ArticleNature chemical biology2008
Identification of a copper-binding metallothionein in pathogenic mycobacteria.
Article in Nature chemical biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 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
109 citing papers in PubMed, 208 citations in OpenAlex.
- A copper uptake ABC transport system is essential forEmerging microbes & infections · 2026Article
- Identification and characterization of TrxA: a novel bacterial thioredoxin-metallothionein chimera.Applied microbiology and biotechnology · 2026Article
- Structural and functional characterization of VapBC52 toxin-antitoxin system from Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Review
- VapC36-mediated intrinsic stress adaption is required for copper tolerance and pathogenesis ofScience advances · 2026Article
- Pseudopaline-mediated zinc uptake byInfection and immunity · 2026Article
- Metal-Coordination Specificity and Structural Dynamics of C. elegans Metallothionein I: Insights From 3D Modeling and MD Simulations.Proteins · 2026Article
- Kupyaphores─Self-Assembling Diisocyanolipopeptide ZnJournal of the American Chemical Society · 2025Article
- Review
- Metals in Motion: Understanding Labile Metal Pools in Bacteria.Biochemistry · 2025Review
- Iron, Copper, and Zinc Homeostasis in the Battle between Macrophage andCurrent medicinal chemistry · 2025Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Bacterial metallothionein, PmtA, a novel stress protein found on the bacterial surface ofmSphere · 2024Article
- The efflux pumps Rv1877 and Rv0191 play differential roles in the protection ofFrontiers in microbiology · 2024Article
- Differentiated Zn(II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn.Metallomics : integrated biometal science · 2023Article
- Aldehyde accumulation inmBio · 2023Article
- Article
- Important Structural Features of Thiolate-Rich Four-Helix Bundles for Cu(I) Uptake and Removal.Inorganic chemistry · 2023Article
- Nutritional immunity: the battle for nutrient metals at the host-pathogen interface.Nature reviews. Microbiology · 2022Review
- Diisonitrile Lipopeptides Mediate Resistance to Copper Starvation in Pathogenic Mycobacteria.mBio · 2022Article
49 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
A screen of a genomic library from Mycobacterium tuberculosis (Mtb) identified a small, unannotated open reading frame (MT0196) that encodes a 4.9-kDa, cysteine-rich protein. Despite extensive nucleotide divergence, the amino acid sequence is highly conserved among mycobacteria that are pathogenic in vertebrate hosts. We synthesized the protein and found that it preferentially binds up to six Cu(I) ions in a solvent-shielded core. Copper, cadmium and compounds that generate nitric oxide or superoxide induced the gene's expression in Mtb up to 1,000-fold above normal expression. The native protein bound copper within Mtb and partially protected Mtb from copper toxicity. We propose that the product of the MT0196 gene be named mycobacterial metallothionein (MymT). To our knowledge, MymT is the first metallothionein of a Gram-positive bacterium with a demonstrated 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.