ArticleThe Journal of biological chemistry2016
Recombinant Collagen Engineered to Bind to Discoidin Domain Receptor Functions as a Receptor Inhibitor.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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.
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Who cites it
15 citing papers in PubMed, 38 citations in OpenAlex.
- Recombinant collagen in regenerative medicine: Expression strategies, structural design, and translational applications.Materials today. Bio · 2025Review
- Innovations and challenges in collagen and gelatin production through precision fermentation.World journal of microbiology & biotechnology · 2025Review
- Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
- The Collagen Receptor Discoidin Domain Receptor 1b Enhances Integrin β1-Mediated Cell Migration by Interacting With Talin and Promoting Rac1 Activation.Frontiers in cell and developmental biology · 2022Article
- Ablation of collagen VI leads to the release of platelets with altered function.Blood advances · 2021Article
- Collagen Mimetic Peptides.Bioengineering (Basel, Switzerland) · 2021Review
- Three Decades of Research on Recombinant Collagens: Reinventing the Wheel or Developing New Biomedical Products?Bioengineering (Basel, Switzerland) · 2020Review
- Article
- Discoidin domain receptors: Micro insights into macro assemblies.Biochimica et biophysica acta. Molecular cell research · 2019Review
- Role of prolyl hydroxylation in the molecular interactions of collagens.Essays in biochemistry · 2019Review
- The predominant roles of the sequence periodicity in the self-assembly of collagen-mimetic mini-fibrils.Protein science : a publication of the Protein Society · 2019Article
- Collagen Gly missense mutations: Effect of residue identity on collagen structure and integrin binding.Journal of structural biology · 2018Article
- Collagen induces activation of DDR1 through lateral dimer association and phosphorylation between dimers.eLife · 2017Article
- Discoidin domain receptor 1 kinase activity is required for regulating collagen IV synthesis.Matrix biology : journal of the International Society for Matrix Biology · 2017Article
- Mapping the Effect of Gly Mutations in Collagen on α2β1 Integrin Binding.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 4 countries.
Funding
Abstract
A bacterial collagen-like protein Scl2 has been developed as a recombinant collagen model system to host human collagen ligand-binding sequences, with the goal of generating biomaterials with selective collagen bioactivities. Defined binding sites in human collagen for integrins, fibronectin, heparin, and MMP-1 have been introduced into the triple-helical domain of the bacterial collagen and led to the expected biological activities. The modular insertion of activities is extended here to the discoidin domain receptors (DDRs), which are collagen-activated receptor tyrosine kinases. Insertion of the DDR-binding sequence from human collagen III into bacterial collagen led to specific receptor binding. However, even at the highest testable concentrations, the construct was unable to stimulate DDR autophosphorylation. The recombinant collagen expressed in Escherichia coli does not contain hydroxyproline (Hyp), and complementary synthetic peptide studies showed that replacement of Hyp by Pro at the critical Gly-Val-Met-Gly-Phe-Hyp position decreased the DDR-binding affinity and consequently required a higher concentration for the induction of receptor activation. The ability of the recombinant bacterial collagen to bind the DDRs without inducing kinase activation suggested it could interfere with the interactions between animal collagen and the DDRs, and such an inhibitory role was confirmed in vitro and with a cell migration assay. This study illustrates that recombinant collagen can complement synthetic peptides in investigating structure-activity relationships, and this system has the potential for the introduction or inhibition of specific biological activities.
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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.