ArticleJournal of molecular biology2010
Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 25 citations in OpenAlex.
- Design Principles and Benefits of Spatially Explicit Models of Myofilament Function.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Nonmuscle Myosin IIA Regulates the Precise Alignment of Hexagonal Eye Lens Epithelial Cells During Fiber Cell Formation and Differentiation.Investigative ophthalmology & visual science · 2023Article
- The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020Review
- Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes.The Journal of cell biology · 2020Article
- Mammalian muscle fibers may be simple as well as slow.The Journal of general physiology · 2019Article
- Fine mapping titin's C-zone: Matching cardiac myosin-binding protein C stripes with titin's super-repeats.Journal of molecular and cellular cardiology · 2019Article
- Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The sarcomeric M-region: a molecular command center for diverse cellular processes.BioMed research international · 2015Review
- The intriguing dual lattices of the Myosin filaments in vertebrate striated muscles: evolution and advantage.Biology · 2014Review
- Molecular basis of the mechanical hierarchy in myomesin dimers for sarcomere integrity.Biophysical journal · 2014Article
- Article
- Three-dimensional structure of the human myosin thick filament: clinical implications.Global cardiology science & practice · 2013Review
- Superhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties.PLoS biology · 2012Article
- Quasiperiodic distribution of rigor cross-bridges along a reconstituted thin filament in a skeletal myofibril.Biophysical journal · 2011Article
- Modeling of supramolecular centrosymmetry effect on sarcomeric SHG intensity pattern of skeletal muscles.Biophysical journal · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 4 institutions in 2 countries.
Funding
Abstract
The rods of anti-parallel myosin molecules overlap at the centre of bipolar myosin filaments to produce an M-region (bare zone) that is free of myosin heads. Beyond the M-region edges, myosin molecules aggregate in a parallel fashion to yield the bridge regions of the myosin filaments. Adjacent myosin filaments in striated muscle A-bands are cross-linked by the M-band. Vertebrate striated muscle myosin filaments have a 3-fold rotational symmetry around their long axes. In addition, at the centre of the M-region, there are three 2-fold axes perpendicular to the filament long axis, giving the whole filament dihedral 32-point group symmetry. Here we describe the three-dimensional structure obtained by a single-particle analysis of the M-region of myosin filaments from goldfish skeletal muscle under relaxing conditions and as viewed in negative stain. This is the first single-particle reconstruction of isolated M-regions. The resulting three-dimensional reconstruction reveals details to about 55 Å resolution of the density distribution in the five main nonmyosin densities in the M-band (M6', M4', M1, M4 and M6) and in the myosin head crowns (P1, P2 and P3) at the M-region edges. The outermost crowns in the reconstruction were identified specifically by their close similarity to the corresponding crown levels in our previously published bridge region reconstructions. The packing of myosin molecules into the M-region structure is discussed, and some unidentified densities are highlighted.
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.