ArticleTissue engineering. Part A2013
Human recombinant type I collagen produced in plants.
Article in Tissue engineering. Part A, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 66 citations in OpenAlex.
- Expression and identification of a novel high-activity recombinant humanized type I collagen SynthCol1 in Pichia pastoris GS115.Applied microbiology and biotechnology · 2026Article
- Versatility of Collagen as a Natural Biopolymer for Biomedical, Food, and Cosmetic Applications.Current protein & peptide science · 2026Review
- Recombinant collagen in regenerative medicine: Expression strategies, structural design, and translational applications.Materials today. Bio · 2025Review
- Advances in lung bioengineering: Where we are, where we need to go, and how to get there.Frontiers in transplantation · 2023Review
- Evaluation of polyglycolic acid as an animal-free biomaterial for three-dimensional culture of human endometrial cells.Clinical and experimental reproductive medicine · 2022Article
- Comparative genomic and biochemical analyses identify a collagen galactosylhydroxylysyl glucosyltransferase from Acanthamoeba polyphaga mimivirus.Scientific reports · 2022Article
- 3D Bioprinting of Engineered Tissue Flaps with Hierarchical Vessel Networks (VesselNet) for Direct Host-To-Implant Perfusion.Advanced materials (Deerfield Beach, Fla.) · 2021Article
- 3D Printing for Bio-Synthetic Biliary Stents.Bioengineering (Basel, Switzerland) · 2019Article
- Surface modification of PVDF using non-mammalian sources of collagen for enhancement of endothelial cell functionality.Journal of materials science. Materials in medicine · 2016Article
- Transdermal Delivery of Functional Collagen Via Polyvinylpyrrolidone Microneedles.Annals of biomedical engineering · 2015Article
- Marine origin collagens and its potential applications.Marine drugs · 2014Review
- Measuring the osmotic water permeability coefficient (Pf) of spherical cells: isolated plant protoplasts as an example.Journal of visualized experiments : JoVE · 2014Article
- Preparation and characterization of monomers to tetramers of a collagen-like domain from Streptococcus pyogenes.Bioengineered · 2014Article
- Mussel-inspired human gelatin nanocoating for creating biologically adhesive surfaces.International journal of nanomedicine · 2014Article
- Collagen Type I: A Versatile Biomaterial.Advances in experimental medicine and biologyReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As a central element of the extracellular matrix, collagen is intimately involved in tissue development, remodeling, and repair and confers high tensile strength to tissues. Numerous medical applications, particularly, wound healing, cell therapy, bone reconstruction, and cosmetic technologies, rely on its supportive and healing qualities. Its synthesis and assembly require a multitude of genes and post-translational modifications, where even minor deviations can be deleterious or even fatal. Historically, collagen was always extracted from animal and human cadaver sources, but bare risk of contamination and allergenicity and was subjected to harsh purification conditions resulting in irreversible modifications impeding its biofunctionality. In parallel, the highly complex and stringent post-translational processing of collagen, prerequisite of its viability and proper functioning, sets significant limitations on recombinant expression systems. A tobacco plant expression platform has been recruited to effectively express human collagen, along with three modifying enzymes, critical to collagen maturation. The plant extracted recombinant human collagen type I forms thermally stable helical structures, fibrillates, and demonstrates bioactivity resembling that of native collagen. Deployment of the highly versatile plant-based biofactory can be leveraged toward mass, rapid, and low-cost production of a wide variety of recombinant proteins. As in the case of collagen, proper planning can bypass plant-related limitations, to yield products structurally and functionally identical to their native counterparts.
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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.