ArticleThe Journal of biological chemistry2009
A straight path to circular proteins.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 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
64 citing papers in PubMed.
- Phosphoglycerate Kinase Can Adopt Topologically Misfolded Forms That Are More Stable Than Its Native State.Journal of the American Chemical Society · 2026Article
- Peptide and Protein Cyclization by a Promiscuous Graspetide Synthetase.ACS central science · 2025Article
- Coiled Coil Peptide Tiles (CCPTs): Expanding the Peptide Building Block Design with Multivalent Peptide Macrocycles.Journal of the American Chemical Society · 2024Article
- Folds from fold: Exploring topological isoforms of a single-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Efficient production of fluorophore-labeled CC chemokines for biophysical studies using recombinant enterokinase and recombinant sortase.Biopolymers · 2024Article
- A single-domain protein catenane of dihydrofolate reductase.National science review · 2023Article
- A single-domain green fluorescent protein catenane.Nature communications · 2023Article
- Discovery and Characteristics of a Novel Antitumor Cyclopeptide Derived from Shark.Bioengineering (Basel, Switzerland) · 2023Article
- Orthogonal Crosslinking: A Strategy to Generate Novel Protein Topology and Function.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Structural basis for proenzyme maturation, substrate recognition, and ligation by a hyperactive peptide asparaginyl ligase.The Plant cell · 2022Article
- Peptide/protein-based macrocycles: from biological synthesis to biomedical applications.RSC chemical biology · 2022Review
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- Enzymatic C-to-C Protein Ligation.Angewandte Chemie (International ed. in English) · 2022Article
- Targeted substrate loop insertion by VCP/p97 during PP1 complex disassembly.Nature structural & molecular biology · 2021Article
- Protein Macrocyclization for Tertiary Structure Stabilization.Chembiochem : a European journal of chemical biology · 2021Review
- Asparaginyl endopeptidases: enzymology, applications and limitations.Organic & biomolecular chemistry · 2021Review
- Approaches for peptide and protein cyclisation.Organic & biomolecular chemistry · 2021Review
- Stability Enhancement of a Dimeric HER2-Specific Affibody Molecule through Sortase A-Catalyzed Head-to-Tail Cyclization.Molecules (Basel, Switzerland) · 2021Article
- Article
- Yeast-based bioproduction of disulfide-rich peptides and their cyclization via asparaginyl endopeptidases.Nature protocols · 2021Article
4 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
6 authors.
Funding
Abstract
Folding and stability are parameters that control protein behavior. The possibility of conferring additional stability on proteins has implications for their use in vivo and for their structural analysis in the laboratory. Cyclic polypeptides ranging in size from 14 to 78 amino acids occur naturally and often show enhanced resistance toward denaturation and proteolysis when compared with their linear counterparts. Native chemical ligation and intein-based methods allow production of circular derivatives of larger proteins, resulting in improved stability and refolding properties. Here we show that circular proteins can be made reversibly with excellent efficiency by means of a sortase-catalyzed cyclization reaction, requiring only minimal modification of the protein to be circularized.
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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.