ArticleTrends in chemistry2024
Peptide Crosslinking by a Class of Plant Copper Enzymes.
Article in Trends in chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- Emerging classes of copper enzymes.Current opinion in chemical biology · 2026Review
- When the wrong metal stops the cycle: Dynamics and specificity in plant copper-dependent peptide cyclases.Journal of inorganic biochemistry · 2026Article
- P450 Cyptide Synthase KwwB Catalyzes Trp-C5-Trp-N1 Cross-Linking and Accepts Diverse Precursor Peptides.Organic letters · 2026Article
- Recent Advances in Bioinspired Cu-Directed C-H Hydroxylation Reactions.Accounts of chemical research · 2025Article
- Peptide Recognition Sequence Guides Catalytic Side Chain Cross-Linking of Plant Peptides by Copper-Dependent Cyclases.Journal of the American Chemical Society · 2025Article
- Aromatic side-chain crosslinking in RiPP biosynthesis.Nature chemical biology · 2025Review
- Plant genome mining of burpitides from fused precursor peptides.Methods in enzymology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
BURP domain peptide cyclases, or BpCs (an abbreviation we recommend in this opinion), are an emerging class of copper enzymes which catalyze the oxidative macrocyclization of peptides in plants. A close examination of their novel protein fold, along with the unique dicopper active site that meticulously controls crosslinking within peptides, highlights how nature exploits intricate mechanistic strategies to achieve diverse functionalities. Here, we summarize recent discoveries regarding the sequence, structure, function, and proposed chemistry of BpCs. We also present plausible mechanistic ideas and recommend important structural considerations that could advance investigations and discussions surrounding their reactivity and underlying mechanisms.
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.