ArticleThe Journal of biological chemistry2010
Microfibril structure masks fibrillin-2 in postnatal tissues.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 50 citations in OpenAlex.
- Sonic hedgehog signaling promotes basal epidermalbioRxiv : the preprint server for biology · 2025Article
- Control of epithelial tissue organization by mRNA localization.Nature communications · 2025Article
- Missense variants ofMolecular genetics and metabolism reports · 2024Article
- Genetic models of fibrillinopathies.Genetics · 2024Review
- Digits in a dish: AnFrontiers in cell and developmental biology · 2023Article
- The fibrillinopathies: New insights with focus on the paradigm of opposing phenotypes for both FBN1 and FBN2.Human mutation · 2022Review
- Article
- Circulating fibrillin fragment concentrations in patients with and without aortic pathology.JVS-vascular science · 2022Article
- Altered Ocular Fibrillin Microfibril Composition in Mice With a Glaucoma-Causing Mutation of Adamts10.Investigative ophthalmology & visual science · 2021Article
- Latent-transforming growth factor beta-binding protein-2 (LTBP-2) is required for longevity but not for development of zonular fibers.Matrix biology : journal of the International Society for Matrix Biology · 2021Article
- The quest for substrates and binding partners: A critical barrier for understanding the role of ADAMTS proteases in musculoskeletal development and disease.Developmental dynamics : an official publication of the American Association of Anatomists · 2021Review
- The ADAMTS/Fibrillin Connection: Insights into the Biological Functions of ADAMTS10 and ADAMTS17 and Their Respective Sister Proteases.Biomolecules · 2020Review
- Adamts17 is involved in skeletogenesis through modulation of BMP-Smad1/5/8 pathway.Cellular and molecular life sciences : CMLS · 2019Article
- Targeted deletion of fibrillin-1 in the mouse eye results in ectopia lentis and other ocular phenotypes associated with Marfan syndrome.Disease models & mechanisms · 2019Article
- Article
- A heart for fibrillin: spatial arrangement in adult wild-type murine myocardial tissue.Histochemistry and cell biology · 2018Article
- A novelClinical case reports · 2018Article
- Design of an elastin-layered dermal regeneration template.Acta biomaterialia · 2017Article
- Unusual life cycle and impact on microfibril assembly of ADAMTS17, a secreted metalloprotease mutated in genetic eye disease.Scientific reports · 2017Article
- Proteomic Analysis of the Bovine and Human Ciliary Zonule.Investigative ophthalmology & visual science · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 6 institutions in 1 country.
Funding
Abstract
Fibrillin microfibrils are polymeric structures present in connective tissues. The importance of fibrillin microfibrils to connective tissue function has been demonstrated by the multiple genetic disorders caused by mutations in fibrillins and in microfibril-associated molecules. However, knowledge of microfibril structure is limited, largely due to their insolubility. Most previous studies have focused on how fibrillin-1 is organized within microfibril polymers. In this study, an immunochemical approach was used to circumvent the insolubility of microfibrils to determine the role of fibrillin-2 in postnatal microfibril structure. Results obtained from studies of wild type and fibrillin-1 null tissues, using monoclonal and polyclonal antibodies with defined epitopes, demonstrated that N-terminal fibrillin-2 epitopes are masked in postnatal microfibrils and can be revealed by enzymatic digestion or by genetic ablation of Fbn1. From these studies, we conclude that fetal fibrillin polymers form an inner core within postnatal microfibrils and that microfibril structure evolves as growth and development proceed into the postnatal period. Furthermore, documentation of a novel cryptic site present in EGF4 in fibrillin-1 underscores the molecular complexity and tissue-specific differences in microfibril structure.
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.