ArticleBiomacromolecules2010
Expanding the family of collagen proteins: recombinant bacterial collagens of varying composition form triple-helices of similar stability.
Article in Biomacromolecules, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 64 citations in OpenAlex.
- Data storage and retrieval with unnatural proteins expressed via E. coli.Nature communications · 2026Article
- Recombinant collagen in regenerative medicine: Expression strategies, structural design, and translational applications.Materials today. Bio · 2025Review
- Ectopical expression of bacterial collagen-like protein supports its role as adhesin in host-parasite coevolution.Royal Society open science · 2024Article
- Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.Matrix biology plus · 2024Review
- Genomic and panproteomic analysis of the development of infant immune responses to antigenically-diverse pneumococci.Nature communications · 2024Article
- Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
- A Rare, VirulentPHAGE (New Rochelle, N.Y.) · 2020Article
- Role for Cell-Surface Collagen ofACS infectious diseases · 2020Article
- Synthesis and Application of Collagens for Assembling a Corneal Implant.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Expression and Purification of Collagen-Like Proteins of Group A Streptococcus.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Polymorphisms of a Collagen-Like Adhesin Contributes toFrontiers in microbiology · 2019Article
- Surface-exposed loops and an acidic patch in the Scl1 protein of group AThe Journal of biological chemistry · 2018Article
- Collagen-like proteins of pathogenic streptococci.Molecular microbiology · 2017Review
- Collagen cross-linking: insights on the evolution of metazoan extracellular matrix.Scientific reports · 2016Article
- Recombinant Collagen Engineered to Bind to Discoidin Domain Receptor Functions as a Receptor Inhibitor.The Journal of biological chemistry · 2016Article
- Article
- Bacterial collagen-like proteins that form triple-helical structures.Journal of structural biology · 2014Article
- A simple cost-effective methodology for large-scale purification of recombinant non-animal collagens.Applied microbiology and biotechnology · 2014Article
- Circular permutation directs orthogonal assembly in complex collagen peptide mixtures.The Journal of biological chemistry · 2013Article
- A new class of animal collagen masquerading as an insect silk.Scientific reports · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The presence of the (Gly-Xaa-Yaa)(n) open reading frames in different bacteria predicts the existence of an expanded family of collagen-like proteins. To further explore the triple-helix motif and stabilization mechanisms in the absence of hydroxyproline (Hyp), predicted novel collagen-like proteins from Gram-positive and -negative bacteria were expressed in Escherichia coli and characterized. Soluble proteins capable of successful folding and in vitro refolding were observed for collagen proteins from Methylobacterium sp 4-46, Rhodopseudomonas palustris and Solibacter usitatus . In contrast, all protein constructs from Clostridium perfringens were found predominantly in inclusion bodies. However, attachment of a heterologous N-terminal or C-terminal noncollagenous folding domain induced the Clostridium perfringens collagen domain to fold and become soluble. The soluble constructs from different bacteria had typical collagen triple-helical features and showed surprisingly similar thermal stabilities despite diverse amino acid compositions. These collagen-like proteins provide a resource for the development of biomaterials with new properties.
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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.