ArticleScientific reports2016
Structural insight for chain selection and stagger control in collagen.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 53 citations in OpenAlex.
- Determinants of Chain Selection and Staggering in Heterotrimeric Collagens: A Comprehensive Review of the Structural Data.International journal of molecular sciences · 2025Review
- Molecular network of metabolic reprogramming and precision diagnosis and treatment of hepatocellular carcinoma.Biomarker research · 2025Review
- 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
- Collagen Biosynthesis and Its Molecular Ensemble: What Remains Unexplored.Biochemistry · 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
- An Overview of Seafood Allergens: Structure-Allergenicity Relationship and Allergenicity Elimination Processing Techniques.Foods (Basel, Switzerland) · 2025Review
- Deciphering the folding code of collagens.Nature communications · 2025Article
- Hydrogels for preventing post-endoscopic submucosal dissection stenosis in early esophageal cancer: a comprehensive literature review.Therapeutic advances in gastroenterology · 2025Review
- In silico assessment of biocompatibility and toxicity: molecular docking and dynamics simulation of PMMA-based dental materials for interim prosthetic restorations.Journal of materials science. Materials in medicine · 2024Article
- Unlocking the Potential of Collagenases: Structures, Functions, and Emerging Therapeutic Horizons.Biodesign research · 2024Article
- A recombinant technique for mapping functional sites of heterotrimeric collagen helices: Collagen IV CB3 fragment as a prototype for integrin binding.The Journal of biological chemistry · 2023Article
- Hollow Octadecameric Self-Assembly of Collagen-like Peptides.Journal of the American Chemical Society · 2023Article
- An epitope-enriched immunogen expands responses to a conserved viral site.Cell reports · 2022Article
- A 3D-Printed Polycaprolactone/Marine Collagen Scaffold Reinforced with Carbonated Hydroxyapatite from Fish Bones for Bone Regeneration.Marine drugs · 2022Article
- Selective covalent capture of collagen triple helices with a minimal protecting group strategy.Chemical science · 2022Article
- Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
- Site-Specific Labeling andBiochemistry · 2021Article
- Collagen Binding Proteins of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- New Aspects Towards a Molecular Understanding of the Allicin Immunostimulatory Mechanism via Colec12, MARCO, and SCARB1 Receptors.International journal of molecular sciences · 2019Article
- A cysteine-based molecular code informs collagen C-propeptide assembly.Nature communications · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagen plays a fundamental role in all known metazoans. In collagens three polypeptides form a unique triple-helical structure with a one-residue stagger to fit every third glycine residue in the inner core without disturbing the poly-proline type II helical conformation of each chain. There are homo- and hetero-trimeric types of collagen consisting of one, two or three distinct chains. Thus there must be mechanisms that control composition and stagger during collagen folding. Here, we uncover the structural basis for both chain selection and stagger formation of a collagen molecule. Three distinct chains (α1, α2 and α3) of the non-collagenous domain 2 (NC2) of type IX collagen are assembled to guide triple-helical sequences in the leading, middle and trailing positions. This unique domain opens the door for generating any fragment of collagen in its native composition and stagger.
Indexed as
Identifiers
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.