ArticleJournal of structural biology2014
Bacterial collagen-like proteins that form triple-helical structures.
Article in Journal of structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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
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Who cites it
57 citing papers in PubMed, 150 citations in OpenAlex.
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- Data storage and retrieval with unnatural proteins expressed via E. coli.Nature communications · 2026Article
- Comparative Genomics of the Endosymbiont Cardinium Causing Reproductive Manipulation in Encarsia Parasitoid Wasps.MicrobiologyOpen · 2025Article
- Recombinant collagen in regenerative medicine: Expression strategies, structural design, and translational applications.Materials today. Bio · 2025Review
- Horizontal transfer of matrix metalloproteinase genes links early animal and microbial evolution.Biology direct · 2025Article
- Around the collagen triple helix: an introduction to studying associated genetic and acquired diseases.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Designed Fibril-Forming Mini-Collagens Engineered to Exhibit up to Two Orders of Magnitude Differences in Rates of Matrix Metalloproteinase I Susceptibility.Biomacromolecules · 2025Article
- Highly printable and multifunctional cell-laden collagen-based bioinks for precise DLP bioprinting and rapid diabetic wound regeneration.Materials today. Bio · 2025Article
- The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans.Nature communications · 2024Article
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- Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.Matrix biology plus · 2024Review
- Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing.Molecules (Basel, Switzerland) · 2023Article
- In-Silico Analysis Highlights the Existence in Members ofMicroorganisms · 2023Article
- Comparative Genomic and Metagenomic Investigations of the Corynebacterium tuberculostearicum Species Complex Reveals Potential Mechanisms Underlying Associations To Skin Health and Disease.Microbiology spectrum · 2023Article
- Regulation of Collagen I and Collagen III in Tissue Injury and Regeneration.Cardiology and cardiovascular medicine · 2023Article
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- Design of synthetic collagens that assemble into supramolecular banded fibers as a functional biomaterial testbed.Nature communications · 2022Article
- Recombinant collagen hydrogels induced by disulfide bonds.Journal of biomedical materials research. Part A · 2022Article
- Discovering design principles of collagen molecular stability using a genetic algorithm, deep learning, and experimental validation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
A large number of collagen-like proteins have been identified in bacteria during the past 10years, principally from analysis of genome databases. These bacterial collagens share the distinctive Gly-Xaa-Yaa repeating amino acid sequence of animal collagens which underlies their unique triple-helical structure. A number of the bacterial collagens have been expressed in Escherichia coli, and they all adopt a triple-helix conformation. Unlike animal collagens, these bacterial proteins do not contain the post-translationally modified amino acid, hydroxyproline, which is known to stabilize the triple-helix structure and may promote self-assembly. Despite the absence of collagen hydroxylation, the triple-helix structures of the bacterial collagens studied exhibit a high thermal stability of 35-39°C, close to that seen for mammalian collagens. These bacterial collagens are readily produced in large quantities by recombinant methods, either in the original amino acid sequence or in genetically manipulated sequences. This new family of recombinant, easy to modify collagens could provide a novel system for investigating structural and functional motifs in animal collagens and could also form the basis of new biomedical materials with designed structural properties and functions.
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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.