ArticleNature chemical biology2020
Chain alignment of collagen I deciphered using computationally designed heterotrimers.
Article in Nature chemical biology, 2020. 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, 43 citations in OpenAlex.
- Molecular basis of collagen triple helix recognition by VWF A-like domain two of collagen VII: Implications for interlaced anchoring fibril formation.The Journal of biological chemistry · 2026Article
- Molecular foundations of collagen triple helical assembly: the central role of prolyl-4-hydroxylation.The Biochemical journal · 2026Review
- 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
- β-Turn Mimicking Crosslinking Provides Hyperstability and Fast Folding Kinetics for Short Collagen Triple Helices.Chembiochem : a European journal of chemical biology · 2025Article
- Identification and Structural Characterization of a Novel COL3A1 Gene Duplication in a Family With Vascular Ehlers-Danlos Syndrome.Molecular genetics & genomic medicine · 2025Article
- Deciphering the folding code of collagens.Nature communications · 2025Article
- Extracellular Matrix ModulationCurrent medicinal chemistry · 2025Article
- Versatile Self-Assembly of Triblock Peptides into Stable Collagen Mimetic Heterotrimers.International journal of molecular sciences · 2024Article
- 3D cotton-type anisotropic biomimetic scaffold with low fiber motion electrospun via a sharply inclined array collector for induced osteogenesis.Scientific reports · 2024Article
- Stability of collagen heterotrimer with same charge pattern and different charged residue identities.Biophysical journal · 2023Article
- 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
- Biomimetic Remineralized Three-Dimensional Collagen Bone Matrices with an Enhanced Osteostimulating Effect.Biomimetics (Basel, Switzerland) · 2023Article
- Terminal repeats impact collagen triple-helix stability through hydrogen bonding.Chemical science · 2022Article
- Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy.Biomolecules · 2022Article
- Selective covalent capture of collagen triple helices with a minimal protecting group strategy.Chemical science · 2022Article
- The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature.International journal of molecular sciences · 2022Article
- Collagen's primary structure determines collagen:HSP47 complex stoichiometry.The Journal of biological chemistry · 2021Article
- Collagen's enigmatic, highly conservedProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Multimerin 1 supports platelet function in vivo and binds to specific GPAGPOGPX motifs in fibrillar collagens that enhance platelet adhesion.Journal of thrombosis and haemostasis : JTH · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
The most abundant member of the collagen protein family, collagen I (also known as type I collagen; COL1), is composed of one unique (chain B) and two similar (chain A) polypeptides that self-assemble with one amino acid offset into a heterotrimeric triple helix. Given the offset, chain B can occupy either the leading (BAA), middle (ABA) or trailing (AAB) position of the triple helix, yielding three isomeric biomacromolecules with different protein recognition properties. Despite five decades of intensive research, there is no consensus on the position of chain B in COL1. Here, three triple-helical heterotrimers that each contain a putative von Willebrand factor (VWF) and discoidin domain receptor (DDR) recognition sequence from COL1 were designed with chain B permutated in all three positions. AAB demonstrated a strong preference for both VWF and DDR, and also induced higher levels of cellular DDR phosphorylation. Thus, we resolve this long-standing mystery and show that COL1 adopts an AAB register.
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.