ArticleThe Journal of general physiology2021
The N2A region of titin has a unique structural configuration.
Article in The Journal of general physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 18 citations in OpenAlex.
- Solution NMR study of the titin I-band IgI domain I82 shows unusual conformational dynamics.Journal of biomolecular NMR · 2026Article
- Mechanically weak and highly dynamic state of mechanosensitive titin Ig domains induced by proline isomerization.Nature communications · 2025Article
- The calcium-binding protein S100A1 binds to titin's N2A insertion sequence in a pH-dependent manner.The Journal of general physiology · 2025Article
- The calcium-binding protein S100A1 binds to titin's N2A insertion sequence in a pH-dependent manner.The Journal of general physiology · 2025Article
- Human calpain-3 and its structural plasticity: dissociation of a homohexamer into dimers on binding titin.bioRxiv : the preprint server for biology · 2024Article
- Molecular insights into titin's A-band.Journal of muscle research and cell motility · 2023Article
- Titin activates myosin filaments in skeletal muscle by switching from an extensible spring to a mechanical rectifier.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Pairwise sequence similarity mapping with PaSiMap: Reclassification of immunoglobulin domains from titin as case study.Computational and structural biotechnology journal · 2022Article
- The titin N2B and N2A regions: biomechanical and metabolic signaling hubs in cross-striated muscles.Biophysical reviews · 2021Review
- Titin N2A Domain and Its Interactions at the Sarcomere.International journal of molecular sciences · 2021Review
- Titin N2A: More than a signaling node?The Journal of general physiology · 2021Article
- Further progress in understanding of myofibrillar function in health and disease.The Journal of general physiology · 2021Article
Corrections and comments
- Commented on by
Authors and funding
7 authors at 4 institutions in 4 countries.
Funding
Abstract
The N2A segment of titin is a main signaling hub in the sarcomeric I-band that recruits various signaling factors and processing enzymes. It has also been proposed to play a role in force production through its Ca2+-regulated association with actin. However, the molecular basis by which N2A performs these functions selectively within the repetitive and extensive titin chain remains poorly understood. Here, we analyze the structure of N2A components and their association with F-actin. Specifically, we characterized the structure of its Ig domains by elucidating the atomic structure of the I81-I83 tandem using x-ray crystallography and computing a homology model for I80. Structural data revealed these domains to present heterogeneous and divergent Ig folds, where I81 and I83 have unique loop structures. Notably, the I81-I83 tandem has a distinct rotational chain arrangement that confers it a unique multi-domain topography. However, we could not identify specific Ca2+-binding sites in these Ig domains, nor evidence of the association of titin N2A components with F-actin in transfected C2C12 myoblasts or C2C12-derived myotubes. In addition, F-actin cosedimentation assays failed to reveal binding to N2A. We conclude that N2A has a unique architecture that predictably supports its selective recruitment of binding partners in signaling, but that its mechanical role through interaction with F-actin awaits validation.
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.