ArticleThe Journal of biological chemistry2011
ClbP is a prototype of a peptidase subgroup involved in biosynthesis of nonribosomal peptides.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 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
63 citing papers in PubMed, 105 citations in OpenAlex.
- Cellular effects of outer membrane vesicles isolated from pks-positive strains of bacteria.Research square · 2026Article
- From inflammation to fibrosis and cancer: the emerging role of AIEC-derived metabolites in intestinal disease progression.Experimental & molecular medicine · 2026Review
- Microbial dl-Peptidases Enable Predator Defense and Facilitate Structure Elucidation of Complex Natural Products.Journal of the American Chemical Society · 2026Article
- Synthesis and Biological Evaluation of Colibactin Derivatives.ACS chemical biology · 2026Article
- Colibactin produced by a honeybee symbiont defends against pathogens and shapes the gut community.bioRxiv : the preprint server for biology · 2025Article
- Programmable conjugative CRISPR interference targeting genotoxin in the gut.Research square · 2025Article
- Programmable conjugative CRISPR interference targeting genotoxin in the gut.bioRxiv : the preprint server for biology · 2025Article
- Bacterial small molecule metabolites implicated in gastrointestinal cancer development.Nature reviews. Microbiology · 2025Review
- Mucosal adjuvanticity and mucosal booster effect of colibactin-depleted probioticHuman vaccines & immunotherapeutics · 2024Article
- Article
- Putrescine Supplementation Limits the Expansion of pks+ Escherichia coli and Tumor Development in the Colon.Cancer research communications · 2024Article
- Metabolic Interaction Between Host and the Gut Microbiota During High-Fat Diet-Induced Colorectal Cancer.Journal of microbiology (Seoul, Korea) · 2024Review
- Current understandings of colibactin regulation.Microbiology (Reading, England) · 2024Review
- Targeted depletion ofmSystems · 2023Article
- Genotoxins: The Mechanistic Links betweenCancers · 2023Review
- Structure and function of prodrug-activating peptidases.Biochimie · 2023Review
- Review
- Inulin impacts tumorigenesis promotion by colibactin-producingFrontiers in microbiology · 2023Article
- Article
- Delivery, structure, and function of bacterial genotoxins.Virulence · 2022Review
3 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
11 authors at 6 institutions in 1 country.
Funding
Abstract
The pks genomic island of Escherichia coli encodes polyketide (PK) and nonribosomal peptide (NRP) synthases that allow assembly of a putative hybrid PK-NRP compound named colibactin that induces DNA double-strand breaks in eukaryotic cells. The pks-encoded machinery harbors an atypical essential protein, ClbP. ClbP crystal structure and mutagenesis experiments revealed a serine-active site and original structural features compatible with peptidase activity, which was detected by biochemical assays. Ten ClbP homologs were identified in silico in NRP genomic islands of closely and distantly related bacterial species. All tested ClbP homologs were able to complement a clbP-deficient E. coli mutant. ClbP is therefore a prototype of a new subfamily of extracytoplasmic peptidases probably involved in the maturation of NRP compounds. Such peptidases will be powerful tools for the manipulation of NRP biosynthetic pathways.
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.