and zinc are present in all cells at high abundance and typically cofactor approximately one-third of the proteome. The integrity of this metalloproteome must be functionally resilient to changes in metal bioavailability induced by metal toxicity and metal scarcity, such that cellular processes dependent on these metalloenzymes are maintained. An emerging hypothesis is that the cellular response to zinc scarcity involves the expression of one or more GTP hydrolysis-dependent zinc metallochaperones, which are proposed to allocate zinc to specific downstream "clients". Here we critically evaluate the available evidence in support of this hypothesis with a focus on Cluster of Orthologous Groups 0523 (COG0523) superfamily of nucleotide-dependent metallochaperones. These enzymes are found in all kingdoms and yet the identification of biochemically validated client proteins continues to lag. Approaches to close this knowledge gap are discussed.
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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 Socratic graph.